Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA.

Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Research Abstract Details 

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Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Abstract Text:

H Zeng,T Yoshida,T Kurosaki,H Yamamura,A Oshima,D Kitamura,T Watanabe,M Morikawa,

Human Fc gamma receptor IIIA (hFc gamma RIIIA) cDNA was introduced into mouse macrophage/monocyte cell line P388D1, and several stable cell clones expressing hFc gamma RIIIA were isolated. This facilitated the study of the biological function of Fc gamma RIIIA in monocytes/macrophages. The cloned cells showed the high phagocytic activity mediated by hFc gamma-RIIIA, while the original P388D1 cells did not. In order to examine the phosphorylation of proteins involved in hFc gamma RIIIA signal transduction, these receptors were stimulated by cross-linking. The cross-linking of hFc gamma RIIIA induced a rapid increase in tyrosine phosphorylation of several proteins, including PLC-gamma 1, Syk, HS1, and p21rasGAP-associated p190 and p60 proteins. Immunoblotting with a polyclonal antibody specific for the GAP-associated p62 protein, which was originally found in fibroblasts and is homologous with an RNA-binding protein, revealed that the p60 phosphorylated after cross-linking of hFc gamma RIIIA seemed to represent a novel GAP-associated protein unrelated to the known GAP-associated p62 protein, which was also present in the P388D1 cells.

Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Publishing Authors By Initials

H Zeng,T Yoshida,T Kurosaki,H Yamamura,A Oshima,D Kitamura,T Watanabe,M Morikawa,

For similar type c phospholipases research abstracts see: type c phospholipases research

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Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 118

Page Numbers: 1166-74

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1995

Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Keywords Mesh Terms:

KEYWORDS: Type C Phospholipases

MESH TERMS: metabolism

Chemical & Substance for Abstract: Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA. Information

Substance Name: Type C Phospholipases

Registry Number: EC 3.1.4.-

Grant and Affiliation Information for Phosphorylation of HS1, GAP-associated p190 and a novel GAP-associated p60 protein by cross-linking of Fc gamma RIIIA.

AFFILIATION: Tokyo Institute for Immunopharmacology, Inc.

Country: JAPAN

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MEDLINETA: J Biochem

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