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Effects of Butanol Fraction of Crataegi Fructus on the Translocation of PKC $\alpha$ and Myosin Phosphatase Subnits in Vascular Smooth Muscle  

Lee Heon Jae (Department of Physiology, College of Oriental Medicine, Dongguk University)
Choi Ho Jeong (Department of Physiology, College of Oriental Medicine, Dongguk University)
Kim Gil Whon (Department of Physiology, College of Oriental Medicine, Dongguk University)
Shin Heung Mook (Department of Physiology, College of Oriental Medicine, Dongguk University)
Publication Information
Journal of Physiology & Pathology in Korean Medicine / v.16, no.5, 2002 , pp. 1060-1065 More about this Journal
Abstract
LC20 phosphorylation and PKC α play an important role in modulation of contractile activity of smooth muscle. Besides, myosin phosphatase is also related with smooth muscle contraction in signaling pathways. We previously demonstrated that Crataegi Fructus inhibited phenylephrine-induced contraction and which might be implicated in nitrite formation(Son et al., 2002). In this study, we investigated the effects of butanol fraction of Crataegi Fructus(BFFC) on the localization of α-protein kinease C(PKC α) and myosin phosphatase subnits(MPs) in freshly isolated single ferret potal vein cells, and phosphorylation of LC20 during phenylephrine stimulation. In PKC α and MPs localization, BFFC blocked its translocation from the cytosol to the cell membrane by treatment of phenylephrine. BFFC have also dephosphorylated LC20 phosphorylation by phenylephrine stimulation under basal level, but no significant. These results indicate that the relaxation effect of BFFC is associated with inhibition of PKC α activation and MPs dissociation, and thus myosin phosphatase activity may be increased.
Keywords
Smooth muscle contraction; Butanol fraction of Crataegi Fructus(BFFC); PKC α; MPs localization; LC20 phosphorylation;
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Times Cited By KSCI : 1  (Citation Analysis)
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