• Title/Summary/Keyword: inhibition of protein phosporylation

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Protein Fraction from Panax ginseng C.A. Meyer Results the Glycogen Contents by Modulating the Protein Phosphorylation in Rat Liver (고려홍삼 단백질분획의 쥐간 단백질 인산화 조절에 의한 글리코겐 함량조절)

  • Park, Hwa-Jin;Rhee, Man-Hee;Park, Kyeong-Mee;No, Young-Hee;Lee, Hee-Bong
    • Journal of Ginseng Research
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    • v.18 no.2
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    • pp.102-107
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    • 1994
  • When at liver homogenates were incubated with 1mM $CCl_4$ for five min, glycogen level was decreased, while treatment with protein fraction $G_4$ increased the glycogen level. In addition $G_4$ inhibited the phosphorylation of 34 KD and 118 KD polypeptides induced by $CCl_4$. These protein were more strongly phosphorylated by $Ca^{2+}$/calmodulin-dependent kinase than by C-kinase. Since 34 KD polypeptide was solely phosphorylated by NaF (50mM), an inhibitor of both glycogen syntheses and phosphoprotein phosphates, it is inferred that 3 KD polypeptide is glycogen synthase-likd protein. Because glycogen synthesis is inhibited by phosphorylation of $Ca^{2+}$-dependent glycogen syntheses, it is suggested that $G_4$ increased liver glycogen level by inhibiting phosphorylation of 34 KD polypeptide which is thought to glycogen syntheses-like protein.

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