The In Vitro Effects of Glycyrrhizin and the Derivatives of Glycyrrhetinic Acid on the Activity of cAMP-Dependent Protein Kinase and Phosphorylation of Cellular Polypeptide by the Kinase from Ehrlich Ascites Tumor Cells

SHAMSA, F., NAGATA, N., On-ISHI, M. and OHTSUKI, K. The In Vitro Effects of Glycyrrhizin and the Derivatives of Glycyrrhetinic Acid on the Activity of cAMP-Dependent Protein Kinase and Phosphorylation of Cellular Polypeptide by the Kinase from Ehrlich Ascites Tumor Cells. Tohoku J. Exp. Med., 1991,...

Full description

Saved in:
Bibliographic Details
Published in:The Tohoku Journal of Experimental Medicine Vol. 165; no. 4; pp. 305 - 318
Main Authors: SHAMSA, FAZEL, NAGATA, NOBUYUKI, OH-ISHI, MASAMICHI, OHTSUKI, KENZO
Format: Journal Article
Language:English
Published: Japan Tohoku University Medical Press 1991
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:SHAMSA, F., NAGATA, N., On-ISHI, M. and OHTSUKI, K. The In Vitro Effects of Glycyrrhizin and the Derivatives of Glycyrrhetinic Acid on the Activity of cAMP-Dependent Protein Kinase and Phosphorylation of Cellular Polypeptide by the Kinase from Ehrlich Ascites Tumor Cells. Tohoku J. Exp. Med., 1991, 165 (4), 305-318-The effects of glycyrrhizin (GL) and the derivatives of glycyrrhetinic acid (GA) on the activity of cAMP-dependent protein kinase (A-kinase) and the phosphorylation of cellular polypeptides by the kinase purified from Ehrlich ascites tumor cells had been investigated in vitro. It was found that (i) the derivatives [3β-hydroxy-olean-11, 13 (18)-diene-30-oic acid Na, olean-9(11), 12 diene-3β, 30-diol-3β, 30-di-o-hemiphthalate 2Na and olean-12-ene-3β, 30-diol 3β, 30-di-o-phosphate 2Na] of GA inhibited the activity of A-kinase at the concentrations higher than 25μM; (ii), at 10μM, these derivatives and native GL stimulated the activity of the kinase significantly; and (iii) the inhibitory and stimulatory effects of some GA derivatives were clearly correlated with their chemical structures. Moreover, sodium dodecyl sulfate polyacrylamide gel electrophoresis and two dimensional gel electrophoresis followed by autoradiography detected several acidic polypeptides, including polypeptides with approximate molecular weights of 35, 000 (pI 4.3), 27, 000 (pI 4.5) and 18, 000-21, 000 (pI 4.5), phosphorylated by A-kinase, to be functioning as mediators in response to these drugs. This observation suggests that the GL-induced inhibition of phosphorylation of these cellular polypeptides by A-kinase may be physiologically implicated in the biochemical mechanisms involved in the anti-inflammatory effect of the drug.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0040-8727
1349-3329
DOI:10.1620/tjem.165.305