Effects of Ca** (2) + and protein kinase C on the chick myoblast differentiation
1989
Chung, K.W. | Kim, S.J. | Park, J.W. | Lee, C.C. (Seoul National Univ., Seoul (Korea R.). Dept. of Zoology) | Park, Y.C. (Konju Teacher's Coll., Kongju (Korea R.). Dept. of Biology Education)
Alteration of intracellular calcium ion concentration by adding of either calcium ionophore A23187 or EGTA in culture medium at 24 hr after cell plating resulted in remarkable changes in the progression of differentiation of chick embryo myoblast. When separated myoblast protein using two-dimensional gel electrophoresis, synthesis patterns of several proteins changed upon the addition of either A23187 or EGTA. Treatment of A23187 and calcium-activated neutral protease at 24 hr after initial plating caused an increase in the rate of fusion compared to control culture. However, EGTA inhibited the myoblast fusion to a marked degree. A23187 treated at 24 hr also increased the activity of protein kinase C during the fusion-progressed period. It seems that intracellular calcium ion plays an important role in the myoblast differentiation in vitro together with the protein kinase C and calcium-activated neutral protease
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