Phosphorylation of a tropomyosin-like (30 KD) protein during platelet activation.

Abstract:

:In this study, we have used the tumor promoter 12-o-tetradecanoylphorbol-13-acetate (TPA), as well as its biologically inactive analogue 4 alpha-phorbol 12,13-didecanoate (4 alpha-PDD), to investigate platelet protein phosphorylation and its possible correlation with platelet activation. Our data show that TPA, but not 4 alpha-PDD, induces a preferential phosphorylation of a 30,000 dalton (30 KD) protein. This phosphoprotein is found to be physically associated with an actomyosin-containing platelet cytoskeleton complex. Further analysis using both standard two-dimensional gel electrophoresis and one-dimensional urea-SDS gel electrophoresis reveals that this 30 KD protein has several tropomyosin-like properties. Most importantly, the degree of TPA-induced phosphorylation of the 30 KD protein is directly proportional to the extent of platelet granule release and the shape change of the platelet, as well as to the degree of aggregation. We speculate that this phosphorylated tropomyosinlike protein may play a pivotal role in the regulation of actomyosin-mediated platelet contractility, which has been previously implicated in a variety of platelet functions.

journal_name

J Cell Biochem

authors

Bourguignon LY,Field S,Bourguignon GJ

doi

10.1002/jcb.240290103

subject

Has Abstract

pub_date

1985-01-01 00:00:00

pages

19-30

issue

1

eissn

0730-2312

issn

1097-4644

journal_volume

29

pub_type

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