Neutrophil-induced immunoglobulin binding to erythrocytes involves proteolytic and oxidative injury

Neutrophil‐induced alterations in feline erythrocytes were studied to better understand the pathogenesis of erythrocyte destruction associated with inflammatory diseases. As in previous studies, addition of superoxide dismutase/catalase to a coculture of erythrocytes and activated neutrophils attenu...

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Bibliographic Details
Published in:Journal of leukocyte biology 1992-01, Vol.51 (1), p.19-23
Main Authors: Weiss, Douglas J., Aird, Betsy, Murtaugh, Michael P.
Format: Article
Language:English
Subjects:
anemia
Animals
Anion Exchange Protein 1, Erythrocyte - analysis
Biological and medical sciences
Cats
Cells, Cultured
Endopeptidases - pharmacology
erythrocytes
Erythrocytes - cytology
Erythrocytes - metabolism
Erythrocytes - ultrastructure
Freeze Fracturing
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Immunobiology
Immunoglobulin G - metabolism
inflammation
leukocytes (neutrophilic)
Microscopy, Electron
Myeloid cells: ontogeny, maturation, markers, receptors
natural autoimmunity
Neutrophils - cytology
Neutrophils - physiology
Oxidants - pharmacology
Phenylmethylsulfonyl Fluoride - pharmacology
Polynuclears
Protein Binding
Serine Endopeptidases - physiology
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Summary:Neutrophil‐induced alterations in feline erythrocytes were studied to better understand the pathogenesis of erythrocyte destruction associated with inflammatory diseases. As in previous studies, addition of superoxide dismutase/catalase to a coculture of erythrocytes and activated neutrophils attenuated neutrophil‐induced immunoglobulin G (IgG) binding. However, incubation of erythrocytes with hydrogen peroxide or neutrophil‐derived anuclear cytoplasts (neutroplasts) failed to induce IgG binding. Addition of phenylmethylsulfonyl fluoride, a serine protease inhibitor, to the erythrocyte‐neutrophil coculture attenuated IgG binding. These observations suggest that neutrophil‐derived serine protease activity is involved in IgG binding to erythrocytes. Further, incubation of erythrocytes with serine proteases, but not metalloproteases or sulfhydryl proteases, induced immunoglobulin binding. Freeze‐fracture replicas of the erythrocyte membrane failed to demonstrate clustering of band 3 protein, suggesting that spatial rearrangement of band 3 protein was not the cause of the IgG binding. Neutrophil‐induced IgG binding due to the combined action of proteases and oxidants may explain the accelerated destruction of erythrocytes in inflammatory diseases.
ISSN:0741-5400
1938-3673
DOI:10.1002/jlb.51.1.19