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Suppressive effect of transforming growth factor-beta on the phosphorylation of endogenous substrates by conventional and novel protein kinase C in primary cultured mouse epidermal cells.

Abstract：

:The effect of transforming growth factor-beta (TGF-beta) on the endogenous protein phosphorylation caused by phorbol 12-myristate 13-acetate (PMA), a potent activator of protein kinase C (PKC), was examined in primary cultured mouse epidermal cells. PMA markedly stimulates phosphorylation of endogenous proteins, i.e. KP-1 and KP-2, through Ca(2+)-dependent conventional PKC (cPKC), and KP-10 through Ca(2+)-independent novel PKC (nPKC) in intact epidermal cells. TGF-beta strongly suppressed the PMA-stimulated phosphorylation of these three proteins. Rate of dephosphorylation of these phosphorylated proteins was not affected by TGF-beta. Treatment of epidermal cells with TGF-beta decreased cPKC activity both in cytosolic and particulate fractions, but not nPKC activity. These results indicate that TGF-beta suppresses cPKC- and nPKC-mediated endogenous protein phosphorylation in intact epidermal cells, but the mechanisms of suppression are different.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Nishikawa K,Yamamoto S,Nagumo H,Otsuka C,Kato R

doi

10.1006/bbrc.1993.1635

subject

Has Abstract

pub_date

1993-05-28 00:00:00

pages

384-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71635-9

journal_volume

193

pub_type

杂志文章

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