Bi-directional regulation of ginsenoside Re on smooth muscle myosin of gizzard

Abstract

The ginsenoside Re is the major ingredient of ginsenosides, which was isolated from ginseng (genus Panax). The purpose of the study is to investigate into the effect of ginsenoside Re on Mg2+-ATPase activity of smooth muscle myosin and phosphorylation of myosin light chain by myosin light chain kinase (MLCK), and try to find out the regular pattern resulting from ginsenoside Re on myosin function. Myosin and MLCK used in our study were purified from the chicken gizzard smooth muscle. Myosin phorphorylation was determined by glycerol polyacrylamide gel electrophoresis (PAGE). Myosin Mg2+-ATPase activity was measured by Pi liberation method. The results showed that ginsenoside Re stimulates Mg2+-ATPase activities, promotes phosphorylation of partially phosphorylated myosin, inhibits Mg2+-ATPase activity and decrease phosphorylation of fully phosphorylated myosin in a dose dependent manner and in a time dependent manner. The findings demonstrated that the use of ginsenoside Re on various states of myosin phosphorylation produced different responses in a purified incubation system. Key words: Ginsenoside Re, myosin phosphorylation, myosin Mg2+-ATPase activity, bi-directional regulation.