Free radicals and phagocytic cells

Rosen, Gerald M.; Pou, Sovitj; Ramos, Carroll L.; Cohen, Myron S.; Britigan, Bradley E.

doi:10.1096/fasebj.9.2.7540156

Cited by 478Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressBioactive Compounds and Antitumor Agents

Free radicals and phagocytic cells

Rosen, Gerald M., Pou, Sovitj, Ramos, Carroll L., Cohen, Myron S., Britigan, Bradley E.·1995·The FASEB Journal

DOI 10.1096/fasebj.9.2.7540156

Open this paper in CoChat — free account

Abstract

Phagocytes mediate their innate immunological response by releasing products that damage invading microorganisms. These products include proteins such as lysozyme, peroxidases, and elastase as well as reactive oxygen species such as superoxide, hydrogen peroxide, hypohalous acid, and hydroxyl radical. Although it is clear that many phagocytic secretory products have direct cytotoxic potential, understanding is limited of how multiple products interact to generate and modulate the cytotoxic response. This review focuses on recent findings that elucidate the biochemical nature of secretory product interaction in the formation of free radicals, particularly the highly reactive hydroxyl radical. The possible role of these reactions in phagocyte microbicidal activity and inflammatory tissue injury is discussed.—Rosen, G. M., Pou, S., Ramos, C. L., Cohen, M. S., Britigan, B. E. Free radicals and phagocytic cells. FASEB J. 9, 200–209 (1995)

Integrity signals

Registry

Crossref · 10.1096/fasebj.9.2.7540156

Cites

100 of 100 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

NOX2 consists of five catalytic subunits, which assemble after phagocytosis forming an active enzymatic complex producing superoxide anions and hydrogen peroxide along with the formation of hydroxyl radicals, the latter pathway being catalyzed by iron via the Fenton reaction.
“NOX2 consists of five catalytic subunits, which assemble after phagocytosis thereby forming an active enzymatic complex producing superoxide anions and hydrogen peroxide along with the formation of hydroxyl radicals, the latter pathway being catalyzed by iron via the Fenton reaction (56, 59–61).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [60]
Iron has various effects on the immune system, either by modulating immune cell proliferation and differentiation, by controlling various immune effector mechanisms of immune cells, or by directly interfering with anti-microbial immune effector pathways such as the catalysis of toxic radical formation by macrophages.
“Iron has various effects on the immune system, either by modulating immune cell proliferation and differentiation, by controlling various immune effector mechanism of immune cells and by directly interfering with anti-microbial immune effector pathways such as the catalysis of toxic radical formation by macrophages”
From Iron in immune cell function and host defense (2021) · cites this paper as [118]

Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works
Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029 · see citing works
The L-Arginine-Nitric Oxide Pathway
Epstein, F. H., Moncada, S., & Higgs, A. (1993) · New England Journal of Medicine · doi:10.1056/nejm199312303292706 · Cited by 6,678 · see citing works
Free radicals, antioxidants, and human disease: where are we now?
Halliwell, B. B., Gutteridge, J. M. C., & Cross, C. E. (1992) · PubMed · Cited by 2,155 · see citing works
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121 · see citing works
Oxygen radicals and human disease
CROSS, C. E., HALLIWELL, B., BORISH, E. T., PRYOR, W. A., AMES, B. N., SAUL, R. L., McCORD, J. M., & HARMAN, D. (1987) · Annals of Internal Medicine · doi:10.7326/0003-4819-107-4-526 · Cited by 1,856 · see citing works
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549 · see citing works
Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide
Koppenol, W. H., Moreno, J. J., Pryor, W. A., Ischiropoulos, H., & Beckman, J. S. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00030a017 · Cited by 1,338 · see citing works
DNA Deaminating Ability and Genotoxicity of Nitric Oxide and its Progenitors
Wink, D. A., Kasprzak, K. S., Maragos, C. M., Elespuru, R. K., Misra, M., Dunams, T. M., Cebula, T. A., Koch, W. H., Andrews, A. W., Allen, J. S., et al. (1991) · Science · doi:10.1126/science.1948068 · Cited by 1,235 · see citing works
The Reduction of Cytochrome c by Milk Xanthine Oxidase
McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,205 · see citing works
Ferritin: a cytoprotective antioxidant strategem of endothelium.
Balla, G., Jacob, H., Balla, J., Rosenberg, M. E., Nath, K. A., Apple, F., Eaton, J. W., & Vercellotti, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37165-0 · Cited by 1,097 · see citing works
DNA damage and mutation in human cells exposed to nitric oxide in vitro.
Nguyen, T., Brunson, D. C., Crespi, C. L., Penman, B. W., Wishnok, J. S., & Tannenbaum, S. R. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.3030 · Cited by 972 · see citing works
Spin trapping of superoxide and hydroxyl radical: Practical aspects
Finkelstein, E., Rosen, G. M., & Rauckman, E. J. (1980) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(80)90323-9 · Cited by 913 · see citing works
Self-citation
Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: comparison with enzymatically formed nitric oxide from L-arginine
Ignarro, L. J., Fukuto, J. M., Griscavage, J. M., Rogers, N. E., & Byrns, R. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8103 · Cited by 856 · see citing works
Generation of superoxide by purified brain nitric oxide synthase
Pou, S., Pou, W. S., Bredt, D. S., Snyder, S. H., & Rosen, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35745-4 · Cited by 750 · see citing works
Self-citation
H2O2 Release from Human Granulocytes during Phagocytosis
Root, R. K., & Metcalf, J. A. (1977) · Journal of Clinical Investigation · doi:10.1172/jci108886 · Cited by 587 · see citing works
Microbiostatic effect of murine-activated macrophages for Toxoplasma gondii . Role for synthesis of inorganic nitrogen oxides from l -arginine.
Adams, L. B., Hibbs, J. B., Taintor, R. R., & Krahenbuhl, J. L. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.7.2725 · Cited by 563 · see citing works
Evidence for cytokine-inducible nitric oxide synthesis from L-arginine in patients receiving interleukin-2 therapy
Hibbs, J. B., Westenfelder, C., Taintor, R., Vavrin, Z., Kablitz, C., Baranowski, R. L., Ward, J. H., Menlove, R. L., McMurry, M. P., & Kushner, J. P. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115666 · Cited by 485 · see citing works
Bactericidal activity of peroxynitrite
Zhu, L., Gunn, C., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90434-x · Cited by 438 · see citing works
Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis
Grootveld, M. C., Bell, J. D., Halliwell, B. B., Aruoma, O. I., Bomford, A. B., & Sadler, P. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83758-9 · Cited by 404 · see citing works
Long-Lived Oxidants Generated by Human Neutrophils: Characterization and Bioactivity
Weiss, S. J., Lampert, M. B., & Test, S. T. (1983) · Science · doi:10.1126/science.6635660 · Cited by 390 · see citing works
Aromatic hydroxylation and nitration of phenylalanine and tyrosine by peroxynitrite
van der Vliet, A., O’neill, C. A., Halliwell, B. B., Cross, C. E., & Kaur, H. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80391-9 · Cited by 381 · see citing works
Spin Trapping of Superoxide
Finkelstein, E., Rosen, G. M., Rauckman, E. J., & Paxton, J. (1979) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13797-8 · Cited by 372 · see citing works
Self-citation
Brominating Oxidants Generated by Human Eosinophils
Weiss, S. J., Test, S. T., Eckmann, C. M., Roos, D., & REGIANI, S. R. (1986) · Science · doi:10.1126/science.3018933 · Cited by 360 · see citing works
Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.
Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354 · see citing works
Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system.
Ambruso, D. R., & Johnston, R. B. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110042 · Cited by 334 · see citing works
Specific amino acid (L-arginine) requirement for the microbiostatic activity of murine macrophages.
Granger, D. L., Hibbs, J. B., Perfect, J. R., & Durack, D. T. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113427 · Cited by 326 · see citing works
Oxygen- and carbon-centered free radical formation during carbon tetrachloride metabolism. Observation of lipid radicals in vivo and in vitro.
McCay, P. B., Lai, E. K., Poyer, J. L., DuBose, C. M., & Janzen, E. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43327-8 · Cited by 318 · see citing works
Human neutrophils and mononuclear cells inhibit platelet aggregation by releasing a nitric oxide-like factor.
Salvemini, D., Nucci, G. D., Gryglewski, R. J., & Vane, J. R. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.16.6328 · Cited by 307 · see citing works
Ferric iron and superoxide ions are required for the killing of cultured hepatocytes by hydrogen peroxide. Evidence for the participation of hydroxyl radicals formed by an iron-catalyzed Haber-Weiss reaction.
Starke-Reed, P. E., & Farber, J. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39218-9 · Cited by 298 · see citing works
Generation of nitric oxide by human neutrophils
Wright, C. D., Mülsch, A., Busse, R., & Oßwald, H. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92506-0 · Cited by 292 · see citing works
Mechanisms involved in mycobacterial growth inhibition by gamma interferon-activated bone marrow macrophages: role of reactive nitrogen intermediates
Flesch, I. E. A., & Kaufmann, S. H. E. (1991) · Infection and Immunity · doi:10.1128/iai.59.9.3213-3218.1991 · Cited by 280 · see citing works
Generation of Hydroxyl Radical by Enzymes, Chemicals, and Human Phagocytes In Vitro
Repine, J. E., Eaton, J. W., Anders, M. W., Hoidal, J. R., & Fox, R. B. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109626 · Cited by 280 · see citing works
Hydrogen peroxide kills Staphylococcus aureus by reacting with staphylococcal iron to form hydroxyl radical.
Repine, J. E., Fox, R. B., & Berger, E. M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68927-1 · Cited by 279 · see citing works
Hemoglobin potentiates central nervous system damage.
Sadrzadeh, S. M. H., Anderson, D. K., Panter, S. S., Hallaway, P. E., & Eaton, J. W. (1987) · Journal of Clinical Investigation · doi:10.1172/jci112865 · Cited by 265 · see citing works
Chlorohydrin Formation From Unsaturated Fatty Acids Reacted With Hypochlorous Acid
Winterbourn, C. C., van den Berg, J. J. M., Roitman, E., & Kuypers, F. A. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90609-z · Cited by 258 · see citing works
Evidence for hydroxyl radical production by human neutrophils.
Tauber, A. I., & BABIOR, B. M. (1977) · Journal of Clinical Investigation · doi:10.1172/jci108786 · Cited by 256 · see citing works
Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl-radical generation?
Aruoma, O. I., & Halliwell, B. B. (1987) · Biochemical Journal · doi:10.1042/bj2410273 · Cited by 248 · see citing works
L-citrulline production from L-arginine by macrophage nitric oxide synthase. The ureido oxygen derives from dioxygen.
Kwon, N. S., Nathan, C. F., Gilker, C. D., Griffith, O. W., Matthews, D. E., & Stuehr, D. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77366-3 · Cited by 247 · see citing works
Spin trapping evidence for myeloperoxidase-dependent hydroxyl radical formation by human neutrophils and monocytes.
Ramos, C. L., Pou, S., Britigan, B. E., Cohen, M. S., & Rosen, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42443-x · Cited by 230 · see citing works
Self-citation
Leukocytic Oxygen Activation and Microbicidal Oxidative Toxin
Hurst, J. K., & Barrette, W. C. (1989) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238909082555 · Cited by 228 · see citing works
The Human Neutrophil Respiratory Burst Oxidase
Clark, R. A. (1990) · The Journal of Infectious Diseases · doi:10.1093/infdis/161.6.1140 · Cited by 222 · see citing works
Free Hydroxyl Radicals are Formed on Reaction Between the Neutrophil-Derived Species Superoxide Anion and Hypochlorous Acid
Candeias, L. P., Patel, K. B., Stratford, M. R. L., & Wardman, P. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80394-a · Cited by 212 · see citing works
Human granulocyte generation of hydroxyl radical.
Weiss, S. J., Rustagi, P. K., & LoBuglio, A. F. (1978) · The Journal of Experimental Medicine · doi:10.1084/jem.147.2.316 · Cited by 191 · see citing works
Failure of Nitro Blue Tetrazolium reduction in the phagocytic vacuoles of leukocytes in chronic granulomatous disease
Nathan, D. G., Baehner, R. L., & Weaver, D. K. (1969) · Journal of Clinical Investigation · doi:10.1172/jci106156 · Cited by 184 · see citing works
L-Arginine-Dependent Reactive Nitrogen Intermediates and the Antimicrobial Effect of Activated Human Mononuclear Phagocytes
Murray, H. W., & Teitelbaum, R. (1992) · The Journal of Infectious Diseases · doi:10.1093/infdis/165.3.513 · Cited by 176 · see citing works
Role of myeloperoxidase in the respiratory burst of human neutrophils
Nauseef, W., Metcalf, J., & Root, R. (1983) · Blood · doi:10.1182/blood.v61.3.483.483 · Cited by 175 · see citing works
Do human neutrophils make hydroxyl radical? Determination of free radicals generated by human neutrophils activated with a soluble or particulate stimulus using electron paramagnetic resonance spectrometry.
Britigan, B. E., Rosen, G. M., Chai, Y., et al. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38517-4 · Cited by 168 · see citing works
Self-citation
The production of hydroxyl and superoxide radicals by stimulated human neutrophils — measurements by EPR spectroscopy
Green, M. R., Hill, H. A. O., Okolow-Zubkowska, M. J., et al. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)81123-0 · Cited by 161 · see citing works
Hydroxyl radical generation by polymorphonuclear leukocytes measured by electron spin resonance spectroscopy.
Rosen, H., & Klebanoff, S. J. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109637 · Cited by 158 · see citing works
Problems associated with spin trapping oxygen-centered free radicals in biological systems
Pou, S., Hassett, D. J., Britigan, B. E., Cohen, M. S., & Rosen, G. M. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90002-x · Cited by 148 · see citing works
Self-citation
The effect of human serum transferrin and milk lactoferrin on hydroxyl radical formation from superoxide and hydrogen peroxide.
Baldwin, D. A., Jenny, E. R., & Aisen, P. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90707-6 · Cited by 145 · see citing works
Clearance of Neutrophil-derived Myeloperoxidase by the Macrophage Mannose Receptor
Shepherd, V. L., & Hoidal, J. R. (1990) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/2.4.335 · Cited by 143 · see citing works
Source of iron in neutrophil-mediated killing of endothelial cells.
Gannon, D. E., Varani, J., Phan, S. H., Ward, J. H., Kaplan, J., Till, G. O., Simon, R. H., Ryan, U. S., & Ward, P. A. (1987) · PubMed · Cited by 133 · see citing works
Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity.
Slungaard, A., & Mahoney, J. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67734-3 · Cited by 128 · see citing works
Lower respiratory tract iron burden is increased in association with cigarette smoking.
Thompson, A. B., Bohling, T., Heires, A. J., Linder, J., & Rennard, S. I. (1991) · PubMed · Cited by 128 · see citing works
Ethylene formation by polymorphonuclear leukocytes. Role of myeloperoxidase.
Klebanoff, S. J., & Rosen, H. (1978) · The Journal of Experimental Medicine · doi:10.1084/jem.148.2.490 · Cited by 122 · see citing works
A Kinetic Approach to the Selection of a Sensitive Spin Trapping System for the Detection of Hydroxyl Radical
Pou, S., Ramos, C. L., Gladwell, T., et al. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1085 · Cited by 121 · see citing works
Self-citation
Hydrogen peroxide-mediated toxicity for Leishmania donovani chagasi promastigotes. Role of hydroxyl radical and protection by heat shock.
Zarley, J. H., Britigan, B. E., & Wilson, M. E. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115461 · Cited by 112 · see citing works
Self-citation
Myeloperoxidase as an effective inhibitor of hydroxyl radical production. Implications for the oxidative reactions of neutrophils.
Winterbourn, C. C. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112607 · Cited by 111 · see citing works
Rate of reaction of superoxide radical with chloride-containing species
Long, C. A., & Bielski, B. H. J. (1980) · The Journal of Physical Chemistry · doi:10.1021/j100442a023 · Cited by 111 · see citing works
Stimulated human neutrophils limit iron-catalyzed hydroxyl radical formation as detected by spin-trapping techniques.
Britigan, B. E., Rosen, G. M., Thompson, B. Y., Chai, Y., & Cohen, M. S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75994-8 · Cited by 107 · see citing works
Self-citation
Hydroxyl radical production by stimulated neutrophils reappraised.
Samuni, A. M., BLACK, C. D. V., Krishna, C. M., et al. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68313-9 · Cited by 101 · see citing works
Oxidation of salicylates by stimulated granulocytes: evidence that these drugs act as free radical scavengers in biological systems.
Sagone, A. L., & Husney, R. M. (1987) · The Journal of Immunology · doi:10.4049/jimmunol.138.7.2177 · Cited by 98 · see citing works
Effects of the putative neutrophil-generated toxin, hypochlorous acid, on membrane permeability and transport systems of Escherichia coli.
Albrich, J. M., Gilbaugh, J. H., Callahan, K. B., & Hurst, J. K. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112548 · Cited by 96 · see citing works
Spin trapping evidence for the lack of significant hydroxyl radical production during the respiration burst of human phagocytes using a spin adduct resistant to superoxide-mediated destruction.
Britigan, B. E., Coffman, T. J., & Buettner, G. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39850-3 · Cited by 94 · see citing works
Self-citation
Lactoferrin-catalysed hydroxyl radical production. Additional requirement for a chelating agent
Winterbourn, C. C. (1983) · Biochemical Journal · doi:10.1042/bj2100015 · Cited by 93 · see citing works
A new method for the detection of hydroxyl radical production by phagocytic cells
Sagone, A. L., Decker, M. A., Wells, R. M., et al. (1980) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(80)90354-2 · Cited by 89 · see citing works
Aromatic hydroxylation of phenylalanine as an assay for hydroxyl radicals: Application to activated human neutrophils and to the heme protein leghemoglobin
Kaur, H., Fagerheim, I., Grootveld, M. C., Puppo, A., & Halliwell, B. B. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90456-3 · Cited by 82 · see citing works
Pseudomonas and neutrophil products modify transferrin and lactoferrin to create conditions that favor hydroxyl radical formation.
Britigan, B. E., & Edeker, B. L. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115408 · Cited by 81 · see citing works
Self-citation
Superoxide-dependent reduction of nitroxides by thiols
Finkelstein, E., Rosen, G. M., & Rauckman, E. J. (1984) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(84)90038-2 · Cited by 80 · see citing works
Self-citation
Spin-trapping and Human Neutrophils: Limits of detection of hydroxyl radical
Pou, S., Rosen, G. M., Cohen, M. S., et al. (2023) · PubMed · doi:10.17615/39py-g663 · Cited by 73 · see citing works
Self-citation
Possible role of bacterial siderophores in inflammation. Iron bound to the Pseudomonas siderophore pyochelin can function as a hydroxyl radical catalyst.
Coffman, T. J., Cox, C. D., Edeker, B. L., & Britigan, B. E. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114805 · Cited by 72 · see citing works
Self-citation
Neutrophil degranulation inhibits potential hydroxyl-radical formation. Relative impact of myeloperoxidase and lactoferrin release on hydroxyl-radical production by iron-supplemented neutrophils assessed by spin-trapping techniques
Britigan, B. E., Hassett, D. J., Rosen, G. M., et al. (1989) · Biochemical Journal · doi:10.1042/bj2640447 · Cited by 69 · see citing works
Self-citation
Iron sequestration by macrophages decreases the potential for extracellular hydroxyl radical formation.
Olakanmi, O., McGowan, S. E., Hayek, M. B., & Britigan, B. E. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116310 · Cited by 66 · see citing works
Self-citation
Nucleotide chloramines and neutrophil‐mediated cytotoxicity
Bernofsky, C. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.3.1848195 · Cited by 65 · see citing works
Uptake of lactoferrin by mononuclear phagocytes inhibits their ability to form hydroxyl radical and protects them from membrane autoperoxidation
Britigan, B. E., Serody, J. S., Hayek, M. B., Charniga, L., & Cohen, M. S. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.12.4271 · Cited by 62 · see citing works
Self-citation
Do humans neutrophils form hydroxyl radical? Evaluation of an unresolved controversy
Cohen, M. S., Britigan, B. E., Hassett, D. J., et al. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90033-0 · Cited by 62 · see citing works
Self-citation
Enhanced Killing of Myeloperoxidase-Coated Bacteria in the Myeloperoxidase-H2O2-C1- System
Selvaraj, R. J., Zgliczyński, J. M., Paul, B. B., & Sbarra, A. J. (1978) · The Journal of Infectious Diseases · doi:10.1093/infdis/137.4.481 · Cited by 57 · see citing works
Loss of DNA-membrane interactions and cessation of DNA synthesis in myeloperoxidase-treated Escherichia coli.
Rosen, H., Orman, J. V., Rakita, R. M., Michel, B. R., & VanDevanter, D. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.10048 · Cited by 54 · see citing works
Eosinophil peroxidase-dependent hydroxyl radical generation by human eosinophils.
McCormick, M. L., Roeder, T. L., Railsback, M. A., & Britigan, B. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46874-3 · Cited by 53 · see citing works
Self-citation
Role of free radical processes in stimulated human polymorphonuclear leukocytes
Thomas, M. J., Shirley, P. S., Hedrick, C. C., & DeChatelet, L. R. (1986) · Biochemistry · doi:10.1021/bi00372a037 · Cited by 52 · see citing works
Insight into the nature and site of oxygen-centered free radical generation by endothelial cell monolayers using a novel spin trapping technique
Britigan, B., Roeder, T., & Shasby, D. (1992) · Blood · doi:10.1182/blood.v79.3.699.699 · Cited by 47 · see citing works
Self-citation
The interaction of lactoferrin with human monocytes.
Hs, B. (1991) · PubMed · Cited by 46 · see citing works
The catalytic activity of iron in synovial fluid as monitored by the ascorbate free radical
Buettner, G. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90144-8 · Cited by 41 · see citing works
Conversion of superoxide generated by polymorphonuclear leukocytes to hydroxyl radical: A direct spectrophotometric detection system based on degradation of deoxyribose
Greenwald, R. A., Rush, S. W., Moak, S. A., et al. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90084-1 · Cited by 37 · see citing works
Threshold responses in production of reactive oxygen metabolites in individual neutrophils detected by flow cytometry and microfluorimetry
Patel, A., Hallett, M. B., & Campbell, A. K. (1987) · Biochemical Journal · doi:10.1042/bj2480173 · Cited by 36 · see citing works
Oxygen‐derived radicals from Trypanosoma cruzi‐stimulated human neutrophils
Docampo, R., Casellas, A. M., Madeira, E. D., et al. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80201-4 · Cited by 31 · see citing works
Pseudomonas siderophore pyochelin enhances neutrophil-mediated endothelial cell injury
Britigan, B. E., Rasmussen, G. T., & Cox, C. D. (1994) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1994.266.2.l192 · Cited by 31 · see citing works
Self-citation
Eosinophil peroxidase deficiency: morphological and immunocytochemical studies of the eosinophil-specific granules
Zabucchi, G., Soranzo, M., Menegazzi, R., et al. (1992) · Blood · doi:10.1182/blood.v80.11.2903.2903 · Cited by 29 · see citing works
Spin trap determination of free radical burst kinetics in stimulated neutrophils.
Kleinhans, F. W., & Barefoot, S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45226-x · Cited by 29 · see citing works
Laboratory models of chronic granulomatous disease.
Holmes, B., & Ra, G. (1972) · PubMed · Cited by 29 · see citing works
Release of iron from phagocytosed Escherichia coli and uptake by neutrophil lactoferrin
Molloy, A., & Winterbourn, C. (1990) · Blood · doi:10.1182/blood.v75.4.984.984 · Cited by 24 · see citing works
Intracellular spin-trapping of oxygen-centered radicals generated by human neutrophils
Pou, S., Rosen, G. M., Britigan, B. E., et al. (1989) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(89)90073-1 · Cited by 22 · see citing works
Self-citation
Phagocyte-Derived Free Radicals Stimulated by Ingestion of Iron-Rich Staphylococcus aureus: A Spin-Trapping Study
Cohen, M. S., Britigan, B. E., Chai, Y. S., et al. (1991) · The Journal of Infectious Diseases · doi:10.1093/infdis/163.4.819 · Cited by 19 · see citing works
Self-citation
Determination of Alternate Pathway Complement Kinetics by Electron Spin Resonance Spectroscopy
Hawley, D. A., Kleinhans, F. W., & Biesecker, J. L. (1983) · American Journal of Clinical Pathology · doi:10.1093/ajcp/79.6.673 · Cited by 18 · see citing works
Myeloperoxidase-mediated inhibition of microbial respiration: damage to Escherichia coli ubiquinol oxidase
Rakita, R. M., Michel, B. R., & Rosen, H. (1989) · Biochemistry · doi:10.1021/bi00433a044 · Cited by 13 · see citing works
Penicillin-binding protein inactivation by human neutrophil myeloperoxidase.
Rakita, R. M., & Rosen, H. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115372 · Cited by 13 · see citing works
N-hydroxylamine is not an intermediate in the conversion of l -arginine to an activator of soluble guanylate cyclase in neuroblastoma N1E-115 cells
Pou, S., Pou, W. S., Rosen, G. M., et al. (1991) · Biochemical Journal · doi:10.1042/bj2730547 · Cited by 11 · see citing works
Self-citation
Inhibition of bacterial DNA synthesis by myeloperoxidase-derived oxidants
Rosen, H., Michel, B. R., Wu, A. Y., et al. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90356-y · Cited by 2 · see citing works

Flagged first, then by citations

Sorted by citations

Superoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters
Fridovich, I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18515 · Cited by 1,337 · see citing works
Macrophage defense mechanisms against intracellular bacteria
Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · see citing works
A highly sensitive fluorescent micro-assay of h2o2 release from activated human leukocytes using a dihydroxyphenoxazine derivative
Mohanty, J. G., Jaffe, J. S., Schulman, E. S., & Raible, D. G. (1997) · Journal of Immunological Methods · doi:10.1016/s0022-1759(96)00244-x · Cited by 496 · see citing works
ROS production in phagocytes: Why, when, and where?
Dupré-Crochet, S., Erard, M., & Nüβe, O. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1012544 · Cited by 467 · see citing works
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468 · see citing works
Cytokine-mediated regulation of iron transport in human monocytic cells
Ludwiczek, S., Aigner, E., Theurl, I., & Weiss, G. (2003) · Blood · doi:10.1182/blood-2002-08-2459 · Cited by 420 · see citing works
Redox control of inflammation in macrophages
Brüne, B., Dehne, N., Grossmann, N., Jung, M., Namgaladze, D., Schmid, T., von Knethen, A., & Weigert, A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4785 · Cited by 377 · see citing works
Iron metabolism in the anemia of chronic disease
Weiss, G. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.08.006 · Cited by 322 · see citing works
Iron and immunity: a double-edged sword.
Weiss, G. (2002) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2002.0320s1070.x · Cited by 317 · see citing works
The inflammatory response in mild and in severe psoriasis
Rocha-Pereira, P., Santos-Silva, A., Rebelo, I., Figueiredo, A., Quintanilha, A., & Teixeira, F. (2004) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2004.05984.x · Cited by 258 · see citing works
Treatment with N-acetylcysteine plus deferoxamine protects rats against oxidative stress and improves survival in sepsis*
Ritter, C., Andrades, M. E., Reinke, A., Menna-Barreto, S., Moreira, J. C. F., & Dal-Pizzol, F. (2004) · Critical Care Medicine · doi:10.1097/01.ccm.0000109454.13145.ca · Cited by 233 · see citing works
Pathways underlying iron accumulation in human nonalcoholic fatty liver disease
Aigner, E., Theurl, I., Theurl, M., Lederer, D., Haufe, H., Dietze, O., Strasser, M., Datz, C., & Weiss, G. (2008) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/87.5.1374 · Cited by 190 · see citing works
Iron in immune cell function and host defense
Haschka, D., Hoffmann, A., & Weiss, G. (2021) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2020.12.005 · Cited by 188 · see citing works
Central role of transcription factor NF‐IL6 for cytokine and iron‐mediated regulation of murine inducible nitric oxide synthase expression
Dlaska, M., & Weiss, G. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.10.6171 · Cited by 176 · see citing works
Impaired Superoxide Production Due to a Deficiency in Phagocyte NADPH Oxidase Fails to Inhibit Atherosclerosis in Mice
Kirk, E. A., Dinauer, M. C., Rosen, H., Chait, A., Heinecke, J. W., & LeBoeuf, R. C. (2000) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.20.6.1529 · Cited by 171 · see citing works
Iron status and the outcome of HIV infection: an overview
Gordeuk, V. R., Delanghe, J. R., Langlois, M. R., & Boelaert, J. R. (2001) · Journal of Clinical Virology · doi:10.1016/s1386-6532(00)00134-7 · Cited by 124 · see citing works
Iron Chelation Therapy for Malaria
Mabeza, G. F., Loyevsky, M., Gordeuk, V. R., & Weiss, G. (1999) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(98)00037-0 · Cited by 111 · see citing works
Pathways for the regulation of interferon-γ-inducible genes by iron in human monocytic cells
Oexle, H., Kaser, A., Möst, J., Bellmann-Weiler, R., Werner, E. R., Werner-Felmayer, G., & Weiss, G. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0802420 · Cited by 108 · see citing works
Effect of iron treatment on circulating cytokine levels in ESRD patients receiving recombinant human erythropoietin
Weiss, G., Meusburger, E., Radacher, G., Garimorth, K., Neyer, U., & Mayer, G. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00099.x · Cited by 105 · see citing works
Hypochlorous Acid Stimulation of the Mitogen-Activated Protein Kinase Pathway Enhances Cell Survival
Midwinter, R. G., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2530 · Cited by 90 · see citing works
Regulatory Interactions between Iron and Nitric Oxide Metabolism for Immune Defense againstPlasmodium falciparumInfection
Fritsche, G., Larcher, C., Schennach, H., & Weiss, G. (2001) · The Journal of Infectious Diseases · doi:10.1086/319860 · Cited by 84 · see citing works
The Macrophage: A Cellular Factory at the Interphase Between Iron and Immunity for the Control of Infections
Theurl, I., Fritsche, G., Ludwiczek, S., Garimorth, K., Bellmann-Weiler, R., & Weiss, G. (2005) · BioMetals · doi:10.1007/s10534-005-3710-1 · Cited by 72 · see citing works
Heme oxygenase 1 controls early innate immune response of macrophages toSalmonellaTyphimurium infection: Heme oxygenase 1 expression affects Salmonellainfection
Mitterstiller, A.-M., Haschka, D., Dichtl, S., Nairz, M., Demetz, E., Talasz, H., Soares, M. P., Einwallner, E., Esterbauer, H., Fang, F. C., et al. (2016) · Cellular Microbiology · doi:10.1111/cmi.12578 · Cited by 62 · see citing works
Neutrophil gelatinase-associated lipocalin and interleukin-10 regulate intramacrophage Chlamydia pneumoniae replication by modulating intracellular iron homeostasis
Bellmann-Weiler, R., Schroll, A., Engl, S., Nairz, M., Talasz, H., Seifert, M., & Weiss, G. (2013) · Immunobiology · doi:10.1016/j.imbio.2012.11.004 · Cited by 43 · see citing works
The Role of Iron in Staphylococcus aureus Infection and Human Disease: A Metal Tug of War at the Host—Microbe Interface
van Dijk, M. C., de Kruijff, R. M., & Hagedoorn, P.-L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.857237 · Cited by 41 · see citing works
Divergent effects of α1-antitrypsin on the regulation of iron metabolism in human erythroleukaemic (K562) and myelomonocytic (THP-1) cells
WEISS, G., GRAZIADEI, I., URBANEK, M., GRÜNEWALD, K., & VOGEL, W. (1996) · Biochemical Journal · doi:10.1042/bj3190897 · Cited by 19 · see citing works
Nutraceuticals in immunosenescence
Magrone, T., & Jirillo, E. (2015) · Anti‐ageing nutrients · doi:10.1002/9781118823408.ch5 · Cited by 4 · see citing works

Lizozim kao prirodni prehrambeni konzervans
Bertović, T. (2014)
Palmitoyl Lysozyme-Induced Stabilization of PE (Phosphatidylethanolamine) Liposomes and Their Interaction with Candida albicans1
Lee, E., & Kim, J.-D. (1995) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124720 · Cited by 10 · see citing works
Stability studies of lysozyme for preformulation
Yan-qiang, Z. (2010) · The Journal of Pharmaceutical Practice
Regeneration to the Native Form of Hen Egg-White Lysozyme from Its Protected Derivatives
Aimoto, S., & Shimonishi, Y. (1978) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.51.205 · Cited by 6 · see citing works
난백 lysozyme의 역가측정과 안정성에 관한 연구
이성기, 유익종, 김기성, et al. (1990) · Korean Journal of Poultry Science

Authors: Rosen, G. M., Pou, S., Ramos, C. L., Cohen, M. S., & Britigan, B. E.
Affiliations: University of Maryland, Baltimore (US)
University of North Carolina at Chapel Hill (US)
University of Iowa (US)
Corresponding author: Rosen, Gerald M.
ORCID: Rosen, Gerald M.
Pou, Sovitj
Cohen, Myron S.
Britigan, Bradley E.
Venue: The FASEB Journal
Publisher: Wiley
Published: 1995-02
Volume: 9
Issue: 2
Pages: 200-209
ISSN: 0892-6638 (ISSN-L)
1530-6860
DOI: 10.1096/fasebj.9.2.7540156
OpenAlex: W2110509373
Cited by: 478
References: 100
Citations by year: 2026: 4 · 2024: 8 · 2023: 6 · 2022: 13 · 2021: 8 · 2020: 9 · 2019: 7 · 2018: 12 · 2017: 12 · 2016: 8 · 2015: 19 · 2014: 15 · 2013: 12 · 2012: 9
FWCI: 11.04
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The FASEB Journal (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r29hl044275-05, 5p01ai028412-05, 5r01hl033550-08)
National Heart, Lung, and Blood Institute (HL-44275, HL33550)
National Institute of Allergy and Infectious Diseases (AI-28412)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
Keywords: phagocytes, free radicals, hydroxyl radicals, reactive oxygen species, lysozyme, peroxidase, elastase, superoxide, hydrogen peroxide, hypohalous acids, microbicidal activity, innate immunity, cytotoxicity
MeSH terms: Amino Acid Oxidoreductases, Animals, Catalysis, Free Radicals, Humans, Inflammation, Leukocytes, NADH, NADPH Oxidoreductases, Nitric Oxide, Oxidation-Reduction, Phagocytes, Phagocytosis, Hydroxyl Radical, Nitric Oxide Synthase, NADPH Oxidases

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

Free radicals and phagocytic cells

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks