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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/16245


    Title: Involvement of mu- and m-calpains and protein kinase C isoforms in L8 myoblast differentiation
    Authors: 葉貞吟;Yeh, Jan-Ying
    Contributors: 生物科技學系
    Keywords: Calpains;Antisense oligonucleotide;Protein kinase C;L8 myoblast
    Date: 2006-04
    Issue Date: 2012-11-23 17:10:26 (UTC+8)
    Abstract: The objectives were to investigate the roles of different calpains and protein kinase C (PKC) isoforms in muscle differentiation. Concentrations of mu- and m-calpain increased significantly whereas PKCalpha and delta declined significantly during L8 myoblast differentiation. Both mu-calpain and m-calpain antisense oligonucleotides inhibited myotube formation and creatine kinase activity during L8 myoblast differentiation. These results implied that both mu- and m-calpain were involved in L8 myoblast differentiation. To investigate the involvement of calpain in regulation of PKC concentrations, mu-calpain antisense oligonucleotides were added to L8 myoblasts. PKCalpha remained unchanged and PKCdelta declined. By adding m-calpain antisense oligonucleotides instead, PKCalpha level remained unchanged and PKCdelta concentrations increased significantly during differentiation. These results suggest that PKCalpha, but not PKCdelta, is the substrate for mu-calpain and PKCalpha and delta are the substrates for the m-calpain. In addition, more phosphorylated myogenin was found in day 2 antisense oligonucleotides treated L8 cells. It is concluded that the decline of PKCalpha mediated by m- and mu-calpain is essential for L8 myoblast differentiation. The decline of PKC during myoblast differentiation may cause hypo-phosphorylation of myogenin, which in turn activates muscle-specific genes during myogenesis.
    Relation: INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, V.38 N.4:662–670.
    Appears in Collections:[生物科技學系] 期刊論文

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