Nitric Oxide in Macrophage Immunometabolism: Hiding in Plain Sight
Open accessAbstract
Nitric Oxide (NO) is a soluble endogenous gas with various biological functions like signaling, and working as an effector molecule or metabolic regulator. In response to inflammatory signals, immune myeloid cells, like macrophages, increase production of cytokines and NO, which is important for pathogen killing. Under these proinflammatory circumstances, called “M1”, macrophages undergo a series of metabolic changes including rewiring of their tricarboxylic acid (TCA) cycle. Here, we review findings indicating that NO, through its interaction with heme and non-heme metal containing proteins, together with components of the electron transport chain, functions not only as a regulator of cell respiration, but also a modulator of intracellular cell metabolism. Moreover, diverse effects of NO and NO-derived reactive nitrogen species (RNS) involve precise interactions with different targets depending on concentration, temporal, and spatial restrictions. Although the role of NO in macrophage reprogramming has been in evidence for some time, current models have largely minimized its importance. It has, therefore, been hiding in plain sight. A review of the chemical properties of NO, past biochemical studies, and recent publications, necessitates that mechanisms of macrophage TCA reprogramming during stimulation must be re-imagined and re-interpreted as mechanistic results of NO exposure. The revised model of metabolic rewiring we describe here incorporates many early findings regarding NO biochemistry and brings NO out of hiding and to the forefront of macrophages immunometabolism.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The role of •NO in macrophage reprogramming has been known for a long time, but current models greatly underestimate its importance.
“The role of •NO in macrophage reprogramming has been known for a long time, but current models greatly underestimate its importance [125].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [125]
The •NO/ROS balance is important during the transition from Th1 to Th2.
“The •NO/ROS balance is also important during the transition from Th1 to Th2 [125,126].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [125]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Nitric oxide: physiology, pathophysiology, and pharmacology.
Moncada, S., Palmer, R. M., & Higgs, E. A. (1991) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06663-3 · Cited by 15,525 · see citing works
Furchgott, R. F., & Zawadzki, J. V. (1980) · Nature · doi:10.1038/288373a0 · Cited by 12,064 · cited 1× · see citing works
“Early descriptions of an Endothelium-derived relaxing factor (EDRF) capable of inducing vasodilation began in 1980 [1].”
BackgroundAnalysis of nitrate, nitrite, and [15N]nitrate in biological fluids
Green, L. C., Wagner, D. A., Glogowski, J. A., Skipper, P. L., Wishnok, J. S., & Tannenbaum, S. R. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90118-x · Cited by 12,061 · see citing works
Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide.
Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., & Chaudhuri, G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.9265 · Cited by 5,074 · see citing works
NITRIC OXIDE AND MACROPHAGE FUNCTION
MacMicking, J. D., Xie, Q. W., & Nathan, C. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.323 · Cited by 4,184 · cited 1× · see citing works
“nitrogen intermediates through NOS2 [135], and increased production of effectors such as cationic peptides, lysosomal hydrolases, and metabolic inhibitors [136], including itaconate (antibacterial) [107] and 25-hydroxycholesterol (antiviral) [137], all contribute to macrophage antimicrobial responses.”
BackgroundSuccinate is an inflammatory signal that induces IL-1β through HIF-1α
Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · cited 23× · see citing works
“Both groups have reported elevated IL-1β in Nos2−/− macrophages likely due to the lack of NO-mediated nitrosation of the inflammasome complex [179–181].”
BackgroundInfluentialKim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905 · see citing works
Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS
Chouchani, E. T., Pell, V. R., Gaude, E., Aksentijević, D., Sundier, S. Y., Robb, E. L., Logan, A., Nadtochiy, S. M., Ord, E. N. J., Smith, A. C., et al. (2014) · Nature · doi:10.1038/nature13909 · Cited by 2,907 · cited 1× · see citing works
“A similar mechanism has been proposed for the involvement of succinate in damage associated with reperfusion injury in the heart [133].”
BackgroundPeroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,499 · see citing works
Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291 · cited 2× · see citing works
“As a fuel for Complex II, succinate can drive ROS production in macrophages and, therefore, be critical in antibacterial function [131], and via reverse electron transport, succinate can fuel ROS production by Complex I.”
BackgroundHIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., & Denko, N. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.012 · Cited by 2,267 · cited 5× · see citing works
“These findings led to the suggestion that in polarized macrophages, pseudo-hypoxia, caused by reduction in α-KG /succinate ratios and suppression of dioxygenase activity [113,114], leads to HIF1α stabilization and expression of Pyruvate Dehydrogenase Kinase 1 (Pdk1) that phosphorylates Pyruvate Dehydrogenase (PDH), re…”
BackgroundInfluentialSuccinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase
Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108 · cited 2× · see citing works
“These findings led to the suggestion that in polarized macrophages, pseudo-hypoxia, caused by reduction in α-KG /succinate ratios and suppression of dioxygenase activity [113,114], leads to HIF1α stabilization and expression of Pyruvate Dehydrogenase Kinase 1 (Pdk1) that phosphorylates Pyruvate Dehydrogenase (PDH), re…”
BackgroundJha, A. K., Huang, S. C.-C., Sergushichev, A., Lampropoulou, V., Ivanova, Y., Loginicheva, E., Chmielewski, K., Stewart, K. M., Ashall, J., Everts, B., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.005 · Cited by 2,066 · cited 13× · see citing works
“In brief, this interrupted TCA cycle is thought to drive the accumulation of key intermediates of metabolism such as citrate, itaconate, and succinate [106,107] that support effector functions.”
BackgroundInfluentialNitric oxide: A cytotoxic activated macrophage effector molecule
Hibbs, J. B., Taintor, R. R., Vavrin, Z., & Rachlin, E. M. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80015-9 · Cited by 2,030 · cited 1× · see citing works
“In 1988–89, Hibbs as well as Stuehr and Nathan [8,9] connected the dots by showing NO to be the key effector molecule used by activated murine macrophages to kill tumors.”
BackgroundMitochondrial membrane potential
Zorova, L. D., Popkov, V. A., Plotnikov, E. Y., Silachev, D. N., Pevzner, I. B., Jankauskas, S. S., Babenko, V. A., Zorov, S. D., Balakireva, A. V., Juhaszova, M., et al. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2017.07.009 · Cited by 2,015 · cited 1× · see citing works
“They align perfectly with a model where the hyperpolarization of mitochondrial membranes, the condition where the mitochondrial inner membrane becomes more negative on the matrix side [148,149], is induced by NO initially blocking Complex IV and favoring hydrolysis of glycolytically-derived ATP [80,150] (Figure 2a).”
BackgroundItaconate is an anti-inflammatory metabolite that activates Nrf2 via alkylation of KEAP1
Mills, E. L., Ryan, D. G., Prag, H. A., Dikovskaya, D., Menon, D., Zaslona, Z., Jedrychowski, M. P., Costa, A. S. H., Higgins, M., Hams, E., et al. (2018) · Nature · doi:10.1038/nature25986 · Cited by 1,885 · see citing works
Nrf2 suppresses macrophage inflammatory response by blocking proinflammatory cytokine transcription
Kobayashi, E. H., Suzuki, T., Funayama, R., Nagashima, T., Hayashi, M., Sekine, H., Tanaka, N., Moriguchi, T., Motohashi, H., Nakayama, K., et al. (2016) · Nature Communications · doi:10.1038/ncomms11624 · Cited by 1,878 · cited 1× · see citing works
“Our recent description of a NOS2-dependent NRF2 gene signature in murine macrophages, together with NRF2′s known ability to attenuate inflammation [177], suggests that NO reprograms metabolism while supporting the antioxidant response, all at the expense of full inflammatory potential.”
BackgroundMetabolic reprogramming in macrophages and dendritic cells in innate immunity
Kelly, B., & O'Neill, L. A. (2015) · Cell Research · doi:10.1038/cr.2015.68 · Cited by 1,876 · cited 2× · see citing works
“Others have referred to evidence that many metabolic enzymes could be s-nitrosated by NO [143] and assumed that cysteine nitrosation could affect the activity of these enzymes in immune cells as well [144].”
BackgroundStuehr, D. J., & Nathan, C. F. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.5.1543 · Cited by 1,744 · cited 1× · see citing works
“In 1988–89, Hibbs as well as Stuehr and Nathan [8,9] connected the dots by showing NO to be the key effector molecule used by activated murine macrophages to kill tumors.”
BackgroundTHE MITOCHONDRIAL ELECTRON TRANSPORT AND OXIDATIVE PHOSPHORYLATION SYSTEM
Hatefi, Y. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.005055 · Cited by 1,650 · cited 2× · see citing works
“However, assumption and generalization that all enzymes containing Fe-S clusters are inhibited by the same mechanism cannot be made, as Complex III, although containing a 2Fe-2S cluster essential for electron transport function [57], was found to be still functional in injured target cells.”
BackgroundImmunometabolism governs dendritic cell and macrophage function
O'Neill, L., & Pearce, E. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151570 · Cited by 1,641 · cited 1× · see citing works
“Although alterations in the TCA are considered to be vital for appropriate immune responses [115,176], evidence suggests that in cells that lack NO, the functional TCA cycle and stabilization of KEAP1 (Kelch-like ECH-associated protein 1), a key regulator of the transcription factor NRF2, prevents NRF2-mediated transc…”
BackgroundLampropoulou, V., Sergushichev, A., Bambousková, M., Nair, S., Vincent, E. E., Loginicheva, E., Cervantes‐Barragán, L., Ma, X., Huang, S. C., Griss, T., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.004 · Cited by 1,547 · cited 2× · see citing works
“This is likely due to its weak, but substantial, inhibitory effect on SDH, although this mechanism is disputed [111,112].”
BackgroundMacrophage cytotoxicity: role for L-arginine deiminase and imino nitrogen oxidation to nitrite
Hibbs, J. B., Taintor, R. R., & Vavrin, Z. (1987) · Science · doi:10.1126/science.2432665 · Cited by 1,527 · cited 3× · see citing works
“In contrast to vascular integrity, the roles of NO in immunity involve it being a toxic agent towards infectious organisms [13,22,23], an inducer or suppressor of leukocyte apoptosis [24] or an immunoregulator [25–31].”
BackgroundAltered immune responses in mice lacking inducible nitric oxide synthase
Wei, X., Charles, I. G., Smith, A. G., Ure, J. M., Feng, G.-J., Huang, F.-P., Xu, D., Müller, W., Moncada, S., & Liew, F. Y. (1995) · Nature · doi:10.1038/375408a0 · Cited by 1,292 · see citing works
α-ketoglutarate orchestrates macrophage activation through metabolic and epigenetic reprogramming
Liu, P.-S., Wang, H., Li, X., Chao, T., Teav, T., Christen, S., Di Conza, G., Cheng, W.-C., Chou, C.-H., Vavakova, M., et al. (2017) · Nature Immunology · doi:10.1038/ni.3796 · Cited by 1,264 · cited 2× · see citing works
“These findings led to the suggestion that in polarized macrophages, pseudo-hypoxia, caused by reduction in α-KG /succinate ratios and suppression of dioxygenase activity [113,114], leads to HIF1α stabilization and expression of Pyruvate Dehydrogenase Kinase 1 (Pdk1) that phosphorylates Pyruvate Dehydrogenase (PDH), re…”
BackgroundMartin, W., Villani, G. M., Jothianandan, D., & Furchgott, R. F. (1985) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)20898-9 · Cited by 1,259 · cited 1× · see citing works
“It worked by stimulating soluble guanylate cyclase (sGC) and could be inhibited by hemoglobin, superoxide, and methylene blue [2].”
BackgroundToll-like receptor–induced changes in glycolytic metabolism regulate dendritic cell activation
Krawczyk, C. M., Holowka, T., Sun, J., Blagih, J., Amiel, E., DeBerardinis, R. J., Cross, J. R., Jung, E., Thompson, C. B., Jones, R. G., et al. (2010) · Blood · doi:10.1182/blood-2009-10-249540 · Cited by 1,246 · cited 13× · see citing works
“This changes the ETC to a more reduced state and leads to a defense response where reversal of the ATP synthase will hydrolyze cytoplasmic glycolytic ATP extruding protons (H+).”
BackgroundInfluentialCleeter, M. W. J., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., & Schapira, A. H. V. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00424-2 · Cited by 1,241 · see citing works
Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production
Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., Binz, T., Wegner, A., Tallam, A., Rausell, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218599110 · Cited by 1,191 · cited 3× · see citing works
“nitrogen intermediates through NOS2 [135], and increased production of effectors such as cationic peptides, lysosomal hydrolases, and metabolic inhibitors [136], including itaconate (antibacterial) [107] and 25-hydroxycholesterol (antiviral) [137], all contribute to macrophage antimicrobial responses.”
BackgroundIgnarro, L. J., Byrns, R. E., Buga, G. M., & Wood, K. S. (1987) · Circulation Research · doi:10.1161/01.res.61.6.866 · Cited by 1,164 · see citing works
Stuehr, D. J., & Marletta, M. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.22.7738 · Cited by 1,126 · cited 12× · see citing works
“A year before these studies on tumor cells, Stuehr and Marletta had demonstrated that macrophages exposed to recombinant interferon-γ (rIFNγ) and LPS synthesize nitrite (NO2−) and nitrate (NO3−) [7,65].”
BackgroundInfluentialEverts, B., Amiel, E., Huang, S. C.-C., Smith, A. M., Chang, C.-H., Lam, W. Y., Redmann, V., Freitas, T. C., Blagih, J., van der Windt, G. J. W., et al. (2014) · Nature Immunology · doi:10.1038/ni.2833 · Cited by 1,064 · cited 4× · see citing works
“In summary, current M1 polarization models suggest that rewiring of carbon utilization takes place through the concomitant suppression of IDH1 (via unknown mechanisms), SDH (via itaconate), and the PDH complex (via HIF1α– induced Pdk1) [102,106,117,119,141] and a subsequent increase in glutaminolysis.”
BackgroundInfluentialBrown, G. C., & Cooper, C. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01290-3 · Cited by 1,055 · cited 1× · see citing works
“At an O2 concentration of 145 μM (approximately same as arterial concentration), the IC50 for NO inhibition is 270 nM, whereas at 30 μM (approximately the tissue concentration of O2) the IC50 falls to 60 nM [38].”
BackgroundMitochondrial dysfunction prevents repolarization of inflammatory macrophages
Van den Bossche, J., Baardman, J., Otto, N. A., van der Velden, S., Neele, A. E., van den Berg, S. M., Luque-Martin, R., Chen, H.-J., Boshuizen, M. C. S., Ahmed, M., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.008 · Cited by 1,027 · cited 2× · see citing works
“also support the conclusion that the inhibition of mitochondrial respiration is not essential for maintaining inflammatory polarization [108,178].”
BackgroundRodríguez-Prados, J.-C., Través, P. G., Cuenca, J., Rico, D., Aragonés, J., Martín-Sanz, P., Cascante, M., & Boscá, L. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901698 · Cited by 1,022 · cited 2× · see citing works
“Lastly, Hif1α -/- macrophages have been shown to maintain PDK1 expression, the stimulation-induced TCA break and to compromise PDH activity [101], and we found no significant effect of Hif1α deletion on LPS-induced glycolytic flux.”
BackgroundMacrophage defense mechanisms against intracellular bacteria
Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · cited 1× · see citing works
“nitrogen intermediates through NOS2 [135], and increased production of effectors such as cationic peptides, lysosomal hydrolases, and metabolic inhibitors [136], including itaconate (antibacterial) [107] and 25-hydroxycholesterol (antiviral) [137], all contribute to macrophage antimicrobial responses.”
BackgroundThe chemical biology of nitric oxide: Implications in cellular signaling
Thomas, D. D., Ridnour, L. A., Isenberg, J. S., Flores-Santana, W., Switzer, C. H., Donzelli, S., Hussain, P., Vecoli, C., Paolocci, N., Ambs, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.020 · Cited by 975 · see citing works
Self-citationNitric oxide in immunity and inflammation
Coleman, J. W. (2001) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00086-8 · Cited by 945 · cited 6× · see citing works
“Therefore, evidence suggests that the high NO production sustained by inducible NOS (iNOS or NOS2) is fundamental for the biology of NO linked to inflammation, in contrast to NO pulses produced by the constitutive NOS enzymes that elicit a low NO wave within fractions of seconds as needed in cardiovascular responses […”
BackgroundInfluentialHibbs, J. B., Vavrin, Z., & Taintor, R. R. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.138.2.550 · Cited by 938 · cited 2× · see citing works
“put the pieces together and reported then that when murine macrophages become cytotoxic, they acquire the ability to convert L-arginine to L-citrulline, NO2− and NO3− through a pathway independent of the urea cycle [13,66].”
BackgroundReactive oxygen and reactive nitrogen intermediates in innate and specific immunity
Bogdan, C., Röllinghoff, M., & Diefenbach, A. (2000) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)00052-7 · Cited by 936 · cited 1× · see citing works
“Therefore, evidence suggests that the high NO production sustained by inducible NOS (iNOS or NOS2) is fundamental for the biology of NO linked to inflammation, in contrast to NO pulses produced by the constitutive NOS enzymes that elicit a low NO wave within fractions of seconds as needed in cardiovascular responses […”
BackgroundEndogenous nitric oxide release required for long-term synaptic depression in the cerebellum
Shibuki, K., & Okada, D. (1991) · Nature · doi:10.1038/349326a0 · Cited by 871 · see citing works
Clementi, E., Brown, G. C., Feelisch, M., & Moncada, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7631 · Cited by 863 · cited 1× · see citing works
“Considering the history of NO chemistry and the elegant dissection of metabolic mechanisms associated with macrophage cytotoxicity noted above, it is surprising that most in the immunometabolism field have been speculating that the inhibitory effects of NO on oxidative mitochondrial metabolism might be simply due to d…”
BackgroundRole of oxidative carbonylation in protein quality control and senescence
Nyström, T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600599 · Cited by 791 · see citing works
Does nitric oxide modulate mitochondrial energy generation and apoptosis?
Moncada, S., & Erusalimsky, J. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm762 · Cited by 789 · cited 3× · see citing works
“In fact, various degrees of rescue of ATP-linked mitochondrial respiration can indeed be achieved upon genetic ablation or pharmacologic inhibition of NOS2 in myeloid cells [45,108,142].”
BackgroundThomas, D. D., Liu, X., Kantrow, S. P., & Lancaster, J. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.355 · Cited by 760 · see citing works
Poderoso, J. J., Carreras, M. C., Lisdero, C., Riobó, N., Schöpfer, F., & Boveris, A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0146 · Cited by 726 · cited 1× · see citing works
“A consequence of NO inhibition of cytochrome c oxidase would be increased availability of O2 in the surrounding tissues [46,47].”
BackgroundMaragos, C. M., Morley, D., Wink, D. A., Dunams, T. M., Saavedra, J. E., Hoffman, A., Bove, A. A., Isaac, L., Hrabie, J. A., & Keefer, L. K. (1991) · Journal of Medicinal Chemistry · doi:10.1021/jm00115a013 · Cited by 722 · see citing works
Self-citationStuehr, D. J., & Marletta, M. A. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.139.2.518 · Cited by 713 · cited 10× · see citing works
“A year before these studies on tumor cells, Stuehr and Marletta had demonstrated that macrophages exposed to recombinant interferon-γ (rIFNγ) and LPS synthesize nitrite (NO2−) and nitrate (NO3−) [7,65].”
BackgroundInfluentialInhibition of Mitochondrial Electron Transport by Peroxynitrite
Radi, R., Rodriguez, M., Castro, L., & Telleri, R. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1013 · Cited by 693 · cited 14× · see citing works
“Interestingly, Cysteine39 in the ND3 subunit becomes exposed in the D-form and is susceptible to covalent modification by nitrosothiols (RSNO), ROS, and RNS [89–91], perhaps making it a specific site of physiological SNO regulation.”
BackgroundInfluentialThe multifaceted roles of nitric oxide in cancer
Wink, D. (1998) · Carcinogenesis · doi:10.1093/carcin/19.5.711 · Cited by 682 · cited 1× · see citing works
“Together, the integration of these effects may define a powerful therapeutic target [235,236].”
BackgroundSelf-citationThe Sedoheptulose Kinase CARKL Directs Macrophage Polarization through Control of Glucose Metabolism
Haschemi, A., Kosma, P., Gille, L., Evans, C. R., Burant, C. F., Starkl, P., Knapp, B., Haas, R., Schmid, J. A., Jandl, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.023 · Cited by 635 · cited 1× · see citing works
“[101] demonstrated this at the level of gene expression and many groups [102,103] have now shown that metabolic changes can be present as early as 30 min after activation.”
BackgroundItaconate: the poster child of metabolic reprogramming in macrophage function
O'Neill, L. A. J., & Artyomov, M. N. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0128-5 · Cited by 624 · cited 1× · see citing works
“The biology and biochemistry of itaconate has been recently reviewed in detail by others [128,129].”
BackgroundA roadmap for interpreting 13C metabolite labeling patterns from cells
Buescher, J. M., Antoniewicz, M. R., Boros, L. G., Burgess, S. C., Brunengraber, H., Clish, C. B., DeBerardinis, R. J., Féron, O., Frezza, C., Ghesquière, B., et al. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.02.003 · Cited by 623 · cited 1× · see citing works
“For many years, researchers have tried to link inflammatory stimuli such as LPS to altered mitochondrial function [95,96], but recent technologies [97,98] have brought advances in the field.”
BackgroundCardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I
Chouchani, E. T., Methner, C., Nadtochiy, S. M., Logan, A., Pell, V. R., Ding, S., James, A. M., Cochemé, H. M., Reinhold, J., Lilley, K. S., et al. (2013) · Nature Medicine · doi:10.1038/nm.3212 · Cited by 619 · cited 2× · see citing works
“Considering the history of NO chemistry and the elegant dissection of metabolic mechanisms associated with macrophage cytotoxicity noted above, it is surprising that most in the immunometabolism field have been speculating that the inhibitory effects of NO on oxidative mitochondrial metabolism might be simply due to d…”
BackgroundNewsholme, P. (2001) · Journal of Nutrition · doi:10.1093/jn/131.9.2515s · Cited by 619 · see citing works
Arnelle, D. R., & Stamler, J. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1231 · Cited by 604 · see citing works
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602 · see citing works
Drapier, J., & Hibbs, J. B. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.140.8.2829 · Cited by 592 · cited 4× · see citing works
“First of all, as noted above, unlike IDH1, ACO2 is a long known target of NO via attack of its FeS cluster [53,68,69].”
BackgroundResultInfluentialMishra, B. B., Rathinam, V. A. K., Martens, G. W., Martinot, A. J., Kornfeld, H., Fitzgerald, K. A., & Sassetti, C. M. (2013) · Nature Immunology · doi:10.1038/ni.2474 · Cited by 571 · see citing works
Commitment to glycolysis sustains survival of NO-producing inflammatory dendritic cells
Everts, B., Amiel, E., van der Windt, G. J. W., Freitas, T. C., Chott, R., Yarasheski, K. E., Pearce, E. L., & Pearce, E. J. (2012) · Blood · doi:10.1182/blood-2012-03-419747 · Cited by 532 · cited 4× · see citing works
“The early dissection of macrophage cytotoxic mechanisms by Hibbs and Drapier, and the finding that the metabolic switch in macrophages and DCs activated with LPS was dependent on NOS2 led to the suggestion that NO generated by NOS2 mediates the LPS-induced mitochondrial dysfunction and increase in glycolysis [142].”
BackgroundInfluentialThe dual role of iNOS in cancer
Vannini, F., Kashfi, K., & Nath, N. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.009 · Cited by 529 · cited 1× · see citing works
“Therapeutically shifting the TME from tumorigenic simmering iNOS activity driven by the tumor itself, towards an immune surveillance situation where macrophages are reprogrammed to produce higher, effector level, NO fluxes could be beneficial [237,238].”
BackgroundCordes, T., Wallace, M., Michelucci, A., Divakaruni, A. S., Sapcariu, S. C., Sousa, C., Koseki, H., Cabrales, P., Murphy, A. N., Hiller, K., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.685792 · Cited by 526 · cited 5× · see citing works
“The rapid and profound increase of itaconate in stimulated macrophages [112], Nos2−/− cells bearing higher levels of itaconate with high fractional incorporation of glucose carbon at the expense of glutamine carbon, together with the sensitivity of inhibition of PDH and ACO2 to NO, all justify a new, corrected model f…”
BackgroundInfluentialMechanistic aspects of the reactions of nitric oxide with transition-metal complexes
Ford, P. C., & Lorkovic, I. M. (2002) · Chemical Reviews · doi:10.1021/cr0000271 · Cited by 525 · cited 1× · see citing works
“The rate constant for association of NO to heme centers is typically very high relative to other potential targets [20], such that even low nanomolar levels of NO are sufficient to activate sGC [21].”
BackgroundTriggering the succinate receptor GPR91 on dendritic cells enhances immunity
Rubic, T., Lametschwandtner, G., Jost, S., Hinteregger, S., Kund, J., Carballido-Perrig, N., Schwärzler, C., Junt, T., Voshol, H., Meingassner, J. G., et al. (2008) · Nature Immunology · doi:10.1038/ni.1657 · Cited by 525 · cited 1× · see citing works
“Succinate has been implicated in various aspects of inflammatory function including acting in trans via the succinate receptor expressed on internal organs as well as on immune cells [130].”
BackgroundAnalysis and Interpretation of Microplate-Based Oxygen Consumption and pH Data
Divakaruni, A. S., Paradyse, A. R., Ferrick, D. A., Murphy, A. N., & Jastroch, M. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00016-3 · Cited by 525 · cited 1× · see citing works
“For many years, researchers have tried to link inflammatory stimuli such as LPS to altered mitochondrial function [95,96], but recent technologies [97,98] have brought advances in the field.”
BackgroundPKM2 regulates the Warburg effect and promotes HMGB1 release in sepsis
Yang, L., Xie, M., Yang, M., Yu, Y., Zhu, S., Hou, W., Kang, R., Lotze, M. T., Billiar, T. R., Wang, H., et al. (2014) · Nature Communications · doi:10.1038/ncomms5436 · Cited by 503 · cited 1× · see citing works
“[151] also exposed apparent incongruences with studies indicating that HIF1α-dependent upregulation of Pdk1 and consequent suppression of acetyl-CoA synthesis, may be responsible for OXPHOS regulation in macrophages [152].”
BackgroundNitric oxide and asthmatic inflammation
Barnes, P. J., & Liew, F. Y. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80128-6 · Cited by 502 · see citing works
Inducible nitric oxide synthase in pulmonary alveolar macrophages from patients with tuberculosis.
Nicholson, S., Bonecini-Almeida, M. D. G., Silva, J. R. L. E., Nathan, C., Xie, Q. W., Mumford, R. A., Weidner, J. R., Calaycay, J. R., Geng, J., Boéchat, N., et al. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.5.2293 · Cited by 497 · see citing works
Drapier, J., Wietzerbin, J., & Hibbs, J. B. (1988) · European Journal of Immunology · doi:10.1002/eji.1830181018 · Cited by 497 · cited 4× · see citing works
“found a correlation between the ability of combinations of stimuli to induce NO2− and NO3− synthesis from L-arginine and their ability to cause reductions in aconitase activity in the producer macrophages [67].”
BackgroundInfluentialPalmieri, E. M., Gonzalez-Cotto, M., Baseler, W. A., Davies, L. C., Ghesquière, B., Maio, N., Rice, C. M., Rouault, T. A., Cassel, T., Higashi, R. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14433-7 · Cited by 472 · cited 16× · see citing works
“Carbon tracing suggests contributions of glucose- but primarily glutamine-derived carbon during itaconate production [109].”
BackgroundInfluentialSelf-citationImmunometabolism at the interface between macrophages and pathogens
Russell, D. G., Huang, L., & VanderVen, B. C. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0124-9 · Cited by 461 · cited 4× · see citing works
“Lastly, Hif1α -/- macrophages have been shown to maintain PDK1 expression, the stimulation-induced TCA break and to compromise PDH activity [101], and we found no significant effect of Hif1α deletion on LPS-induced glycolytic flux.”
BackgroundInfluentialBagasra, O., Michaels, F. H., Zheng, Y., Bobroski, L. E., Spitsin, S. V., Fu, Z., Tawadros, R., & Koprowski, H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12041 · Cited by 456 · see citing works
Weinberg, J., Misukonis, M., Shami, P., Mason, S. N., Sauls, D., Dittman, W. A., Wood, E., Smith, G., McDonald, B., & Bachus, K. (1995) · Blood · doi:10.1182/blood.v86.3.1184.1184 · Cited by 435 · see citing works
Almeida, A., Almeida, J., Bolaños, J. P., & Moncada, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261560998 · Cited by 423 · cited 10× · see citing works
“This changes the ETC to a more reduced state and leads to a defense response where reversal of the ATP synthase will hydrolyze cytoplasmic glycolytic ATP extruding protons (H+).”
BackgroundInfluentialDiffusion of Nitric Oxide in the Aorta Wall Monitored in Situ by Porphyrinic Microsensors
Malinski, T., Taha, Z., Grunfeld, S., Patton, S. R., Kapturczak, M., & Tomboulian, P. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1735 · Cited by 417 · see citing works
Drapier, J., & Hibbs, J. B. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112642 · Cited by 415 · cited 2× · see citing works
“First of all, as noted above, unlike IDH1, ACO2 is a long known target of NO via attack of its FeS cluster [53,68,69].”
BackgroundNitric Oxide‐Mediated Inhibition of the Mitochondrial Respiratory Chain in Cultured Astrocytes
Bolaños, J. P., Peuchen, S., Heales, S., Land, J. M., & Clark, J. B. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030910.x · Cited by 413 · cited 1× · see citing works
“These authors, however, were skeptical of which oxidant compounds might be responsible for this inhibition: they found that NO2− + NO3− released by LPS+FNγ treatment was accompanied by enhanced hydrogen peroxide (H2O2) production consistent with superoxide production [71].”
BackgroundPalmieri, E. M., Menga, A., Martín‐Pérez, R., Quinto, A., Riera‐Domingo, C., Tullio, G. D., Hooper, D. C., Lamers, W. H., Ghesquière, B., McVicar, D. W., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.054 · Cited by 408 · cited 1× · see citing works
“Accordingly, our older work, tracing carbon sources in M1 polarized human monocyte derived macrophages [227], showed full glucose-derived labeling of citrate and this pattern was conserved in downstream metabolites such as α-KG and malate.”
BackgroundSelf-citationNitric oxide suppresses NLRP3 inflammasome activation and protects against LPS-induced septic shock
Mao, K., Chen, S., Chen, M., Ma, Y., Wang, Y., Huang, B., He, Z., Zeng, Y., Hu, Y., Sun, S., et al. (2013) · Cell Research · doi:10.1038/cr.2013.6 · Cited by 397 · see citing works
Effect of exogenous and endogenous nitric oxide on mitochondrial respiration of rat hepatocytes
Stadler, J., Billiar, T. R., CURRAN, R. D., Stuehr, D. J., Ochoa, J. B., & Simmons, R. L. (1991) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1991.260.5.c910 · Cited by 396 · cited 1× · see citing works
“First of all, as noted above, unlike IDH1, ACO2 is a long known target of NO via attack of its FeS cluster [53,68,69].”
BackgroundBeltrán, B., Mathur, A., Duchen, M. R., Erusalimsky, J. D., & Moncada, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.26.14602 · Cited by 392 · cited 10× · see citing works
“This changes the ETC to a more reduced state and leads to a defense response where reversal of the ATP synthase will hydrolyze cytoplasmic glycolytic ATP extruding protons (H+).”
BackgroundResultInfluentialItaconic acid is a mammalian metabolite induced during macrophage activation
Strelko, C. L., Lu, W., Dufort, F. J., Seyfried, T. N., Chiles, T. C., Rabinowitz, J. D., & Roberts, M. F. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2070889 · Cited by 391 · cited 1× · see citing works
“Irg1 is one of the most highly upregulated genes during macrophage M1 polarization and although it has been near the top of many lists of upregulated genes in macrophages for years, it has only recently come into the forefront [107,121].”
Background25-Hydroxycholesterols in innate and adaptive immunity
Cyster, J. G., Dang, E. V., Reboldi, A., & Yi, T. (2014) · Nature Reviews Immunology · doi:10.1038/nri3755 · Cited by 388 · cited 1× · see citing works
“nitrogen intermediates through NOS2 [135], and increased production of effectors such as cationic peptides, lysosomal hydrolases, and metabolic inhibitors [136], including itaconate (antibacterial) [107] and 25-hydroxycholesterol (antiviral) [137], all contribute to macrophage antimicrobial responses.”
BackgroundNitric oxide production and inducible nitric oxide synthase expression in inflammatory arthritides.
Sakurai, H., Kohsaka, H., Liu, M. F., Higashiyama, H., Hirata, Y., Kanno, K., Saito, I., & Miyasaka, N. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118292 · Cited by 388 · see citing works
The mitochondrial citrate carrier: a new player in inflammation
Infantino, V., Convertini, P., Cucci, L., Panaro, M. A., Noia, M. A. D., Calvello, R., Palmieri, F., & Iacobazzi, V. (2011) · Biochemical Journal · doi:10.1042/bj20111275 · Cited by 386 · cited 1× · see citing works
“This was first based on evidence that human histiocytoma cell lines where the mitochondrial citrate transporter had been silenced show deficits in prostaglandin mediators [120].”
BackgroundDenis, M. (1991) · Journal of Leukocyte Biology · doi:10.1002/jlb.49.4.380 · Cited by 386 · see citing works
Activation of NRF2 by Nitrosative Agents and H2O2 Involves KEAP1 Disulfide Formation
Fourquet, S., Guérois, R., Biard, D. S. F., & Tolédano, M. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051714 · Cited by 378 · see citing works
The role of iron in the activation-inactivation of aconitase.
Kennedy, M. C., Emptage, M. H., Dreyer, J.-L., & Beinert, H. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44390-0 · Cited by 377 · see citing works
Cleeter, M. W. J., Cooper, J. M., & Schapira, A. H. V. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09789.x · Cited by 372 · cited 1× · see citing works
“Accordingly, inhibition of cytochrome c oxidase is required for the irreversible loss of Complex I [79].”
BackgroundTaylor-Robinson, A. W., Liew, F. Y., Severn, A., Xu, D., McSorley, S. J., Garside, P., Padron, J., & PHILLIPS, R. S. (1994) · European Journal of Immunology · doi:10.1002/eji.1830240430 · Cited by 370 · see citing works
Wong, P. S.-Y., Hyun, J., Fukuto, J. M., Shirota, F. N., DeMaster, E. G., Shoeman, D. W., & Nagasawa, H. T. (1998) · Biochemistry · doi:10.1021/bi973153g · Cited by 363 · cited 3× · see citing works
“Indeed, the mechanism of irreversible inhibition of aldehyde dehydrogenase by HNO has been speculated to involve the presence of a sulfinamide [240,245].”
BackgroundParadoxical fate and biological action of peroxynitrite on human platelets.
Moro, M. Á., Darley-Usmar, V. M., Goodwin, D. A., Read, N. G., Zamora-Pino, R., Feelisch, M., Radomski, M. W., & Moncada, S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6702 · Cited by 363 · cited 1× · see citing works
“Although the effect of RNS depends on the composition of the microenvironment in which this substance would be generated [84], this situation facilitates the induction of the permeability”
BackgroundMacKenzie, E. D., Selak, M. A., Tennant, D. A., Payne, L. J., Crosby, S., Frederiksen, C. M., Watson, D. G., & Gottlieb, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01927-06 · Cited by 359 · see citing works
Inhibition of Cytochromes P450 by Nitric Oxide and a Nitric Oxide-Releasing Agent
Wink, D. A., Osawa, Y., Darbyshire, J. F., Jones, C. R., Eshenaur, S. C., & Nims, R. W. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1016 · Cited by 357 · see citing works
Self-citationSites of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells.
Granger, D. L., & Lehninger, A. L. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.2.527 · Cited by 348 · cited 1× · see citing works
“They found that Complex I (NADH-coenzyme Q reductase) was most sensitive to inhibition, followed by Complex II (succinate-coenzyme Q reductase) [52].”
BackgroundThe chemistry of nitroxyl (HNO) and implications in biology
Miranda, K. M. (2005) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2004.08.010 · Cited by 339 · cited 1× · see citing works
“Compared to NO and other RNS, HNO has a distinct signaling mechanism of action [242,243] and higher electrophilicity than NO [244].”
BackgroundWang, F., Zhang, S., Jeon, R., Vuckovic, I., Jiang, X., Lerman, A., Folmes, C. D., Dzeja, P. D., & Herrmann, J. (2018) · eBioMedicine · doi:10.1016/j.ebiom.2018.02.009 · Cited by 339 · cited 1× · see citing works
“IFNγ treatment alone, without LPS [170], or stimulation with monophospholipid A [171], or low LPS [112] does not result in the dramatic reductions in mitochondrial ATP production discussed above and in some circles maximal respiratory capacity (MRC) can actually increase early upon bacterial recognition [172].”
BackgroundSchneemann, M., Schoedon, G., Hofer, S., Blau, N., Guerrero, L., & Schaffner, A. (1993) · The Journal of Infectious Diseases · doi:10.1093/infdis/167.6.1358 · Cited by 333 · see citing works
Swain, A., Bambousková, M., Kim, H., Andhey, P. S., Duncan, D., Auclair, K., Chubukov, V., Simons, D. M., Roddy, T. P., Stewart, K. M., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0210-0 · Cited by 332 · cited 13× · see citing works
“However, we find that activation of NRF2 occurs regardless of intracellular availability of itaconate.”
BackgroundInfluentialNitric Oxide Potently and Reversibly Deenergizes Mitochondria at Low Oxygen Tension
Schweizer, M., & Richter, C. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2441 · Cited by 331 · see citing works
Bukrinsky, M., Nottet, H. S. L. M., Schmidtmayerova, H., Dubrovsky, L., Flanagan, C. R., Mullins, M. E., Lipton, S. A., & Gendelman, H. E. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.181.2.735 · Cited by 331 · see citing works
Lizasoaín, I., Moro, M. Á., Knowles, R. G., Darley-Usmar, V. M., & Moncada, S. (1996) · Biochemical Journal · doi:10.1042/bj3140877 · Cited by 318 · see citing works
Dobbins, R. L., Szczepaniak, L. S., Bentley, B., Esser, V., Myhill, J., & McGarry, J. D. (2001) · Diabetes · doi:10.2337/diabetes.50.1.123 · Cited by 315 · see citing works
Mitochondrial respiratory-chain adaptations in macrophages contribute to antibacterial host defense
Garaude, J., Acín-Pérez, R., Martínez-Cano, S., Enamorado, M., Ugolini, M., Nistal-Villán, E., Hervás-Stubbs, S., Pelegrín, P., Sander, L. E., Enríquez, J. A., et al. (2016) · Nature Immunology · doi:10.1038/ni.3509 · Cited by 313 · cited 1× · see citing works
“IFNγ treatment alone, without LPS [170], or stimulation with monophospholipid A [171], or low LPS [112] does not result in the dramatic reductions in mitochondrial ATP production discussed above and in some circles maximal respiratory capacity (MRC) can actually increase early upon bacterial recognition [172].”
BackgroundLachmandas, E., Boutens, L., Ratter, J. M., Hijmans, A., Hooiveld, G. J. E. J., Joosten, L. A. B., Rodenburg, R. J., Fransen, J. A. M., Houtkooper, R. H., van Crevel, R., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.246 · Cited by 310 · cited 1× · see citing works
“Many studies have reported complex metabolic footprints in macrophages activated under different stimuli and tissue environments [168,169].”
BackgroundDaniels, B. P., Kofman, S. B., Smith, J. R., Norris, G. T., Snyder, A. G., Kolb, J. P., Gao, X., Locasale, J. W., Martinez, J., Gale, M., et al. (2019) · Immunity · doi:10.1016/j.immuni.2018.11.017 · Cited by 305 · see citing works
Triacylglycerol synthesis enhances macrophage inflammatory function
Castoldi, Â., Monteiro, L. D. B., Bakker, N. V. T., Sanin, D. E., Rana, N., Corrado, M., Cameron, A. M., Hässler, F., Matsushita, M., Caputa, G., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17881-3 · Cited by 299 · cited 1× · see citing works
“Although DGAT1-dependent TG synthesis has recently been reported to enhance macrophage inflammatory function together with PGE2 signaling [197], this finding still lacks mechanistic understanding regarding its intrinsic connections to metabolic needs and cell function.”
BackgroundProduction of nitric oxide in the synovial membrane of rheumatoid and osteoarthritis patients.
McInnes, I. B., Leung, B. P. L., Field, M., Wei, X., Huang, F., Sturrock, R. D., Kinninmonth, A. W. G., Weidner, J. R., Mumford, R. A., & Liew, F. Y. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1519 · Cited by 288 · see citing works
Biological nitric oxide signalling: chemistry and terminology
Heinrich, T. A., da Silva, R. S., Miranda, K. M., Switzer, C., Wink, D. A., & Fukuto, J. M. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12217 · Cited by 287 · cited 2× · see citing works
“Nitrosation requires NO+ donors since in solution, NO+ has an appreciable lifetime only under high acidic conditions [35].”
BackgroundSelf-citationMiranda, K. M., Paolocci, N., Katori, T., Thomas, D. D., Ford, E., Bartberger, M. D., Espey, M. G., Kass, D. A., Feelisch, M., Fukuto, J. M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1430507100 · Cited by 283 · cited 1× · see citing works
“Compared to NO and other RNS, HNO has a distinct signaling mechanism of action [242,243] and higher electrophilicity than NO [244].”
BackgroundSelf-citationNitric oxide prevents a pathogen-permissive granulocytic inflammation during tuberculosis
Mishra, B. B., Lovewell, R. R., Olive, A. J., Zhang, G., Wang, W., Eugenín, E. A., Smith, C. M., Phuah, J. Y., Long, J. E., Dubuke, M. L., et al. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.72 · Cited by 280 · see citing works
Nair, S., Huynh, J. P., Lampropoulou, V., Loginicheva, E., Esaulova, E., Gounder, A. P., Boon, A. C. M., Schwarzkopf, E. A., Bradstreet, T. R., Edelson, B. T., et al. (2018) · Journal of Experimental Medicine · doi:10.1084/jem.20180118 · Cited by 280 · see citing works
Vouldoukis, I., Riveros‐Moreno, V., Dugas, B., Ouaaz, F., Bécherel, P., Debré, P., Moncada, S., & Mossalayi, M. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7804 · Cited by 267 · see citing works
Iniesta, V., Gómez-Nieto, L. C., & Corraliza, I. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.6.777 · Cited by 267 · cited 1× · see citing works
“Moreover, the NOS intermediate NOHA, supporting effective NO production by suppressing arginase activity freeing cellular arginine for NO production [139], has been shown to be critical in controlling parasites such as Leishmania [140].”
BackgroundItaconic acid mediates crosstalk between macrophage metabolism and peritoneal tumors
Weiss, J. M., Davies, L. C., Karwan, M., Ileva, L., Ozaki, M. K., Cheng, R. Y. S., Ridnour, L. A., Annunziata, C. M., Wink, D. A., & McVicar, D. W. (2018) · Journal of Clinical Investigation · doi:10.1172/jci99169 · Cited by 267 · cited 1× · see citing works
“Itaconate production by the resident macrophages of the peritoneal cavity has also been shown to regulate their ROS production and facilitate their ability to promote tumor growth in this anatomical site [127].”
BackgroundSelf-citationBailey, J. D., Diotallevi, M., NICOL, T., McNeill, E., Shaw, A., Chuaiphichai, S., Hale, A., Starr, A., Nandi, M., Stylianou, E., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.018 · Cited by 266 · cited 20× · see citing works
“Cyt c, cytochrome c; FADH2, flavin-adenine dinucleotide reduced; NADH, nicotinamide adenine dinucleotide reduced; Q, ubiquinone; I, II, III, and IV refer to the complexes of ETC. ANT, adenosine nucleotide translocator.”
BackgroundMethodInfluentialNitric oxide-mediated mitochondrial damage: A potential neuroprotective role for glutathione
Bolaños, J. P., Heales, S. J. R., Peuchen, S., Barker, J. E., Land, J. M., & Clark, J. B. (1996) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00240-7 · Cited by 263 · see citing works
Reddy, D. S. A., Lancaster, J. R., & Cornforth, D. P. (1983) · Science · doi:10.1126/science.6308761 · Cited by 258 · cited 1× · see citing works
“Through Electron Spin Resonance, iron-nitric oxide complexes were detected in proteins in these cells [59].”
BackgroundApoptosis-induced mitochondrial dysfunction causes cytoplasmic lipid droplet formation
Boren, J., & Brindle, K. M. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.34 · Cited by 255 · see citing works
Doulias, P.-T., Tenopoulou, M., Greene, J. L., Raju, K., & Ischiropoulos, H. (2013) · Science Signaling · doi:10.1126/scisignal.2003252 · Cited by 250 · cited 1× · see citing works
“Others have referred to evidence that many metabolic enzymes could be s-nitrosated by NO [143] and assumed that cysteine nitrosation could affect the activity of these enzymes in immune cells as well [144].”
BackgroundMechanisms of triglyceride accumulation in activated macrophages
Feingold, K. R., Shigenaga, J. K., Kazemi, M. R., McDonald, C. M., Patzek, S. M., Cross, A. S., Moser, A. H., & Grünfeld, C. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.1111537 · Cited by 249 · cited 3× · see citing works
“Therefore, the NO-dependent increased formation of lipid vesicles during macrophage activation may facilitate the production and storage of compounds important for subsequent effector function [156,194].”
BackgroundLeukocyte lipid bodies — Biogenesis and functions in inflammation
Bozza, P. T., Magalhães, K. G., & Weller, P. F. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.01.005 · Cited by 245 · cited 1× · see citing works
“Therefore, the NO-dependent increased formation of lipid vesicles during macrophage activation may facilitate the production and storage of compounds important for subsequent effector function [156,194].”
BackgroundTrained Immunity: An Ancient Way of Remembering
Netea, M. G., & van der Meer, J. W. M. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.02.003 · Cited by 245 · cited 1× · see citing works
“Many studies have reported complex metabolic footprints in macrophages activated under different stimuli and tissue environments [168,169].”
BackgroundNitric oxide in parasitic infections
Brunet, L. R. (2001) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00090-x · Cited by 240 · cited 1× · see citing works
“In contrast to vascular integrity, the roles of NO in immunity involve it being a toxic agent towards infectious organisms [13,22,23], an inducer or suppressor of leukocyte apoptosis [24] or an immunoregulator [25–31].”
BackgroundReaction of Superoxide and Nitric Oxide with Peroxynitrite
Jourd’heuil, D., Jourd’heuil, F. L., Kutchukian, P. S., Musah, R. A., Wink, D. A., & Grisham, M. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102341200 · Cited by 239 · see citing works
Self-citationNitrite in Human Saliva. Its Possible Relationship to Nitrosamine Formation23
Tannenbaum, S. R., Sinskey, A. J., Weisman, M., & Bishop, W. (1974) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/53.1.79 · Cited by 237 · see citing works
Mason, M. G., Nicholls, P., Wilson, M. T., & Cooper, C. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506562103 · Cited by 233 · see citing works
A broken Krebs cycle in macrophages
O’Neill, L. A. J. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.017 · Cited by 232 · cited 5× · see citing works
“These findings led to the suggestion that in polarized macrophages, pseudo-hypoxia, caused by reduction in α-KG /succinate ratios and suppression of dioxygenase activity [113,114], leads to HIF1α stabilization and expression of Pyruvate Dehydrogenase Kinase 1 (Pdk1) that phosphorylates Pyruvate Dehydrogenase (PDH), re…”
BackgroundInfluentialThe Immunomodulatory Potential of the Metabolite Itaconate
Hooftman, A., & O'Neill, L. A. J. (2019) · Trends in Immunology · doi:10.1016/j.it.2019.05.007 · Cited by 232 · cited 1× · see citing works
“The biology and biochemistry of itaconate has been recently reviewed in detail by others [128,129].”
BackgroundVijayan, V., Pradhan, P., Braud, L., Fuchs, H. R., Gueler, F., Motterlini, R., Foresti, R., & Immenschuh, S. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101147 · Cited by 231 · cited 1× · see citing works
“For example, the mitochondrial bioenergetic changes observed in murine M1 polarized BMDMs are largely absent in similarly stimulated human PBMC-derived macrophages [100,226].”
BackgroundMYC inhibition induces metabolic changes leading to accumulation of lipid droplets in tumor cells
Zirath, H., Frenzel, A., Oliynyk, G., Segerström, L., Westermark, U., Larsson, K., Persson, M. M., Hultenby, K. R., Lehtiö, J., Einvik, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222404110 · Cited by 229 · see citing works
Nitric Oxide, Cytochrome C Oxidase, and the Cellular Response to Hypoxia
Taylor, C. T., & Moncada, S. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.181628 · Cited by 220 · cited 1× · see citing works
“Although the mechanism of A/D transition may only operate in pathological conditions, when enzyme turnover is limited by hypoxia or by a high NO/O2 ratios [92,162], we suggested that it is the lack of substrates, (i.”
BackgroundYi, Z., Deng, M., Scott, M. J., Fu, G., Loughran, P., Lei, Z., Li, S., Sun, P., Yang, C., Li, W., et al. (2020) · Hepatology · doi:10.1002/hep.31147 · Cited by 216 · see citing works
Molecular Mechanisms of Nitric Oxide in Cancer Progression, Signal Transduction, and Metabolism
Somasundaram, V., Basudhar, D., Bharadwaj, G., No, J. H., Ridnour, L. A., Cheng, R. Y. S., Fujita, M., Thomas, D. D., Anderson, S. K., McVicar, D. W., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7527 · Cited by 215 · cited 4× · see citing works
“Superoxide is generated within complexes I and III as byproduct of mitochondrial electron transfer which, if not consumed by mitochondrial manganese-dependent SOD (MnSOD) [77,78], can react with NO to form ONOO− which is rapidly converted to NO2 and N2O3 [34].”
BackgroundInfluentialSelf-citationOn the expression of nitric oxide synthase by human macrophages. Why no NO?
Albina, J. E. (1995) · Journal of Leukocyte Biology · doi:10.1002/jlb.58.6.643 · Cited by 213 · see citing works
Hypoxia stimulates release of endothelium-derived relaxant factor
Pohl, U., & Busse, R. (1989) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1989.256.6.h1595 · Cited by 207 · cited 1× · see citing works
“As reduced supplies of O2 will make endogenous NO even more effective at inhibiting cytochrome c oxidase [48], this might indeed be a mechanism in the microcirculation by which NO, sensing hypoxia, diverts O2 into adjacent issues and at the same time induces vasodilation in an attempt to improve tissue perfusion [45].”
BackgroundTorres, J., Darley-Usmar, V. M., & Wilson, M. T. (1995) · Biochemical Journal · doi:10.1042/bj3120169 · Cited by 206 · cited 1× · see citing works
“In later studies, NO was found to bind and dissociate very rapidly from the enzyme [40,41].”
BackgroundGroot, C. J. A. D., Ruuls, S. R., THEEUWES, J. W. M., Dijkstra, C. D., & van der Valk, P. (1997) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199701000-00002 · Cited by 205 · see citing works
Vinogradov, A. D. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00026-7 · Cited by 202 · cited 3× · see citing works
“Deactive or dormant (D) enzyme is reactivated by a pulse of NADH, when the enzyme undergoes one or several slow turnovers or chemical conversions as NADH is oxidized and ubiquinone is reduced [87].”
BackgroundManderson, A. P., Kay, J. G., Hammond, L. A., Brown, D. L., & Stow, J. L. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612131 · Cited by 198 · cited 1× · see citing works
“Unlike the NOS2− and NO-independent lipogenesis of species like phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylinositol (PI) which is important to support the need of cytokine secretion within the ER and Golgi network [195,196], the role of TG synthesis via DGAT1 is less clear.”
BackgroundLiew, F. Y., Li, Y., Moss, D., Parkinson, C., Rogers, M. V., & Moncada, S. (1991) · European Journal of Immunology · doi:10.1002/eji.1830211216 · Cited by 197 · see citing works
Muñoz‐Fernández, M. Á., Fernández, M. A., & Fresno, M. (1992) · Immunology Letters · doi:10.1016/0165-2478(92)90090-b · Cited by 197 · see citing works
Oxidative stress and S‐nitrosylation of proteins in cells
Beltrán, B., Orsi, A., Clementi, E., & Moncada, S. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703147 · Cited by 196 · cited 1× · see citing works
“transition pore (PTP), which leads to the collapse of the membrane potential, mitochondrial swelling, outer mitochondrial membrane rupture, release of mitochondrial pro-apoptotic factors, and cell death [85] (Figure 2b).”
BackgroundInducible nitric oxide synthase in the liver: regulation and function.
Taylor, B. S., Alarcon, L. H., & Billiar, T. R. (1998) · PubMed · Cited by 195 · see citing works
Lushchak, O. V., Piroddi, M., Galli, F., & Lushchak, V. I. (2013) · Redox Report · doi:10.1179/1351000213y.0000000073 · Cited by 195 · see citing works
Abu‐Soud, H. M., Wang, J., Rousseau, D. L., Fukuto, J. M., Ignarro, L. J., & Stuehr, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.39.22997 · Cited by 193 · see citing works
Cytokine Secretion in Macrophages: SNAREs, Rabs, and Membrane Trafficking
Murray, R. Z., & Stow, J. L. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00538 · Cited by 190 · cited 1× · see citing works
“Unlike the NOS2− and NO-independent lipogenesis of species like phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylinositol (PI) which is important to support the need of cytokine secretion within the ER and Golgi network [195,196], the role of TG synthesis via DGAT1 is less clear.”
BackgroundRole of nitric oxide in lysis of tumor cells by cytokine-activated endothelial cells.
Li, L. M., Kilbourn, R. G., Adams, J. M., & Fidler, I. J. (1991) · PubMed · Cited by 189 · see citing works
NITRIC OXIDE—A NEW ENDOGENOUS IMMUNOMODULATOR
Langrehr, J. M., HOFFMAN, R. A., Lancaster, J. R., & Simmons, R. L. (1993) · Transplantation · doi:10.1097/00007890-199306000-00001 · Cited by 187 · see citing works
Pellat‐Deceunynck, C., Henry, Y. A., & Drapier, J. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91919-j · Cited by 185 · cited 1× · see citing works
“This work led to the conclusion that inhibition of mitochondrial non-heme iron-dependent enzymes in macrophages is mediated by autologous NO binding to enzymes containing iron-prosthetic groups [67,70].”
BackgroundQualls, J. E., Subramanian, C., Rafi, W., Smith, A. M., Balouzian, L., DeFreitas, A. A., Shirey, K. A., Reutterer, B., Kernbauer, E., Stockinger, S., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.07.012 · Cited by 184 · see citing works
Cutting Edge: Nitric Oxide Inhibits the NLRP3 Inflammasome
Hernandez-Cuellar, E., Tsuchiya, K., Hara, H., Fang, R., Sakai, S., Kawamura, I., Akira, S., & Mitsuyama, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202479 · Cited by 184 · see citing works
Injury of neoplastic cells by murine macrophages leads to inhibition of mitochondrial respiration.
Granger, D. L., Taintor, R. R., Cook, J. L., & Hibbs, J. B. (1980) · Journal of Clinical Investigation · doi:10.1172/jci109679 · Cited by 180 · cited 1× · see citing works
“Reports from 1980 began to show that incubation of a variety of neoplastic cell types with cytotoxic macrophage-conditional medium (CM) leads to inhibition of target cell mitochondrial respiration by as much as 80–90% [51].”
BackgroundWang, C., Liu, C. Y., Lin, H.-C., Yu, C.-T., Chung, K. F., & Kuo, H.-P. (1998) · European Respiratory Journal · doi:10.1183/09031936.98.11040809 · Cited by 176 · see citing works
Maria, R. D., Cifone, M. G., Trotta, R., Rippo, M. R., Festuccia, C., Santoni, A., & Testi, R. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.5.1999 · Cited by 176 · see citing works
Seim, G. L., Britt, E. C., John, S. V., Yeo, F. J., Johnson, A. R., Eisenstein, R. S., Pagliarini, D. J., & Fan, J. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0083-2 · Cited by 174 · cited 21× · see citing works
“concluded that that mechanism only partially reduces the flux through PDH [153].”
BackgroundInfluentialDeMaster, E. G., Redfern, B., & Nagasawa, H. T. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00080-x · Cited by 173 · cited 1× · see citing works
“Indeed, the mechanism of irreversible inhibition of aldehyde dehydrogenase by HNO has been speculated to involve the presence of a sulfinamide [240,245].”
BackgroundSorting cells alters their redox state and cellular metabolome
Llufrio, E. M., Wang, L., Naser, F. J., & Patti, G. J. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.004 · Cited by 172 · cited 1× · see citing works
“Given known metabolic plasticity in vivo and reports that redox states and metabolomes are altered during ex vivo manipulations [228], our in vivo study [109] of a modified Schwartzman-like reaction has important implications for the understanding of the regulation of immunity and disease pathogenesis.”
BackgroundWink, D. A., & Laval, J. (1994) · Carcinogenesis · doi:10.1093/carcin/15.10.2125 · Cited by 167 · see citing works
Self-citationAnalysis of Nitric Oxide Synthase and Nitrotyrosine Expression in Human Pulmonary Tuberculosis
Choi, H.-S., Rai, P. R., Chu, H. W., Cool, C. D., & Chan, E. D. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2201023 · Cited by 161 · see citing works
Kröncke, K., Fehsel, K., Suschek, C. V., & Kolb-Bachofen, V. (2001) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00087-x · Cited by 161 · cited 1× · see citing works
“In contrast to vascular integrity, the roles of NO in immunity involve it being a toxic agent towards infectious organisms [13,22,23], an inducer or suppressor of leukocyte apoptosis [24] or an immunoregulator [25–31].”
BackgroundDhakshinamoorthy, S., & Porter, A. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312492200 · Cited by 159 · see citing works
Nitric oxide activates Nrf2 through S-nitrosylation of Keap1 in PC12 cells
Um, H.-C., Jang, J.-H., Kim, D.-H., Lee, C., & Surh, Y.-J. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.06.001 · Cited by 153 · cited 1× · see citing works
“Ongoing expression analysis and targeted metabolomics in BMDM from Acod1−/−, Nos2−/−, and double knockouts mice and the use of NO donors will likely definitively find that the NRF2 pathway is driven directly by NO as has been suggested for other cell types [193].”
BackgroundNitric oxide stimulates Nrf2 nuclear translocation in vascular endothelium
Buckley, B. J., Marshall, Z. M., & Whorton, A. R. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01308-1 · Cited by 152 · see citing works
Signaling and stress: The redox landscape in NOS2 biology
Thomas, D. D., Heinecke, J. L., Ridnour, L. A., Cheng, R. Y., Kesarwala, A. H., Switzer, C. H., McVicar, D. W., Roberts, D. D., Glynn, S., Fukuto, J. M., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.002 · Cited by 150 · cited 5× · see citing works
“The rate constant for association of NO to heme centers is typically very high relative to other potential targets [20], such that even low nanomolar levels of NO are sufficient to activate sGC [21].”
BackgroundInfluentialSelf-citationMcNeill, E., Crabtree, M. J., Sahgal, N., Patel, J., Chuaiphichai, S., Iqbal, A. J., Hale, A., Greaves, D. R., & Channon, K. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.575 · Cited by 150 · cited 4× · see citing works
“Moreover, Bailey et al. observed increased transcription of Il1b, and although HIF1α can transcriptionally regulate Il1b, both labs concluded that HIF1α was not responsible for their findings.”
BackgroundInfluentialGalkin, A., Meyer, B., Wittig, I., Karas, M., Schägger, H., Vinogradov, A., & Brandt, U. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803190200 · Cited by 147 · see citing works
On the Mechanism of Inhibition of Cytochrome c Oxidase by Nitric Oxide
Giuffrè, A., Sarti, P., D’Itri, E., Buse, G., Soulimane, T., & Brunori, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.52.33404 · Cited by 144 · see citing works
Regulation of mitochondrial processes by protein S-nitrosylation
Piantadosi, C. A. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.03.008 · Cited by 144 · cited 1× · see citing works
“Older reports on the E3 of PDH support its targeting by nitroxyl (HNO) or peroxynitrite [154,155].”
BackgroundGross, T. J., Kremens, K., Powers, L. S., Brink, B., Knutson, T. M., Domann, F. E., Philibert, R. A., Milhem, M. M., & Monick, M. M. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1301758 · Cited by 139 · see citing works
Oxidized Mitochondrial Protein Degradation and Repair in Aging and Oxidative Stress
Ugarte, N., Petropoulos, I., & Friguet, B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2998 · Cited by 136 · see citing works
Cameron, M. L., Granger, D. L., Weinberg, J. B., Kozumbo, W. J., & Koren, H. S. (1990) · American Review of Respiratory Disease · doi:10.1164/ajrccm/142.6_pt_1.1313 · Cited by 135 · cited 1× · see citing works
“An alternative hypothesis was that human monocytes/macrophages cannot synthesize tetrahydrobiopterin, an essential co-factor for iNOS activity and, thus, needed to acquire it from other cells, such as lymphocytes [218,219].”
BackgroundCharacterisation of the active/de-active transition of mitochondrial complex I
Babot, M., Birch, A., Labarbuta, P., & Galkin, A. S. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.018 · Cited by 133 · cited 2× · see citing works
“In brief, the enzyme spontaneously converts into the D-form after exposure to high physiological temperatures (>30 °C) or in the absence of substrate [86,87].”
BackgroundLack of Oxygen Deactivates Mitochondrial Complex I
Galkin, A. S., Abramov, A. Y., Frakich, N., Duchen, M. R., & Moncada, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054346 · Cited by 131 · see citing works
Nitric oxide and T helper cell immunity
van der Veen, R. C. (2001) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00093-5 · Cited by 131 · see citing works
The reemergence of nitric oxide and cancer
Wink, D. A., Ridnour, L. A., Hussain, S. P., & Harris, C. C. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.05.003 · Cited by 130 · see citing works
Self-citationSchoedon, G., Troppmair, J., FONTANA, A., Huber, C., Curtius, H., & Niederwieser, A. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13515.x · Cited by 130 · cited 1× · see citing works
“An alternative hypothesis was that human monocytes/macrophages cannot synthesize tetrahydrobiopterin, an essential co-factor for iNOS activity and, thus, needed to acquire it from other cells, such as lymphocytes [218,219].”
BackgroundDirect Evidence of Nitric Oxide Presence within Mitochondria
López-Figueroa, M. O., Caamaño, C. A., Morano, M. I., Rønn, L. C. B., Akil, H., & Watson, S. J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2748 · Cited by 124 · see citing works
S-Nitrosation of Mitochondrial Complex I Depends on Its Structural Conformation
Galkin, A., & Moncada, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707543200 · Cited by 122 · cited 2× · see citing works
“Re-activation of the D form by NADH was inhibited by nitrosothiols and peroxynitrite whilst the A form was insensitive to such treatment [92].”
BackgroundSuperoxide fluxes limit nitric oxide-induced signaling
Thomas, D. D., Ridnour, L. A., Espey, M. G., Donzelli, S., Ambs, S., Hussain, S. P., Harris, C. C., DeGraff, W., Roberts, D. D., Mitchell, J. B., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602242200 · Cited by 121 · cited 1× · see citing works
“Superoxide is generated within complexes I and III as byproduct of mitochondrial electron transfer which, if not consumed by mitochondrial manganese-dependent SOD (MnSOD) [77,78], can react with NO to form ONOO− which is rapidly converted to NO2 and N2O3 [34].”
BackgroundSelf-citationLIU, X., Peyton, K. J., Ensenat, D., WANG, H., HANNINK, M., Alam, J., & Durante, W. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.004 · Cited by 120 · see citing works
Evaluation of nitrite production by human monocyte-derived macrophages
Padgett, E. L., & Pruett, S. B. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90813-z · Cited by 118 · see citing works
Superoxide production by mitochondria in the presence of nitric oxide forms peroxynitrite
Packer, M. A., Porteous, C. M., & Murphy, M. P. (1996) · IUBMB Life · doi:10.1080/15216549600201103 · Cited by 118 · see citing works
Amiel, E., Everts, B., Fritz, D. I., Beauchamp, S., Ge, B., Pearce, E. L., & Pearce, E. J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302498 · Cited by 116 · cited 1× · see citing works
“This second wave of glycolytic induction is mediated in DCs by mTOR/ HIF1α /NOS2 [142,146].”
BackgroundBaseler, W. A., Davies, L. C., Quigley, L., Ridnour, L. A., Weiss, J. M., Hussain, S. P., Wink, D. A., & McVicar, D. W. (2016) · Redox Biology · doi:10.1016/j.redox.2016.09.005 · Cited by 113 · cited 2× · see citing works
“[151] also exposed apparent incongruences with studies indicating that HIF1α-dependent upregulation of Pdk1 and consequent suppression of acetyl-CoA synthesis, may be responsible for OXPHOS regulation in macrophages [152].”
BackgroundSelf-citationTamura, M., Hazeki, O., Nioka, S., & Chance, B. (1989) · Annual Review of Physiology · doi:10.1146/annurev.ph.51.030189.004121 · Cited by 111 · cited 1× · see citing works
“Intracellularly, the concentration of O2 has been reported to be as low as 10 μM [42].”
BackgroundBasudhar, D., Glynn, S. A., Greer, M., Somasundaram, V., No, J. H., Scheiblin, D. A., Garrido, P., Heinz, W. F., Ryan, A. E., Weiss, J. M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1709119114 · Cited by 110 · cited 1× · see citing works
“Although human endothelial cells, hepatocytes, and other non-myeloid human cell types [198] have been shown to readily express NOS2 [199] and produce substantial fluxes of NO, many authors have reported limited induction of iNOS in human monocytes/macrophages causing continued controversy regarding the role of NO in h…”
BackgroundSelf-citationNitric oxide activation of Keap1/Nrf2 signaling in human colon carcinoma cells
Li, C.-Q., Kim, M. Y., Godoy, L. C., Thiantanawat, A., Trudel, L. J., & Wogan, G. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907539106 · Cited by 108 · see citing works
Buga, G. M., Liu, W., Bauer, P. M., Fukuto, J. M., & Ignarro, L. J. (1998) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1998.275.4.r1256 · Cited by 108 · see citing works
The role of nitric oxide in metabolic regulation of Dendritic cell immune function
Thwe, P. M., & Amiel, E. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.10.032 · Cited by 107 · cited 2× · see citing works
“This phenomenon has led many researchers to assume that HIF1α is critically required for DC glycolytic reprogramming, when in fact this is only the case for the sustained commitment to glycolysis observed in NO-producing DCs [145].”
BackgroundForkink, M., Manjeri, G. R., Liemburg-Apers, D. C., Nibbeling, E. A. R., Blanchard, M. G., Wojtala, A., Smeitink, J. A. M., Wieckowski, M. R., Willems, P. H. G. M., & Koopman, W. J. H. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.04.008 · Cited by 106 · cited 1× · see citing works
“They align perfectly with a model where the hyperpolarization of mitochondrial membranes, the condition where the mitochondrial inner membrane becomes more negative on the matrix side [148,149], is induced by NO initially blocking Complex IV and favoring hydrolysis of glycolytically-derived ATP [80,150] (Figure 2a).”
BackgroundTargeting Tumor Perfusion and Oxygenation to Improve the Outcome of Anticancer Therapy1
Jordan, B. F., & Sonveaux, P. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00094 · Cited by 104 · see citing works
Hypoxia-driven immunosuppression: A new reason to use thermal therapy in the treatment of cancer?
Lee, C.-T., Mace, T. A., & Repasky, E. A. (2010) · International Journal of Hyperthermia · doi:10.3109/02656731003601745 · Cited by 102 · cited 1× · see citing works
“Of consequence, the increased available pO2 associated with elevated NO levels can affect the immune response [234].”
BackgroundLi, C., Wang, Y., Li, Y., Yu, Q., Jin, X., Wang, X., Jia, A., Hu, Y., Han, L., Wang, J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-22039-9 · Cited by 101 · cited 1× · see citing works
“The result is so called M1, proinflammatory macrophages, which demonstrate reduced mitochondrial activity together with substantial upregulation of glycolytic metabolism for the fast generation of ATP needed to sustain phagocytosis and microbial killing [102,104,105].”
BackgroundKolb, J., Paul‐Eugène, N., Damais, C., Yamaoka, K. A., Drapier, J., & Dugas, B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36955-7 · Cited by 100 · see citing works
Kent, T. A., Emptage, M. H., Merkle, H., Kennedy, M. C., Beinert, H., & Münck, E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88861-5 · Cited by 100 · see citing works
Fensterheim, B. A., Young, J. D., Luan, L., Kleinbard, R. R., Stothers, C. L., Patil, N. K., Pereira, A. G. M., Guo, Y., Trenary, I. A., Hernandez, A., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800085 · Cited by 99 · cited 1× · see citing works
“IFNγ treatment alone, without LPS [170], or stimulation with monophospholipid A [171], or low LPS [112] does not result in the dramatic reductions in mitochondrial ATP production discussed above and in some circles maximal respiratory capacity (MRC) can actually increase early upon bacterial recognition [172].”
BackgroundIntraphagosomal Measurement of the Magnitude and Duration of the Oxidative Burst
VanderVen, B. C., Yates, R. M., & Russell, D. G. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00877.x · Cited by 98 · see citing works
Role of nitric oxide in Sjögren's syndrome
Konttinen, Y. T., Platts, L. A. M., Tuominen, S., Eklund, K. K., Santavirta, N., Törnwall, J., Sorsa, T. A., Hukkanen, M., & Polak, J. M. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400515 · Cited by 98 · see citing works
Perrotta, C., Cervia, D., Renzo, I. D., Moscheni, C., Bassi, M. T., Campana, L., Martelli, C., Catalani, E., Giovarelli, M., Zecchini, S., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01186 · Cited by 98 · cited 1× · see citing works
“Therapeutically shifting the TME from tumorigenic simmering iNOS activity driven by the tumor itself, towards an immune surveillance situation where macrophages are reprogrammed to produce higher, effector level, NO fluxes could be beneficial [237,238].”
Background
Flagged first, then by citations
5 of the 252 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Macrophages in immunoregulation and therapeutics
Chen, S., Saeed, A. F. U. H., Liu, Q., Jiang, Q., Xu, H., Xiao, G. G., Rao, L., & Duo, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01452-1 · Cited by 2,348 · see citing works
Macrophage plasticity: signaling pathways, tissue repair, and regeneration
Yan, L., Wang, J., Cai, X., Liou, Y., Shen, H., Hao, J., Huang, C., Luo, G., & He, W. (2024) · MedComm · doi:10.1002/mco2.658 · Cited by 396 · see citing works
Macrophage Reprogramming and Cancer Therapeutics: Role of iNOS-Derived NO
Kashfi, K., Kannikal, J. J., & Nath, N. (2021) · Cells · doi:10.3390/cells10113194 · Cited by 236 · see citing works
“If the cell situation could be altered such that the TME’s low iNOS activity is reprogrammed to produce higher iNOS/NO concentrations, it may then be of therapeutic value [74,75].”
BackgroundMarrocco, A., & Ortiz, L. A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.936167 · Cited by 166 · see citing works
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works
“The •NO/ROS balance is also important during the transition from Th1 to Th2 [125,126].”
BackgroundHan, C., Zhang, X., Wang, F., Yu, Q., Chen, F., Shen, D., Yang, Z., Wang, T., Jiang, M., Deng, T., et al. (2021) · Carbon · doi:10.1016/j.carbon.2021.07.063 · Cited by 135 · see citing works
An Overview of NO Signaling Pathways in Aging
Pourbagher-Shahri, A. M., Farkhondeh, T., Talebi, M., Kopustinskiene, D. M., Samarghandian, S., & Bernatoniene, J. (2021) · Molecules · doi:10.3390/molecules26154533 · Cited by 101 · see citing works
Errico, S., Spagnoletta, A., Verardi, A., Moliterni, S., Dimatteo, S., & Sangiorgio, P. (2021) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12863 · Cited by 100 · see citing works
Redox regulation of macrophages
Tran, N., & Mills, E. L. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103123 · Cited by 97 · see citing works
“S cluster (see reviews [65,93] for further discussion).”
BackgroundArginine metabolism in myeloid cells in health and disease
Karadima, E., Chavakis, T., & Alexaki, V. I. (2025) · Seminars in Immunopathology · doi:10.1007/s00281-025-01038-9 · Cited by 83 · see citing works
“Aside from its function in elimination of bacteria, NO exerts numerous functions within macrophages and their surrounding micro-environment [37].”
Modulation of macrophage metabolism as an emerging immunotherapy strategy for cancer
Dussold, C., Zilinger, K., Turunen, J. R., Heimberger, A. B., & Miska, J. M. (2024) · Journal of Clinical Investigation · doi:10.1172/jci175445 · Cited by 78 · see citing works
“These changes, which are mediated by LPS, promote inflammatory polarization, which leads to increased cytokine and NO production by macrophages (128).”
Modulating Nitric Oxide: Implications for Cytotoxicity and Cytoprotection
Belenichev, I. F., Popazova, O., Bukhtiyarova, N. V., Savchenko, D., Oksenych, V., & Kamyshnyi, O. (2024) · Antioxidants · doi:10.3390/antiox13050504 · Cited by 80 · see citing works
Effect of micro- and nanoplastic particles on human macrophages
Adler, M. Y., Issoual, I., Rückert, M., Deloch, L., Meier, C., Tschernig, T., Alexiou, C., Pfister, F., Ramsperger, A. F. R. M., Laforsch, C., et al. (2024) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2024.134253 · Cited by 69 · see citing works
Zhang, X., Liu, Z., Zhong, C., Pu, Y., Yang, Z., & Bao, Y. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.08.176 · Cited by 64 · see citing works
Ji, C., Zhang, Z., Chen, J., Song, D., Liu, B., Li, J., Liu, R., Niu, J., Wang, D., Ling, N., et al. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c03850 · Cited by 61 · see citing works
Peng, C., Feng, Z., Ou, L., Zou, Y., Sang, S., Liu, H., Zhu, W., Gan, G., Zhang, G., & Yao, M. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105626 · Cited by 57 · see citing works
Palmieri, E. M., Holewinski, R. J., McGinity, C. L., Pierri, C. L., Maio, N., Weiss, J. M., Tragni, V., Miranda, K. M., Rouault, T. A., Andrésson, Þ., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40738-4 · Cited by 57 · see citing works
“In addition, NO suppresses mitochondrial aconitase (ACO2) activity, leading to the accumulation of citrate, which upon export to the cytoplasm supports in fl ammatory lipid production 6 – 8 .”
Self-citationWu, J., Mo, J., Xiang, W. D., Shi, X., Guo, L., Li, Y., Bao, Y., & Li, Z. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114471 · Cited by 54 · see citing works
Evaluation of the Molecular Mechanisms of Sepsis Using Proteomics
He, M., Chen, S., & Ding, R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.733537 · Cited by 49 · see citing works
Histone deacetylase 3 regulates microglial function through histone deacetylation
Meleady, L., Towriss, M., Kim, J. S., Bacarac, V., Dang, V., Rowland, M. E., & Ciernia, A. V. (2023) · Epigenetics · doi:10.1080/15592294.2023.2241008 · Cited by 47 · see citing works
“The primary function of NO release by immune cells is to defend against pathogens [42].”
BackgroundDrehmer, D., Luiz, J. P. M., Speck‐Hernandez, C. A., Alves-Filho, J. C., Hussell, T., Townsend, P. A., & Moncada, S. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102350 · Cited by 43 · see citing works
“8 decreased availability of the essential cofactor tetrahydrobiopterin, hence have limited ability to generate NO [54].”
BackgroundNitric Oxide Modulates Metabolic Processes in the Tumor Immune Microenvironment
McGinity, C. L., Palmieri, E. M., Somasundaram, V., Bhattacharyya, D. D., Ridnour, L. A., Cheng, R. Y. S., Ryan, A. E., Glynn, S. A., Thomas, D. D., Miranda, K. M., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137068 · Cited by 41 · see citing works
“, heme and non-heme iron proteins) [35,69] and (2) reactive radicals (i.”
BackgroundSelf-citationFujii, J., & Osaki, T. (2023) · Molecules · doi:10.3390/molecules28020814 · Cited by 42 · see citing works
The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins
Radzinski, M., Oppenheim, T., Metanis, N., & Reichmann, D. (2021) · Biomolecules · doi:10.3390/biom11030469 · Cited by 40 · see citing works
“One of the major sources of cellular nitric oxide molecules is the enzymatic activity of a family of nitric oxide synthetase (NOS) enzymes involved in cell signaling and immune defense [65,66].”
BackgroundCoutinho, L. L., Femino, E. L., González, A. L., Moffat, R. L., Heinz, W. F., Cheng, R. Y. S., Lockett, S., Rangel, M. C., Ridnour, L. A., & Wink, D. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116103 · Cited by 37 · see citing works
“Similarly to oxygen, NO is a gas with diffusible properties that exhibits higher sol-ubility in hydrophobic compartments than in aqueous environments [24].”
BackgroundSelf-citationWu, J., Yu, G., Zhang, X., Staiger, M. P., Gupta, T. B., Yao, H. L., & Wu, X. (2024) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2024.122530 · Cited by 35 · see citing works
iNOS in Macrophage Polarization: Pharmacological and Regulatory Insights
Kang, J.-H., Kim, J., Gim, J., & Lee, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262412056 · Cited by 35 · see citing works
“…the iNOS heme-or BH 4 -binding environment [3]. iNOS is primarily induced in immune cells such as macrophages and T lymphocytes upon exposure to pro-inflammatory signals including lipopolysaccharide (LPS), interleukin-1 β (IL-1 β ), tumor necrosis factor-α (TNF-α ), and interferon-γ (IFN-γ ) [4].”
Medikonda, R. T., Abikenari, M. A., Schonfeld, E., & Lim, M. K. (2025) · Cancers · doi:10.3390/cancers17111881 · Cited by 33 · see citing works
“Glutamine deficiency also polarizes TAMs and MDSCs toward more immunosuppressive phenotypes and promotes Treg expansion [56,58].”
BODIPY-Based NO Probe for Macrophage-Targeted Immunotherapy Response Monitoring
Li, X., Chen, H., Wang, Y., Chen, H., & Gao, Y. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00409 · Cited by 32 · see citing works
Wei, J., Wang, B., Chen, Y., Wang, Q., Ahmed, A. F., Zhang, Y., & Kang, W. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.899797 · Cited by 31 · see citing works
Zhao, W., Xu, D., Hong, W., Zhang, L., Wu, Q., Gao, M., & Wang, J. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109190 · Cited by 30 · see citing works
Chun, J., Mah, S. Y., & Kim, Y. S. (2023) · Plants · doi:10.3390/plants12152845 · Cited by 29 · see citing works
“However, NO is regarded as a proinflammatory mediator that induces inflammation because of excessive production in abnormal physiological situations [20].”
BackgroundThe versatile biochemistry of iron in macrophage effector functions
Behmoaras, J. V. (2020) · FEBS Journal · doi:10.1111/febs.15682 · Cited by 30 · see citing works
Recent Advances in the Development of Non‐Invasive Imaging Probes for Cancer Immunotherapy
Kazim, M., & Yoo, E. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202310694 · Cited by 28 · see citing works
Nitric oxide-based multi-synergistic nanomedicine: an emerging therapeutic for anticancer
Tang, Y., Li, Q., Zhou, Z., Bai, H., Xiao, N., Xie, J., & Li, C. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02929-z · Cited by 27 · see citing works
“Moreover, NO has a complex effect on the activity of natural killer (NK) cells and macrophages [25, 133, 134].”
BackgroundKumar, S. S., Gunda, V., Reinartz, D. M., Pond, K. W., Thorne, C. A., Raj, P. V. S., Johnson, M. D. L., & Wilson, J. E. (2024) · Infection and Immunity · doi:10.1128/iai.00536-23 · Cited by 26 · see citing works
From Gasotransmitter to Immunomodulator: The Emerging Role of Hydrogen Sulfide in Macrophage Biology
Cornwell, A., & Badiei, A. (2023) · Antioxidants · doi:10.3390/antiox12040935 · Cited by 26 · see citing works
“NO interacts with metal-containing proteins and the electron transport chain, altering cellular respiration and regulating energy production [10].”
BackgroundNitric Oxide: The Missing Factor in COVID-19 Severity?
Nikolaidis, A., Kramer, R., & Ostojić, S. M. (2021) · Medical Sciences · doi:10.3390/medsci10010003 · Cited by 25 · see citing works
“Nitric oxide is also essential in macrophage activation in response to infection and to the body’s whole immune response [58],—macrophage cells release NO in response to inflammatory signals—and the NO increase in macrophages results in a multitude of changes in macrophage immunometabolism with multiple implications i…”
BackgroundImpact of nitric oxide in liver cancer microenvironment
Barbeito, S. D., González, R., Cadenas, M., García, L. F., Víctor, V. M., Padillo, F. J., & Muntané, J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.07.006 · Cited by 25 · see citing works
Francolino, R., Martino, M., Caputo, L., Amato, G., Chianese, G., Gargiulo, E., Formisano, C., Romano, B., Ercolano, G., Ianaro, A., et al. (2023) · Antioxidants · doi:10.3390/antiox12081633 · Cited by 25 · see citing works
“To better characterize the anti-inflammatory effect of WRO and CRO, their ability to modulate the NO pathway, one of the major players involved in macrophage activation [36], was also investigated.”
BackgroundLi, B., Tian, J., Wu, C., Li, Z., Qiao, L., Xie, Z., Song, B., Shan, Y., Chen, S., Tang, Y., et al. (2024) · Advanced Materials · doi:10.1002/adma.202405502 · Cited by 25 · see citing works
Peptidoglycan-induced modulation of metabolic and inflammatory responses
Wolf, A. J. (2023) · Immunometabolism · doi:10.1097/in9.0000000000000024 · Cited by 22 · see citing works
“The impact of PGE2 on mitochondrial function may be a result of increased iNOS expression induced by PGE2 leading to high levels of NO production, which has been shown to inhibit mitochondrial complex IV function [56].”
BackgroundMagri, K., Eftedal, I., Magri, V. P., Mátity, L., Azzopardi, C. P., Muscat, S., & Pace, N. P. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.660402 · Cited by 21 · see citing works
“Metabolic differences between murine and human M1 macrophages have been described (Vijayan et al., 2019; Palmieri et al., 2020).”
BackgroundSun, L., Yu, Y., Peng, Y., Wang, D., Wang, S., Noh, I., Fang, R. H., Gao, W., & Zhang, L. (2023) · Small · doi:10.1002/smll.202308327 · Cited by 21 · see citing works
Izu, G. O., Njoya, E. M., Tabakam, G. T., Nambooze, J., Otukile, K. P., Tsoeu, S. E., Fasiku, V. O., Adegoke, A. M., Erukainure, O. L., Mashele, S. S., et al. (2024) · Antioxidants · doi:10.3390/antiox13040456 · Cited by 20 · see citing works
Pradhan, P., Vijayan, V., Liu, B., Martínez–Delgado, B., Matamala, N., Nikolin, C., Greite, R., DeLuca, D. S., Janciauskiene, S. M., Motterlini, R., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103191 · Cited by 20 · see citing works
“Accordingly, a number of metabolic changes in mouse macrophages, including impairment of mitochondrial respiration and mitochondrial function due to inflammatory activation, have been attributed to NO [37,38].”
Dynamic changes of macrophage activation in mice infected with Trichinella spiralis
Sun, Q., Huang, J., Gu, Y., Liu, S., & Zhu, X. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108716 · Cited by 19 · see citing works
A matter of time: temporal structure and functional relevance of macrophage metabolic rewiring
Seim, G. L., & Fan, J. (2022) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2022.02.005 · Cited by 20 · see citing works
“Drug-Free” chitosan nanoparticles as therapeutic for cancer treatment
Iskandar, A., Kim, S., & Wong, T. W. (2024) · Journal of macromolecular science. Part C, Reviews in macromolecular chemistry and physics/Journal of macromolecular science. Reviews in macromolecular chemistry and physics · doi:10.1080/15583724.2024.2323943 · Cited by 19 · see citing works
Hu, X., Li, Y., Cao, Y., Shi, F., & Li, S. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189156 · Cited by 20 · see citing works
Zavadinack, M., Bellan, D. D. L., Bonaldi, M. P. F., Milhorini, S. D. S., Cordeiro, L. M. C., Simas, F. F., & Iacomini, M. (2024) · Food Research International · doi:10.1016/j.foodres.2024.115205 · Cited by 18 · see citing works
Fever-Range Hyperthermia Promotes Macrophage Polarization towards Regulatory Phenotype M2b
Kozłowski, H. M., Sobocińska, J., Jędrzejewski, T., Maciejewski, B., Dzialuk, A., & Wrotek, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417574 · Cited by 18 · see citing works
“To protect the body against infections, macrophages produce various molecules, including reactive oxygen species (ROS) and nitrogen oxide (NO) [23,24].”
BackgroundBian, B., Miao, X., Zhao, X., Lai, C., Chen, Y., Zhou, M., & Yong, Q. (2024) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2024.122006 · Cited by 18 · see citing works
Polarization of M2 Tumor-Associated Macrophages (TAMs) in Cancer Immunotherapy
Bui, I., & Bonavida, B. (2024) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.2024053830 · Cited by 18 · see citing works
Tomal, F., Sausset, A., Vern, Y. L., Sedano, L., Técher, C., Lacroix‐Lamandé, S., Laurent, F., Silvestre, A., & Bussière, F. I. (2023) · Gut Pathogens · doi:10.1186/s13099-023-00591-8 · Cited by 18 · see citing works
Mangmool, S., Duangrat, R., Rujirayunyong, T., & Anantachoke, N. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.117997 · Cited by 18 · see citing works
Bei, H., Ji, X., Xu, T., Chen, Z., Lam, C.-H., Zhou, X., Yang, Y., Zhang, Y., Wen, C., Liu, Y., et al. (2024) · Composites Part B Engineering · doi:10.1016/j.compositesb.2024.111410 · Cited by 18 · see citing works
Endothelial cell, myeloid, and adaptive immune responses in SARS‐CoV‐2 infection
Degauque, N., Haziot, A., Brouard, S., & Mooney, N. (2021) · The FASEB Journal · doi:10.1096/fj.202100024r · Cited by 14 · see citing works
Куркин, Д. В., Абросимова, Е. Е., Bakulin, D. A., Kovalev, N. S., Дубровина, М. А., Borisov, A. V., Strygin, A. V., Morkovin, E. I., & Tyurenkov, I. N. (2022) · Pharmacy & Pharmacology · doi:10.19163/2307-9266-2022-10-2-130-153 · Cited by 20 · see citing works
Sulfated polysaccharides as multi target molecules to fight COVID 19 and comorbidities
Barriga, E. J. C., & Fields, R. D. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e13797 · Cited by 17 · see citing works
“NO is the critical effector molecule to activate macrophages, as seen in murine cells (Palmieri et al., 2020).”
Mycobacterium tuberculosis and its clever approaches to escape the deadly macrophage
Krishnan, V., Nath, S., Nair, P., & Das, B. (2023) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-023-03735-9 · Cited by 17 · see citing works
Pro-inflammatory macrophage activation does not require inhibition of oxidative phosphorylation
Ball, A. B., Jones, A. E., Nguyễn, K. B., Rios, A., Marx, N., Hsieh, W. Y., Yang, K., Desousa, B. R., Kim, K. K. O., Veliova, M., et al. (2025) · EMBO Reports · doi:10.1038/s44319-024-00351-y · Cited by 22 · see citing works
“Other reports, however, have demonstrated preserved or even enhanced pro-in fl ammatory macrophage function under conditions where oxidative phosphorylation remains functional (Cao et al, 2020; Bailey et al, 2019; Palmieri et al, 2020a; Vijayan et al, 2019).”
InfluentialRuksiriwanich, W., Linsaenkart, P., Khantham, C., Muangsanguan, A., Sringarm, K., Jantrawut, P., Prom‐u‐thai, C., Jamjod, S., Yamuangmorn, S., Arjin, C., et al. (2023) · Plants · doi:10.3390/plants12030653 · Cited by 16 · see citing works
Park, M. A., Park, M., Jang, H., Lee, S. H., Hwang, Y. M., Park, S., Shin, D., & Kim, Y. (2024) · PLoS ONE · doi:10.1371/journal.pone.0299792 · Cited by 16 · see citing works
Moses, J. C., Sapkota, A., Wu, Y., Martinez, I., Handa, H., & Brisbois, E. J. (2025) · Small · doi:10.1002/smll.202411984 · Cited by 16 · see citing works
Harnessing stimuli-responsive NO nanomaterials for advanced multi-disease therapy
Zhang, J., Guo, H., Tang, L., Liu, J., Fang, Q., Yang, D., & Fan, W. (2025) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2025.216540 · Cited by 17 · see citing works
The M2 Macrophages Importance Role in Psoriasis
Alshihmani, A. H. H., Mahmoudi, M., Kheder, R., Fadaee, A., & Esmaeili, S.-A. (2025) · Immunity, Inflammation and Disease · doi:10.1002/iid3.70211 · Cited by 17 · see citing works
Macrophages from naked mole-rat possess distinct immunometabolic signatures upon polarization
Gorshkova, E. A., Gubernatorova, E. O., Dvorianinova, E. M., Yurakova, T. R., Marey, M. V., Averina, O. A., Holtze, S., Hildebrandt, T. B., Dmitriev, A. A., Drutskaya, M. S., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1172467 · Cited by 10 · see citing works
Unraveling the complexities of diet induced obesity and glucolipid dysfunction in metabolic syndrome
Dutta, B., Tripathy, A., Archana, P. R., & Kamath, S. U. (2025) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-025-01837-y · Cited by 17 · see citing works
Li, X., Sun, X., Chen, H., Wang, Y., Chen, H., & Gao, Y. (2024) · ACS Nano · doi:10.1021/acsnano.4c00650 · Cited by 14 · see citing works
Sanjay, S., Yoon, N. Y., Park, E., & Lee, H. (2024) · Applied Sciences · doi:10.3390/app14051794 · Cited by 13 · see citing works
Li, S., Cui, X., Cao, Y., & Sun, J. (2024) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2024.109469 · Cited by 13 · see citing works
Zeng, J., Liu, J., Zhao, N., Wong, I. N., & Huang, R. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134450 · Cited by 14 · see citing works
Ma, D., Zhang, Y., Zhang, J., Shi, J., Gao, S., Long, F., Wang, X., Pu, X., Sun, J., Liang, S., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1501174 · Cited by 12 · see citing works
Cho, H., Park, J.-H., Olawuyi, I. F., Nam, J., & Lee, W. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.142519 · Cited by 13 · see citing works
Smith, K. W. Y., Fung, S. L., Wu, H.-F., Chiesa, I., Vozzi, G., Maria, C. D., & Gottardi, R. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1495613 · Cited by 12 · see citing works
Wu, Y., Chen, Z., Chen, X., Hu, Y., & Ma, Y. (2025) · Redox Report · doi:10.1080/13510002.2025.2564593 · Cited by 11 · see citing works
“These inhibitory effects are dependent on the presence of NO [145].”
Mucorales fungi suppress nitric oxide production by macrophages
Soare, A. Y., & Bruno, V. M. (2023) · mBio · doi:10.1128/mbio.02848-23 · Cited by 11 · see citing works
de Sousa, K. M., Linklater, D. P., Baulin, V. A., Dekiwadia, C. D., Mayes, E. L. H., Murdoch, B. J., Le, P. H., Fluke, C. J., Boshkovikj, V., Wen, C., et al. (2024) · Advanced Materials Interfaces · doi:10.1002/admi.202301021 · Cited by 11 · see citing works
Immunomodulatory Activities of Ammodytes personatus Egg Lipid in RAW264.7 Cells
Lim, J. H., Choi, G. S., Monmai, C., Rod–in, W., Jang, A.-Y., & Park, W. J. (2021) · Molecules · doi:10.3390/molecules26196027 · Cited by 11 · see citing works
“The cell surface receptors respond to external stimuli such as lipopolysaccharides (LPS) or bacteria, which induce the increased synthesis of pro-inflammatory cytokines and NO to eliminate external invaders [7] via activation of the mitogen-activated protein kinase (MAPK) and nuclear factor (NF)-κB [8,9].”
BackgroundDai, X., Yang, L., Zhang, Y. J., Li, Y., Liu, X., Xu, Q., & Gao, F. (2023) · ACS Macro Letters · doi:10.1021/acsmacrolett.3c00052 · Cited by 10 · see citing works
Switzer, C. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16302 · Cited by 10 · see citing works
“Furthermore, recent work elucidating the role of NO signalling on cancer and immune cell metabolism have revealed that NO promotes many aspects of an aggressive cancer cell phenotype (Palmieri et al., 2020).”
Piccionello, A. P., Sassaroli, S., Pennasilico, L., Rossi, G., Cerbo, A. D., Riccio, V., Bella, C. D., Laghi, L., Angelini, M., Marini, C., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-54144-3 · Cited by 10 · see citing works
Models of Trigeminal Activation: Is There an Animal Model of Migraine?
Spekker, E., Fejes-Szabó, A., & Nagy-Grócz, G. (2024) · Brain Sciences · doi:10.3390/brainsci14040317 · Cited by 10 · see citing works
“Macrophages and other immune cells express iNOS in response to inflammatory signals, leading to the production of large amounts of NO [95].”
BackgroundGrubwieser, P., Böck, N., Soto, E. K., Hilbe, R., Moser, P. L., Seifert, M., Dichtl, S., Govrins, M. A., Posch, W., Sonnweber, T., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1508727 · Cited by 10 · see citing works
Wang, G., Zhang, W., Cheng, K., Chen, T., Huang, Z., & Xie, J. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.105777 · Cited by 11 · see citing works
An ultra-rare missense variant in the KIF1B gene linked to autoinflammatory Menière’s disease
Cruz‐Granados, P., Bortoletto, G. B., Arán, I., de Jesús, V. R., & Lopez-Escamez, J. A. (2025) · npj Genomic Medicine · doi:10.1038/s41525-025-00503-6 · Cited by 10 · see citing works
“Nitricoxide (NO) is a byproduct of the immune myeloid cells' in fl ammatory response 30 .”
Choromańska, B., Myśliwiec, P., Kozłowski, T., Łuba, M., Wojskowicz, P., Dadan, J., Myśliwiec, H., Choromańska, K., Makarewicz, K., Zalewska, A., et al. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s337910 · Cited by 10 · see citing works
“of NO, which increase, on a positive feedback, the formation of cytokines, chemokines, and growth factors.(49) This”
BackgroundHu, Y., Lin, Z., Fu, H., Xia, J., Xiong, W., & Li, G. (2022) · Cellular and Molecular Biology · doi:10.14715/cmb/2022.68.4.4 · Cited by 10 · see citing works
Nitric oxide and thiols: Chemical biology, signalling paradigms and vascular therapeutic potential
Dent, M. R., & DeMartino, A. W. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16274 · Cited by 10 · see citing works
“In some circumstances, the relatively electrophilic RSNO sulfur atom may be subject to nucleophilic attack by a thiolate nucleophile in a process called S -thiolation, generating a disulfide and an equivalent of nitroxyl (HNO), another signalling species (Equation 7) (Ford & Miranda, 2020; Hogg, 2000; Wolhuter et al.,…”
InfluentialBőgel, G., Murányi, J., Szokol, B., Kukor, Z., Móra, I., Kardon, T., Őrfi, L., & Hrabák, A. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e08670 · Cited by 10 · see citing works
A Mitochondria-Targeted Nitric Oxide Probe for Multimodality Imaging of Macrophage Immune Responses
Wen, Y., Wu, X., Wu, W., Feng, T., Pan, Y., He, Y., Ji, L., & Chao, H. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c00083 · Cited by 9 · see citing works
Alcarranza, M., Alarcón‐de‐la‐Lastra, C., Recio, R., Fernández, I., Martínez, M. L., & Villegas, I. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c02943 · Cited by 9 · see citing works
Tedeschi, G., Navarro, M. X., Scipioni, L., Sondhi, T. K., Prescher, J. A., & Digman, M. A. (2024) · Chemical & Biomedical Imaging · doi:10.1021/cbmi.4c00049 · Cited by 9 · see citing works
“32,40,41 M2 macro-Table phage polarization relies on the phosphorylation of signal transducer and activator of transcription 6 (STAT6).”
Li, G., Wei, X., Lv, K., Xie, D., Liu, M., Xu, Y., Ma, D., & Jiao, G. (2025) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2025.123578 · Cited by 9 · see citing works
Chen, L., Nie, F., Jiang, H., Gao, T., Yu, C., Xu, J., & Guo, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.145218 · Cited by 9 · see citing works
Zabłocka, A., Jakubczyk, D., Leszczyńska, K., Pacyga-Prus, K., Macała, J., & Górska, S. (2023) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-023-10093-3 · Cited by 9 · see citing works
“NO, synthesized from L-arginine by NOS (NO synthase), is an endogenous gas, which fulfills many biological functions, including metabolic regulator, signaling, and effector molecule [29, 30].”
BackgroundDwijayanti, D. R., Widyananda, M. H., Hermanto, F. E., Soewondo, A., Afiyanti, M., & Widodo, N. (2024) · Food and Agricultural Immunology · doi:10.1080/09540105.2024.2351360 · Cited by 10 · see citing works
“Macrophage secretes nitric oxide (NO) in response to pathogen infection (Palmieri et al., 2020).”
Allen, C. H., Ahmed, D., Raiche-Tanner, O., Chauhan, V., Mostaço-Guidolin, L. B., Cassol, E., & Murugkar, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-93043-9 · Cited by 9 · see citing works
Li, X., Guo, F., Deng, J., Li, J., Zhang, J., Fu, M. C., & Fan, H. (2024) · Immunity Inflammation and Disease · doi:10.1002/iid3.70064 · Cited by 8 · see citing works
- Authors
- Palmieri, E. M., McGinity, C., Wink, D. A., & McVicar, D. W.
- Affiliations
- National Cancer Institute (US)
- Corresponding author
- McVicar, Daniel W.
- Venue
- Metabolites
- Publisher
- MDPI AG
- Published
- 2020-10-26
- Volume
- 10
- Issue
- 11
- Pages
- 429
- ISSN
- 2218-1989 (ISSN-L)
- PMC
- PMC7693038
- OpenAlex
- W3096340664
- Cited by
- 237
- References
- 252
- Citations by year
- 2026: 40 · 2025: 59 · 2024: 56 · 2023: 46 · 2022: 15 · 2021: 20 · 2020: 1
- FWCI
- 2.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Metabolites (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Cancer Institute (ZIA BC 010300, ZIA BC 010899)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune cells in cancer
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- nitric oxide, macrophage immunometabolism, M1 macrophages, reactive nitrogen species, electron transport chain, heme proteins, cellular respiration, macrophage metabolic reprogramming, inflammation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review