Influence of FcγRIIIb polymorphism on its ability to cooperate with FcγRIIa and CR3 in mediating the oxidative burst of human neutrophils.

Autor: Urbaczek AC; Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Rua Expedicionários do Brasil, 1621, Centro, Araraquara, SP CEP 14801-360, Brazil., Toller-Kawahisa JE; Imunologia Básica e Aplicada, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo (USP), Avenida Bandeirantes, 3900, Monte Alegre, Ribeirão Preto, SP CEP 14049-900, Brazil., Fonseca LM; Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Rua Expedicionários do Brasil, 1621, Centro, Araraquara, SP CEP 14801-360, Brazil., Costa PI; Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Rua Expedicionários do Brasil, 1621, Centro, Araraquara, SP CEP 14801-360, Brazil., Faria CM; Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Rua Expedicionários do Brasil, 1621, Centro, Araraquara, SP CEP 14801-360, Brazil., Azzolini AE; Departamento de Física e Química, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo (USP), Avenida do Café, s/n, Monte Alegre, Ribeirão Preto, SP CEP 14040-903, Brazil., Lucisano-Valim YM; Departamento de Física e Química, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo (USP), Avenida do Café, s/n, Monte Alegre, Ribeirão Preto, SP CEP 14040-903, Brazil., Marzocchi-Machado CM; Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo (USP), Avenida do Café, s/n, Monte Alegre, Ribeirão Preto, SP CEP 14040-903, Brazil. Electronic address: clenimar@usp.br.
Jazyk: angličtina
Zdroj: Human immunology [Hum Immunol] 2014 Aug; Vol. 75 (8), pp. 785-90. Date of Electronic Publication: 2014 Jun 16.
DOI: 10.1016/j.humimm.2014.05.011
Abstrakt: Considering that human neutrophil FcγRIIa and FcγRIIIb receptors interact synergistically with CR3 in triggering neutrophil functional responses, allelic polymorphisms in these receptors might influence such interactions. We assessed whether FcγRIIIb polymorphisms affect FcγR/CR cooperation in mediating the neutrophil oxidative burst (OB), in particular the FcγRIIIb/CR3 cooperation that occurs via lectin-saccharide-like interactions. The OB of human neutrophil antigen (HNA)-1a-, HNA-1b-, and HNA-1a/-1b-neutrophils stimulated with immune complexes, opsonized or not with serum complement, was measured by the luminol-enhanced chemiluminescence assay. Compared with HNA-1a-neutrophils, HNA-1b-neutrophils exhibited reduced FcγR-stimulated OB, but increased FcγR/CR-stimulated OB. It suggests that (i) FcγR and CR cooperate more effectively in HNA-1b-neutrophils, and (ii) the HNA-1b allotype influences the FcγRIIIb cooperation with FcγRIIa, but not with CR3. HNA-1a- and HNA-1b-neutrophils exhibited similar OB responses elicited via CR3 alone or via FcγR/CR-independent pathways. In addition, the level of FcγRIIIb, FcγRIIa, and CR3 expression did not differ significantly among the neutrophil groups studied. Together, these results demonstrate that the HNA-1b allotype influences the functional cooperation between FcγRIIIb and FcγRIIa, and suggest that the difference in the glycosylation pattern between HNA-1a and HNA-1b does not affect the FcγRIIIb cooperation with CR3.
(Copyright © 2014 American Society for Histocompatibility and Immunogenetics. Published by Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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