INVOLVEMENT OF TRANSGLUTAMINASE IN MYOFIBRIL ASSEMBLY OF CHICK EMBRYONIC MYOBLASTS IN CULTURE

被引:17
作者
KANG, SJ
SHIN, KS
SONG, WK
HA, DB
CHUNG, CH
KANG, MS
机构
[1] SEOUL NATL UNIV,COLL NAT SCI,DEPT BIOL MOLEC,SEOUL 151742,SOUTH KOREA
[2] SEOUL NATL UNIV,CELL DIFFERENTIAT RES CTR,SEOUL 151742,SOUTH KOREA
[3] KWANGJU INST SCI & TECHNOL,DEPT LIFE SCI,KWANGJU 506303,SOUTH KOREA
关键词
D O I
10.1083/jcb.130.5.1127
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Involvement of transglutaminase in myofibrillogenesis of chick embryonic myoblasts has been investigated in vitro, Both the activity and protein level of transglutaminase initially decreased to a minimal level at the time of burst of myoblast fusion but gradually increased thereafter. The localization of transglutaminase underwent a dramatic change from the whole cytoplasm in a diffuse pattern to the cross-striated sarcomeric A band, being strictly colocalized with the myosin thick filaments. For a brief period prior to the appearance of cross-striation, transglutaminase was localized in nonstriated filamental structures that coincided with the stress fiber-like structures. When 12-o-tetradecanoyl phorbol acetate was added to muscle cell cultures to induce the sequential disassembly of thin and thick filaments, transglutaminase was strictly colocalized with the myosin thick filaments even in the myosacs, of which most of the thin filaments were disrupted. Moreover, monodansylcadaverine, a competitive inhibitor of transglutaminase, reversibly inhibited the myofibril maturation. In addition, myosin heavy chain behaved as one of the potential intracellular substrates for transglutaminase. The cross-linked myosin complex constituted approximately 5% of the total Triton X-100-insoluble pool of myosin molecules in developing muscle cells, and its level was reduced to below 1% upon treatment with monodansylcadaverine. These results suggest that transglutaminase plays a crucial role in myofibrillogenesis of developing chick skeletal muscle.
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页码:1127 / 1136
页数:10
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