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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/7984


    Title: Involvement of mu- and m-calpains and protein kinase C isoforms in L8 myoblast differentiation
    Authors: Liang, Y. C.;Yeh, J. Y.;Forsberg, N. E.;Ou, B. R.
    Contributors: Department of Biotechnology
    Keywords: Calpains;Antisense oligonucleotide;Protein kinase C;L8 myoblast
    Date: 2006
    Issue Date: 2010-03-15 08:11:06 (UTC+0)
    Publisher: Asia University
    Abstract: The objectives were to investigate the roles of different calpains and protein kinase C (PKC) isoforms in muscle differentiation. Concentrations of - and m-calpain increased significantly whereas PKC and declined significantly during L8 myoblast differentiation. Both -calpain and m-calpain antisense oligonucleotides inhibited myotube formation and creatine kinase activity during L8 myoblast differentiation. These results implied that both - and m-calpain were involved in L8 myoblast differentiation. To investigate the involvement of calpain in regulation of PKC concentrations, -calpain antisense oligonucleotides were added to L8 myoblasts. PKC remained unchanged and PKC declined. By adding m-calpain antisense oligonucleotides instead, PKC level remained unchanged and PKC concentrations increased significantly during differentiation. These results suggest that PKC , but not PKC , is the substrate for -calpain and PKC and 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 PKC mediated by m- and -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: The International Journal of Biochemistry & Cell Biology 38(4):662-70
    Appears in Collections:[Department of Biotechnology] Journal Article

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