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Protein tyrosine phosphorylation triggered by human Fc gamma RII.

Abstract：

:The role of the cytoplasmic domain of human Fc gamma RII in cellular activation was studied by transfecting P815 cells with different isoforms or deletion mutants of this receptor and then assaying protein tyrosine phosphorylation after crosslinking with anti-CD32 monoclonal antibodies. Fc gamma RIIa, but not Fc gamma RIIb1 or b2, was able to trigger tyrosine phosphorylation. Deletion of just the carboxyl-terminal 19 amino acids of Fc gamma RIIa markedly reduced induction of protein tyrosine phosphorylation. Deletion of the carboxyl-terminal 38 amino acids of the cytoplasmic domain completely eliminated this response. These results indicate the cytoplasmic domain of human Fc gamma RIIa, the form of Fc gamma RII that predominates on human myeloid cells and platelets, contains sequences that allow activation of tyrosine phosphorylation; Fc gamma RIIb isoforms, the form of Fc gamma RII on human B lymphocytes, lack these sequences.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Liu Z,Pudiak D,Looney RJ

doi

10.1006/bbrc.1994.1775

subject

Has Abstract

pub_date

1994-06-15 00:00:00

pages

829-34

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X8471775X

journal_volume

201

pub_type

杂志文章

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