Inhibitory effect of glycyrrhizin on polypeptide phosphorylation by polypeptide-dependent protein kinase (kinase P) in vitro.

Abstract

The anti-viral mechanism of glycyrrhizin (GL) has been investigated by considering in vitro effects on polypeptide phosphorylation. It was found that GL (i), at low doses, selectively inhibits protein phosphorylation by Kinase P, but has not significant effects on the activities of other kinases (Kinase A, Kinase C and histone kinase); (ii) binds directly to Kinase P and reduces kinase activity in a dose-dependent manner; and (iii) inhibits vesicular stomatitis virus (VSV)-associated kinase activity. These observations strongly suggest that direct binding of GL to the virus causes the direct inactivation of virus-associated kinase and the reduction of the viral infectivity.

• Authors: K Ohtsuki, N Iahida
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 157 Issue 2 Pg. 597-604 (Dec 15 1988) ISSN: 0006-291X [Print] United States
• PMID: 2849432 (Publication Type: Journal Article)

Chemical References

• Caseins
• Phosphoproteins
• Protein Kinase Inhibitors
• Viral Core Proteins
• Viral Nonstructural Proteins
• Glycyrrhizic Acid
• protein kinase P
• Protamine Kinase
• Protein Serine-Threonine Kinases
• Protein Kinase C
• Glycyrrhetinic Acid

Topics

• Capsid (metabolism)
• Caseins (metabolism)
• Glycyrrhetinic Acid (analogs & derivatives, pharmacology)
• Glycyrrhizic Acid
• HeLa Cells
• In Vitro Techniques
• Phosphoproteins (metabolism)
• Protamine Kinase (antagonists & inhibitors)
• Protein Kinase C (antagonists & inhibitors)
• Protein Kinase Inhibitors
• Protein Serine-Threonine Kinases
• Vesicular stomatitis Indiana virus (enzymology)
• Viral Core Proteins (metabolism)
• Viral Nonstructural Proteins