Tyrosine phosphorylation of a 34-kDa protein induced by cross-linking a novel glycosylphosphatidylinositol-anchored glycoprotein (GPI-80) on human neutrophils that may regulate their adherence and migration.

Abstract:

:We previously found a novel glycosylphosphatidylinositol (GPI)-anchored glycoprotein designated GPI-80 that modulates complement receptor 3 integrin-dependent adhesion and in vitro transendothelial migration of neutrophils. In this study, we show that antibody-mediated cross-linking of GPI-80 led to rapid tyrosine phosphorylation mainly of a 34-kDa protein (pp34). Chemical inhibitors, such as genistein, sodium orthovanadate, wortmannin, cytochalasin B, Ro 31-8220, and 1,2-bis(2-aminophenoxy)ethane-N,N,N',N',-tetraacetic acid inhibited this response, whereas pertussis toxin had no effect. These findings demonstrate that the tyrosine phosphorylation of pp34 by cross-linking GPI-80 in human neutrophils involves tyrosine kinases, tyrosine phosphatases, phosphatidylinositol 3-kinase, cytoskeleton reorganization, protein kinase C, and cytoplasmic calcium, but not heterotrimeric G proteins.

journal_name

IUBMB Life

journal_title

IUBMB life

authors

Yu Y,Araki Y,Sendo F

doi

10.1080/713803588

keywords:

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

43-7

issue

1

eissn

1521-6543

issn

1521-6551

journal_volume

49

pub_type

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