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Differentiative action of K252a on protein kinase C and a calcium-unresponsive, phorbol ester/phospholipid-activated protein kinase.

Abstract：

:The Triton X-100 extract of the particulate fraction of porcine spleen contains a protein kinase which can be activated by phospholipid and the phorbol ester TPA but does not respond to phospholipid and calcium. The partially purified kinase has a molecular weight of 76 kDa (p76-kinase) and hence is somewhat smaller than the similarly behaving p82-kinase from mouse epidermis and spleen. The p76-kinase shows strong autophosphorylation. The protein kinase inhibitor K252a clearly differentiates between the Ca2+-unresponsive p76-kinase and Ca2+-responsive PKC. At concentrations of up to 5 x 10(-7)M it fails to suppress p76-kinase-catalyzed autophosphorylation and histone phosphorylation, but it inhibits PKC-catalyzed phosphorylation up to 50%. The IC50 values of K252a regarding PKC and the p76-kinase differ by two orders of magnitude. At low concentrations, K252a appears to slightly activate further TPA-activated p76-kinase. It is not able, however, to replace TPA and to stimulate the p76-kinase in the presence of phospholipid alone.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Gschwendt M,Leibersperger H,Marks F

doi

10.1016/0006-291x(89)91765-8

subject

Has Abstract

pub_date

1989-11-15 00:00:00

pages

974-82

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)91765-8

journal_volume

164

pub_type

杂志文章

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