Red not dead: signaling in and from erythrocytes
Abstract
The oxygen required to meet metabolic needs of all tissues is delivered by the erythrocyte, a small, flexible cell which, in mammals, is devoid of a nucleus and mitochondria. Despite its simple appearance, this 'bag of hemoglobin' has an important role in its own distribution, enabling the delivery of oxygen to precisely meet localized metabolic need. When an erythrocyte enters an area in which tissue oxygen demand exceeds supply, a signaling pathway is activated resulting in the release of adenosine 5'-triphosphate (ATP). This ATP acts in a paracrine fashion to increase vascular caliber resulting in increased oxygen delivery. Defects in this pathway are found in erythrocytes of humans with type 2 diabetes (DM2) and could contribute to the perfusion abnormalities in skeletal muscle associated with this disease.
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All four mammalian molybdenum-containing enzymes (XO, AO, sulfite oxidase, and mARC) are able to reduce nitrite at different intrinsic rates.
“Subsequently, several reports have shown that all mammalian Mo-containing enzymes [XO, aldehyde oxidase (AO), sulfite oxidase, and the mitochondrial amidoxime-reducing component (mARC)] are able to reduce nitrite at different intrinsic rates (Table 4) (575, 880, 990).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [880]
Both mARC enzymes can reduce nitrite to NO in a process very sensitive to oxygen-mediated inhibition.
“Both mARC enzymes can reduce nitrite to NO in a process very sensitive to oxygen-mediated inhibition (Table 4) (880).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [880]
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“Other RBC and Hb fractional saturationdependent mechanisms for stimulating NO signalling have been proposed involving SNO-Hb or adenosine triphosphate (ATP) release.(57,61) These compounds have also been suggested to play a role in vasodilatory responses attributed to nitrite.”
BackgroundHomeostasis of Extracellular ATP in Human Erythrocytes
Montalbetti, N., Denis, M. F. L., Pignataro, O. P., Kobatake, E., Lazarowski, E. R., & Schwarzbaum, P. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.221713 · Cited by 67 · see citing works
Grygorczyk, R., & Orlov, S. N. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01110 · Cited by 63 · see citing works
“Since CFTR activity is regulated by cAMP-dependent PKA, it has been also hypothesized that shear stress- and hypoxia-induced ATP release involves activation of the cAMP signaling pathway (Sprague et al., 2007).”
BackgroundErythrocytes as controllers of perfusion distribution in the microvasculature of skeletal muscle
Sprague, R. S., Bowles, E. A., Achilleus, D., & Ellsworth, M. L. (2010) · Acta Physiologica · doi:10.1111/j.1748-1716.2010.02182.x · Cited by 62 · see citing works
Self-citationSridharan, M. R., Bowles, E. A., Richards, J. P., Krantic, M., Davis, K. L., Dietrich, K. A., Stephenson, A. H., Ellsworth, M. L., & Sprague, R. S. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00998.2011 · Cited by 60 · see citing works
Self-citationDybaś, J., Alcicek, F. C., Wajda, A., Kaczmarska, M. J., Zimna, A., Bułat, K., Blat, A., Степаненко, Т., Mohaissen, T., Szczęsny-Małysiak, E., et al. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2021.116481 · Cited by 58 · see citing works
“[117] Deformation-induced ATP release from RBCs may activate the purinergic receptors on the endothelium and result in vasodilation that causes increased perfusion of the tissue/ organ [118].”
BackgroundIkeda, N., Murata, S., Maruyama, T., Tamura, T., Nozaki, R., Kawasaki, T., Fukunaga, K., Oda, T., Sasaki, R., Homma, M., et al. (2011) · Hepatology Research · doi:10.1111/j.1872-034x.2011.00893.x · Cited by 58 · see citing works
Regulation of Coronary Blood Flow
Goodwill, A. G., Dick, G. M., Kiel, A. M., & Tune, J. D. (2017) · Comprehensive physiology · doi:10.1002/j.2040-4603.2017.tb00750.x · Cited by 56 · see citing works
Regulation of cAMP by phosphodiesterases in erythrocytes
Adderley, S., Sprague, R. S., Stephenson, A. H., & Hanson, M. S. (2010) · Pharmacological Reports · doi:10.1016/s1734-1140(10)70303-0 · Cited by 55 · see citing works
Self-citationExtracellular hemoglobin: the case of a friend turned foe
Quaye, I. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00096 · Cited by 53 · see citing works
“In these compounds heme (type b) is non-covalently coordinated to each globin chain (alpha and beta) through Fe II.”
BackgroundHelenius, M., Vattulainen, S., Orcholski, M. E., Aho, J., Komulainen, A., Taimen, P., Wang, L., Pérez, V. D. J., Koskenvuo, J. W., & Alastalo, T. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00340.2014 · Cited by 52 · see citing works
“In blood vessels, ATP is released from ECs (5, 8, 57), SMCs (28), fibroblasts (21), erythrocytes (48), platelets (4), neutrophils (17), monocytes/macrophages (54), and perivascular nerves (52).”
BackgroundVázquez, B. Y. S., Wettstein, R., Cabrales, P., Tsai, A. G., & Intaglietta, M. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.04.020 · Cited by 50 · see citing works
Alternate and Additional Functions of Erythrocyte Hemoglobin
Kosmachevskaya, O. V., & Topunov, A. F. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918120155 · Cited by 46 · see citing works
Red blood cell age and potentiation of transfusion‐related pathology in trauma patients
Weinberg, J. A., Barnum, S. R., & Patel, R. P. (2011) · Transfusion · doi:10.1111/j.1537-2995.2011.03098.x · Cited by 45 · see citing works
“These three mechanisms, their potential interrelationships, and regulation have been discussed extensively in several articles to which the reader is referred.(23-35) Important to this discussion is the potential for dysfunction in all of these proposed mechanisms during RBC storage leading to compromised NO signaling.”
BackgroundDufour, S. P., Patel, R. P., Brandon, A., Teng, X., Pearson, J., Barker, H., Ali, L., Yuen, A. H. Y., Smolenski, R. T., & González-Alonso, J. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00389.2010 · Cited by 45 · see citing works
“Introduction The erythrocyte has recently been identified as a key player in the regulation of the local processes matching O2 delivery to tissue aerobic energy demand in vessel preparations in vitro (14, 58) and in animals (56, 57) and humans in vivo (25, 26).”
BackgroundExercise intolerance in Type 2 diabetes: is there a cardiovascular contribution?
Poitras, V. J., HUDSON, R. W., & Tschakovsky, M. E. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00070.2017 · Cited by 45 · see citing works
“1 Red blood cell (RBC)-O2 sensor Increases in skeletal muscle O2 demand results in localized red blood cell (RBC) Hb desaturation which triggers proportional ATP release from the RBC (57).”
BackgroundInfluentialMarginedas-Freixa, I., Alvarez, C. L., Moras, M., Denis, M. F. L., Hattab, C., Hallé, F., Bihel, F. J. ‐., Mouro-Chanteloup, I., Lefevre, S. D., Kim, C. L. V., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-29885-7 · Cited by 40 · see citing works
Kinetics of extracellular ATP in mastoparan 7-activated human erythrocytes
Denis, M. F. L., Incicco, J. J., Espelt, M. V., Verstraeten, S. V., Pignataro, O. P., Lazarowski, E. R., & Schwarzbaum, P. J. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.033 · Cited by 38 · see citing works
“Human erythrocytes release ATP upon their exposure to β-adrenergic agonists, mechanical deformation, reduced oxygen tension, or acidosis [4].”
Hanson, M. S., Stephenson, A. H., Bowles, E. A., & Sprague, R. S. (2010) · Experimental Biology and Medicine · doi:10.1258/ebm.2009.009206 · Cited by 38 · see citing works
Self-citationNeuraminidase alters red blood cells in sepsis
Piagnerelli, M., Boudjeltia, K. Z., Rapotec, A., Richard, T., Brohée, D., Babar, S., Bouckaert, V., Simon, A.-C., Toko, J.-P., Walravens, T., et al. (2009) · Critical Care Medicine · doi:10.1097/ccm.0b013e31819cebbe · Cited by 36 · see citing works
Kallakunta, V. M., Slama‐Schwok, A., & Mutus, B. (2013) · Redox Biology · doi:10.1016/j.redox.2013.07.002 · Cited by 36 · see citing works
“The ATP is released from RBC not only when RBC deoxygenates but also in response to mechanical deformation when RBC travel through narrow vessels [11,12].”
Red blood cells (RBCs), epoxyeicosatrienoic acids (EETs) and adenosine triphosphate (ATP)
Jiang, H., Anderson, G. D., & McGiff, J. C. (2010) · Pharmacological Reports · doi:10.1016/s1734-1140(10)70302-9 · Cited by 34 · see citing works
“RBCs generate millimolar amounts of ATP, which exceeds the ATP-generating ability of most tissues [45].”
Oxygen‐dependent ion transport in erythrocytes
Bogdanova, A. Y., Berenbrink, M., & Nikinmaa, M. (2008) · Acta Physiologica · doi:10.1111/j.1748-1716.2008.01934.x · Cited by 33 · see citing works
ATP, an extracellular signaling molecule in red blood cells: A messenger for malaria?
Langsley, G., & Ramdani, G. (2014) · Biomedical Journal · doi:10.4103/2319-4170.132910 · Cited by 33 · see citing works
Scarfı̀, S. (2014) · World Journal of Stem Cells · doi:10.4252/wjsc.v6.i2.153 · Cited by 31 · see citing works
Amyloid peptide inhibits ATP release from human erythrocytes
Misiti, F., Orsini, F., Clementi, M. E., Masala, D., Tellone, E., Galtieri, A., & Giardina, B. (2008) · Biochemistry and Cell Biology · doi:10.1139/o08-139 · Cited by 31 · see citing works
Hanson, M. S., Ellsworth, M. L., Achilleus, D., Stephenson, A. H., Bowles, E. A., Sridharan, M. R., Adderley, S., & Sprague, R. S. (2009) · Microcirculation · doi:10.1080/10739680902855218 · Cited by 30 · see citing works
“Although several mechanisms have been proposed to explain this physiologically important mechanism, none fully explain the observed sensitivity of the precise matching of blood flow (O2 supply) with tissue O2 requirements [11,12,18,47].”
BackgroundResultSelf-citationDynamic Regulation of Cell Volume and Extracellular ATP of Human Erythrocytes
Denis, M. F. L., Alvarez, H. A., Lauri, N., Alvarez, C. L., Chara, O., & Schwarzbaum, P. J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158305 · Cited by 30 · see citing works
“In the vascular lumen, rbc-derived ATP produced not only local vasodilation, but also dilation that was conducted to upstream arterioles [1,18].”
BackgroundInfluentialSridharan, M. R., Sprague, R. S., Adderley, S., Bowles, E. A., Ellsworth, M. L., & Stephenson, A. H. (2010) · Experimental Biology and Medicine · doi:10.1258/ebm.2010.010118 · Cited by 29 · see citing works
Self-citationRole Ca2+ in Mechanisms of the Red Blood Cells Microrheological Changes
Muravyov, A. V., & Tikhomirova, I. A. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_47 · Cited by 26 · see citing works
Detection and possible role of proteasomes in the bronchoalveolar space of the injured lung
Majetschak, M., Sorell, L. T., Patricelli, T., Seitz, D., & Knoeferl, M. (2009) · Physiological Research · doi:10.33549/physiolres.931526 · Cited by 26 · see citing works
Zidova, Z., Kapralova, K., Kořalková, P., Mojzíková, R., Doležal, D., Divoký, V., & Horváthová, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000369665 · Cited by 25 · see citing works
Franke, R., Scharnweber, T., Fuhrmann, R., Wenzel, F., Krüger, A., Mrowietz, C., & Jung, F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089512 · Cited by 25 · see citing works
“Band3 is described to constitute a centre organized into complexes for gas transport [47–50], for cation efflux pumping (anion exchanger) [51–53], for glycolysis [54,55], for the control of cell volume [56] and of erythrocyte life span (senescence) [57], where most probably further complexes exist to cope with mechani…”
BackgroundJiang, H., Anderson, G. D., & McGiff, J. C. (2011) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2011.11.008 · Cited by 24 · see citing works
Knebel, S. M., Elrick, M. M., Bowles, E. A., Zdanovec, A. K., Stephenson, A. H., Ellsworth, M. L., & Sprague, R. S. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213498981 · Cited by 23 · see citing works
“Thus, PGI2 or its analogs, when administered intravenously, can stimulate vasodilation via direct effects on vascular smooth muscle, as well as indirectly by promoting the release of ATP from circulating erythrocytes.(6,15,16) In erythrocytes, IPR-mediated ATP release requires increases in intracellular cAMP.”
BackgroundSelf-citationJensen, F. B., Agnisola, C., & Novak, I. (2008) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2008.11.007 · Cited by 22 · see citing works
Quds, R., Iqbal, Z., Arif, A., & Mahmood, R. (2023) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2023.105453 · Cited by 21 · see citing works
Mechanisms of ATP Release and Inactivation
Burnstock, G., & Verkhratsky, A. (2012) · Springer eBooks · doi:10.1007/978-3-642-28863-0_4 · Cited by 21 · see citing works
Harder, L., & Boshkov, L. (2010) · Critical Care Clinics · doi:10.1016/j.ccc.2010.01.002 · Cited by 21 · see citing works
“When oxygen content falls, red cells can regulate blood flow by releasing mediators like nitric oxide (NO)(56,57) and ATP, which can induce local vasodilation.(27,55,57,58) Hemoglobin itself may act as a tissue oxygen sensor.”
BackgroundUğurel, E., Pişkin, Ş., Aksu, A. C., Eser, A., & Yalçın, Ö. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2019.01559 · Cited by 18 · see citing works
“This would confer RBCs a central role in the process of matching local O2 supply with O2 demand, plausibly by regulating their own properties and functions (Sprague et al., 2007).”
BackgroundRevisiting the question of nucleated versus enucleated erythrocytes in birds and mammals
Yap, K. N., & Zhang, Y. (2021) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00276.2020 · Cited by 18 · see citing works
Sega, M. F., Chu, H., Christian, J. A., & Low, P. S. (2015) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2015.07.004 · Cited by 17 · see citing works
Jeppesen, T. D., Madsen, K. L., Poulsen, N. S., Løkken, N., & Vissing, J. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10081796 · Cited by 16 · see citing works
Vascular disease in pre-diabetes: new insights derived from systems biology.
Sprague, R. S., & Ellsworth, M. L. (2010) · Europe PMC (PubMed Central) · Cited by 15 · see citing works
Self-citationProteomics-based identification of hypoxia-sensitive membrane-bound proteins in rat erythrocytes
Sidorenko, S. V., Ziganshin, R., Luneva, O. G., Deev, L. I., Alekseeva, N. V., Maksimov, G. V., Grygorczyk, R., & Orlov, S. N. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.06.008 · Cited by 15 · see citing works
ATP effects on response of human erythrocyte membrane to high pressure
Yamaguchi, T., & Fukuzaki, S. (2019) · Biophysics and Physicobiology · doi:10.2142/biophysico.16.0_158 · Cited by 14 · see citing works
“Moreover, when tissue oxygen is demanded, ATP released from the erythrocyte is utilized to increase vascular caliber so that oxygen delivery is facilitated [8,9].”
BackgroundFranke, R., Krüger, A., Scharnweber, T., Wenzel, F., & Jung, F. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150916134 · Cited by 13 · see citing works
“Band 3 is described to constitute a center organized into complexes for gas transport [41–44], anion exchanger, for glycolysis [43,45,46], for the control of cell volume [47] and of erythrocyte life span (senescence) [48], where most probably further complexes exist to cope with mechanical deformation [49], and haemos…”
BackgroundExploring the microvascular impact of red blood cell transfusion in intensive care unit patients
Hariri, G., Bourcier, S., Marjanovic, Z., Joffre, J., Lemarie, J., Lavillegrand, J., Charue, D., Duflot, T., Bigé, N., Baudel, J.-L., et al. (2019) · Critical Care · doi:10.1186/s13054-019-2572-9 · Cited by 13 · see citing works
Patch-Clamp Analysis of Membrane Transport in Erythrocytes
Bouyer, G., Thomas, S. L. Y., & Ege, S. (2012) · InTech eBooks · doi:10.5772/37279 · Cited by 10 · see citing works
“Indeed, description of these different channel types in RBCs, using patch clamp techniques, has raised many questions: how do they interfere with the regulation of intracellular homeostasis, cell differentiation or death? But their presence also fits with a new vision of red cells, being much more than an empty bag of…”
BackgroundCooperation of erythrocytes with leukocytes in immune response of a teleost Oplegnathus fasciatus
Jeong, J.-M., An, C. M., Kim, M., & Park, C. (2016) · Genes & Genomics · doi:10.1007/s13258-016-0437-z · Cited by 10 · see citing works
“Erythrocytes transport oxygen and carbon dioxide, which play significant roles in prevention of oxidative stress and control of blood flow to the skeletal muscles (Richards et al. 1998; Sprague et al. 2007; Tsantes et al. 2006).”
BackgroundMarginedas-Freixa, I., Alvarez, C. L., Moras, M., Hattab, C., Bouyer, G., Chêne, A., Lefevre, S. D., Kim, C. L. V., Bihel, F. J. ‐., Schwarzbaum, P. J., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103098 · Cited by 10 · see citing works
“ATP release from RBCs contributed to the control of the blood flow and tissue-oxygenation [32].”
BackgroundZhan, X., Zhong, X. Y., Choi, J. H., Su, L., Wang, J., Nair‐Gill, E., Anderton, P. D., Li, X., Tang, M., Russell, J. L., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020001762 · Cited by 9 · see citing works
“Erythrocytes can release ATP into plasma via a nonlytic pathway or via intravascular hemolysis under specific circumstances.(44,45) Although intracellular levels of ATP could reach millimolar concentrations, the extracellular ATP concentration in plasma is maintained at 2 or 3 magnitudes of order lower by ectonucleoti…”
BackgroundTownsend, A. D., Sprague, R. S., & Martin, R. S. (2019) · Electroanalysis · doi:10.1002/elan.201900157 · Cited by 9 · see citing works
Self-citationAlcicek, F. C., Mohaissen, T., Bułat, K., Dybaś, J., Szczęsny-Małysiak, E., Kaczmarska, M. J., Franczyk‐Żarów, M., Kostogrys, R. B., & Marzec, K. M. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.839323 · Cited by 7 · see citing works
Sueyoshi, K., Sumi, Y., Inoue, Y., Kuroda, Y., Ishii, K., Nakayama, H., Iwabuchi, K., Kurishita, Y., Shigemitsu, H., Hamachi, I., et al. (2016) · Annals of Intensive Care · doi:10.1186/s13613-016-0175-z · Cited by 6 · see citing works
The Role of Platelets in Sickle Cell Disease
Brzóska, T., Kato, G. J., & Sundd, P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813456-6.00031-x · Cited by 6 · see citing works
Sprague, R. S., & Ellsworth, M. L. (2012) · Microcirculation · doi:10.1111/j.1549-8719.2012.00158.x · Cited by 6 · see citing works
Self-citationIntravascular hemolysis: the sacrifice of few…
Thomas, S. L. Y. (2014) · Blood · doi:10.1182/blood-2014-08-595447 · Cited by 6 · see citing works
Man, Y., Wu, D. H., An, R., Wei, P., Monchamp, K., Goreke, U., Sekyonda, Z., Wulftange, W. J., Federici, C., Bode, A., et al. (2023) · Sensors & Diagnostics · doi:10.1039/d2sd00095d · Cited by 5 · see citing works
Kay, L., Tokarska-Schlattner, M., Quenot-Carrias, B., Goudet, B., Bugert, P., Arnold, H., Scheuerbrandt, G., & Schlattner, U. (2017) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2017.03.008 · Cited by 5 · see citing works
Buerk, D. G., Liu, Y., Zaccheo, K. A., Barbee, K. A., & Jaron, D. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01053 · Cited by 5 · see citing works
“They suggest that a significant amount of NO might be transferred to the vasculature from this pool, avoiding quenching by Hb. Alternately, there is evidence that the RBC releases ATP during hypoxia, which can in turn stimulate NO production by eNOS (Sprague et al., 2007; Cao et al., 2009).”
BackgroundBirulina, Y. G., Петрова, И. В., Rozenbaum, Y. A., Shefer, E. A., Smagliy, L. V., Носарев, А. В., & Gusakova, S. V. (2019) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-019-04561-6 · Cited by 5 · see citing works
ATP release from erythrocytes: A role of adenosine1
Misiti, F., Carelli‐Alinovi, C., & Rodio, A. (2022) · Clinical Hemorheology and Microcirculation · doi:10.3233/ch-221379 · Cited by 5 · see citing works
“Previously, it was reported that in pathological erythrocytes, low basal cAMP levels correlate with a reduced ability to release ATP from erythrocytes under hypoxic conditions [37].”
Mysteries in the Local Control of Blood Flow
Chilian, W. M., Yin, L., & Ohanyan, V. A. (2012) · Circulation Research · doi:10.1161/circresaha.112.273060 · Cited by 5 · see citing works
Chmielewski, P. P., Strzelec, B., Chmielowiec, J., Chmielowiec, K., & Borysławski, K. (2017) · Anthropological Review · doi:10.1515/anre-2017-0012 · Cited by 4 · see citing works
“…acting as acid-base buffer, producing nitric oxide, S-nitrosothiol, and certain enzymes, promoting normal blood flow through releasing substances that relax and dilate blood vessels, etc. (Richards et al. 1998; Fonseca et al. 2003; Sprague et al. 2007; Morera and MacKenzie 2011; Jelkmann 2012).”
BackgroundTikhonova, L. A., Maevsky, E. I., Montoliú, C., & Kosenko, E. A. (2025) · Biomolecules · doi:10.3390/biom15040588 · Cited by 3 · see citing works
“The steady-state level of ATP depends not only on the rate of its formation but also on the activation of endogenous ATP-dependent reactions and on the release of ATP following exposure to β -adrenergic stimulation, reduced erythrocyte deformability and oxygen tension, or acidosis [110].”
Hypoxia induces robust ATP release from erythrocytes in ApoE-LDLR double-deficient mice
Alcicek, F. C., Dybaś, J., Bułat, K., Mohaissen, T., Szczęsny-Małysiak, E., Franczyk‐Żarów, M., & Marzec, K. M. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1497346 · Cited by 3 · see citing works
“…that investigated hypoxia-induced ATP release from RBCs (Ellsworth et al., 1995; Dietrich et al., 2000; Olearczyk et al., 2004b; Sprague et al., 2009; Sprague et al., 2010) and uncovered the responsible components in its signal-transduction pathway (Sprague et al., 2007; Sridharan et al., 2010).”
Evolution of potential biomarkers of acute muscle injury after physical exercise
Chielle, E. O., Granella, L. W., Maziero, J. S., Vidigal, T. M. A., Mallmann, B. L. K., & Karal, J. (2019) · Brazilian Journal of Pharmaceutical Sciences · doi:10.1590/s2175-97902019000117594 · Cited by 3 · see citing works
Anhidrasa carbónica, nuevas perspectivas
Monroy, L. E., & Vargas, M. P. S. (2010) · NCT Neumología y Cirugía de Tórax · Cited by 3 · see citing works
The red blood cell: An underestimated actor in alterations of the microcirculation*
Piagnerelli, M. (2009) · Critical Care Medicine · doi:10.1097/ccm.0b013e318196fd86 · Cited by 3 · see citing works
Inoue, M. (2025) · The Receptors · doi:10.1007/978-3-031-81991-9_7 · Cited by 2 · see citing works
Balzan, S., Carpi, A., Evangelista, M., Nicolini, G., Pollastri, A., Bottoni, A., & Iervasi, G. (2011) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2011.03.002 · Cited by 2 · see citing works
“and, consequently, to a reduced hemoglobin oxygen content [1].”
Background
- Authors
- Sprague, R. S., Stephenson, A. H., & Ellsworth, M. L.
- Affiliations
- Saint Louis University (US)
- ORCID
- Sprague, Randy S.
- Venue
- Trends in Endocrinology & Metabolism
- Publisher
- Elsevier BV
- Published
- 2007-11
- Volume
- 18
- Issue
- 9
- Pages
- 350-355
- ISSN
- 1043-2760 (ISSN-L)
- OpenAlex
- W1992160483
- Cited by
- 124
- References
- 68
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 5 · 2020: 4 · 2019: 11 · 2018: 8 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 8 · 2013: 7 · 2012: 8
- FWCI
- 0.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Endocrinology and Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Diabetes Association
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL051298, HL-51298, HL64180, R01HL056249, R01HL064180, HL56249, HL 39226)
- Topics
- Health Sciences › Medicine › Physiology › Erythrocyte Function and Pathophysiology
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Blood properties and coagulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Keywords
- erythrocytes, ATP release, paracrine signaling, oxygen delivery, vascular caliber, type 2 diabetes, skeletal muscle perfusion
- MeSH terms
- Energy Metabolism, Erythrocytes, Humans, Oxygen, Signal Transduction
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