Fc gamma receptor IIb enhances Fc gamma receptor IIa function in an oxidant-dependent and allele-sensitive manner

Salmon, Jane E., Millard, Sean S., Brogle, Nina L. and Kimberly, Robert P. (1995) Fc gamma receptor IIb enhances Fc gamma receptor IIa function in an oxidant-dependent and allele-sensitive manner. Journal of Clinical Investigation, 95 6: 2877-2885. doi:10.1172/JCI117994

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Author Salmon, Jane E.
Millard, Sean S.
Brogle, Nina L.
Kimberly, Robert P.
Title Fc gamma receptor IIb enhances Fc gamma receptor IIa function in an oxidant-dependent and allele-sensitive manner
Formatted title
Fcγ receptor IIb enhances Fcγ receptor IIa function in an oxidant-dependent and allele-sensitive manner
Journal name Journal of Clinical Investigation   Check publisher's open access policy
ISSN 0021-9738
1558-8238
Publication date 1995-06-01
Sub-type Article (original research)
DOI 10.1172/JCI117994
Open Access Status File (Publisher version)
Volume 95
Issue 6
Start page 2877
End page 2885
Total pages 9
Place of publication Philadelphia, PA, United States
Publisher Lippincott Williams & Wilkins
Language eng
Abstract Two classes of receptors for IgG, Fc gamma RIIa and Fc gamma RIIIb, both of which exist in two allelic forms, are expressed on human neutrophils. Neutrophils from normal donors, homozygous for the different allelic phenotypes of Fc gamma RIIIb, have significantly different levels of Fc gamma receptor-mediated phagocytosis of IgG-opsonized erythrocytes (EA). However, the observation that Fc gamma RIIIb mediates phagocytosis of specific mAb-targeted erythrocytes poorly suggests that this receptor may influence EA internalization by Fc gamma RIIa in an allele-sensitive fashion. Donors homozygous for the NA1 allele of Fc gamma RIIIb showed greater activation of Fc gamma RIIa after Fc gamma RIIIb cross-linking than donors homozygous for the NA2 allele of Fc gamma RIIIb. This increase in receptor-specific internalization reflects both an increase in ligand binding by Fc gamma RIIa and an increase in internalization efficiency of targets bound. Activation of Fc gamma RIIa by Fc gamma RIIIb is transferable by supernatants from activated cells and is blocked by inhibitors of reactive oxygen species and the H2O2-myeloperoxidase-chloride system and by serine protease inhibitors. Thus, cross-linking of Fc gamma RIIIb, which leads to neutrophil degranulation and the generation of reactive oxygen intermediates, in turn alters Fc gamma RIIa avidity and efficiency. These oxidant-mediated changes in Fc gamma RIIa function provide a novel mechanism for receptors to collaborate in both an autocrine and paracrine fashion. The allele sensitivity of these effects suggests that Fc gamma receptor polymorphisms may be inherited disease susceptibility factors in host defense against infection and in the development of autoimmunity.
Keyword Phagocytosis
Proteases
Fc gamma receptors
Oxidants
Immunoglobulin G
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biomedical Sciences Publications
 
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Created: Fri, 04 Mar 2016, 11:37:21 EST by Ms Joanne Biles on behalf of School of Biomedical Sciences