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Enhancement of GTP gamma S-binding activity by cAMP-dependent phosphorylation of a filamin-like 250 kDa membrane protein in human platelets.

Abstract：

:The treatment of human platelets with the dibutyryl cyclic AMP (dbcAMP) revealed the presence of a 250 kDa protein which enhanced its GTP-binding activity. This protein was purified from platelet membranes by successive chromatographies on DEAE-cellulose, Ultrogel AcA34, Mono Q, HCA-hydroxyapatite, and TSK-3000SW columns. The positive cross-reaction of the 250 kDa protein with the anti-filamin antibody indicated that this protein is filamin or very close to it. The GTP gamma S-binding activity of this protein, when phosphorylated with cyclic AMP-dependent protein kinase (A-kinase), showed an over tenfold increase, with the specific activity being 3.6 nmol/mg protein. Dephosphorylation of the phosphorylated protein with alkaline phosphatase reduced the GTP gamma S-binding activity to the control untreated level.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yada Y,Okano Y,Nozawa Y

doi

10.1016/s0006-291x(05)80202-5

subject

Has Abstract

pub_date

1990-10-15 00:00:00

pages

256-61

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)80202-5

journal_volume

172

pub_type

杂志文章

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