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The stimulatory and inhibitory effects of glycyrrhizin and a glycyrrhetinic acid derivative on phosphorylation of lipocortin I by A-kinase in vitro.

Authors
  • Ohtsuki, K
  • Oh-Ishi, M
  • Nagata, N
Type
Published Article
Journal
Biochemistry international
Publication Date
Dec 01, 1992
Volume
28
Issue
6
Pages
1045–1053
Identifiers
PMID: 1290459
Source
Medline
License
Unknown

Abstract

The effects of GL and oGA on the activity (phosphorylation of lipocortin I) by A-kinase were investigated in vitro. It was found that (i) phosphorylation of the 35-36 kDa polypeptide by A-kinase was inhibited selectively when the partially purified kinase fraction from EAT cells was incubated with [gamma-32P]ATP in the presence of 60 microM oGA; (ii) the marked polypeptide was identified as a lipocortin I; and (iii) the activity of the kinase was stimulated about 4-fold by 5 microM oGA, but it was inhibited at doses above 25 microM. The drug-induced inhibition of phosphorylation of lipocortin I by A-kinase may be implicated in the anti-inflammatory effect of the drugs.

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