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Titolo:
Fc gamma receptors differ in their structural requirements for interactionwith the tyrosine kinase Syk in the initial steps of signaling for phagocytosis
Autore:
Kim, MK; Pan, XQ; Huang, ZY; Hunter, S; Hwang, PH; Indik, ZK; Schreiber, AD;
Indirizzi:
Univ Penn, Sch Med, Dept Med, Div Hematol Oncol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 tol Oncol, Philadelphia, PA 19104 USA
Titolo Testata:
CLINICAL IMMUNOLOGY
fascicolo: 1, volume: 98, anno: 2001,
pagine: 125 - 132
SICI:
1521-6616(200101)98:1<125:FGRDIT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CYTOPLASMIC DOMAIN; CROSS-LINKING; MEDIATED PHAGOCYTOSIS; MONOCYTIC CELLS; PHOSPHORYLATION; RII; ASSOCIATION; ACTIVATION; PROTEINS; ABSENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Pan, XQ Univ Penn, Sch Med, Dept Med, Div Hematol Oncol, BRB2-3,Room 705,421 CurieBlvd, Philadelphia, PA 19104 USA Univ Penn BRB2-3,Room 705,421 Curie Blvd Philadelphia PA USA 19104
Citazione:
M.K. Kim et al., "Fc gamma receptors differ in their structural requirements for interactionwith the tyrosine kinase Syk in the initial steps of signaling for phagocytosis", CLIN IMMUNO, 98(1), 2001, pp. 125-132

Abstract

Receptors for the constant region of IgG, Fc gamma receptors, are expressed on the surface of hematopoietic cells, where they mediate signaling events, such as phagocytosis, essential for host defense. Fc gamma receptors also play a role in the pathophysiology of autoimmune diseases. We have demonstrated that members of each of the three classes of human Fc gamma receptors, Fc gamma RI, Fc gamma RII, and Fc gamma RIII, mediate phagocytosis, but that important differences exist in their requirements for phagocytic signaling. For example, the Fc gamma receptors Fc gamma RI and Fc gamma RIIIA induce signaling largely by association with a gamma subunit containing a conserved cytoplasmic motif (ITAM) whose tyrosines are phosphorylated following receptor stimulation. Fc gamma RIIA contains a similar moth in its own cytoplasmic domain and does not require the gamma chain for phagocytic signaling. The tyrosine kinase Syk associates with the cytoplasmic domain of boththe Fc gamma receptor gamma chain and Fc gamma RIIA and is required for phagocytosis by both Fc gamma receptor systems. To elucidate the differences in phagocytic signaling by the gamma chain and Fc gamma RIIA, we investigated the requirements for Fc gamma receptor/Syk co-immunoprecipitation, tyrosine phosphorylation, and phagocytosis, Both Fc gamma RIIA and the human gamma chain contain a tyrosine seven amino acids upstream of the ITAM motif. We observed that the upstream tyrosine plays a role in Fc gamma RIIA phagocytic signaling but is not involved in phagocytic signaling by the human gamma chain. Our data also indicate that the two ITAM tyrosines of the human gamma chain and Fc gamma RIIA do not contribute equally to Fc gamma receptor association with Syk kinase and phagocytic signaling. The data indicate that the carboxy-terminal tyrosine of the receptor cytoplasmic domain is especially important both for the interaction with Syk kinase and for phagocytosis. Elucidating such differences in gamma chain and Fc gamma RIIA signalingmay be valuable in designing strategies for therapeutic intervention in hematopoietic and immunological disorders. (C) 2000 Academic Press.

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Documento generato il 12/12/19 alle ore 14:56:10