Skeletal muscle myosin cross-bridge cycling is necessary for myofibrillogenesis

被引:35
作者
Ramachandran, I [1 ]
Terry, M [1 ]
Ferrari, MB [1 ]
机构
[1] Univ Missouri, Sch Biol Sci, Div Mol Biol & Biochem, Kansas City, MO 64110 USA
来源
CELL MOTILITY AND THE CYTOSKELETON | 2003年 / 55卷 / 01期
关键词
muscle differentiation; myosin inhibitor; striated; sarcomere; tension; BTS;
D O I
10.1002/cm.10113
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A major stimulus affecting myofibrillogenesis in both embryonic and mature striated muscle is contractile activity. There are two major signals associated with contractile activity: a physiological signal, the transient increase in intracellular calcium, and a physical signal, the transient increase in tension production. However, dissociating these two signals to examine their relative contributions to myofibrillogenesis has proven difficult. In this study, we have used two different myosin inhibitors to determine the importance of myosin cross-bridge cycling in sarcomere assembly. We find that the small-molecule inhibitor 2,3-butanedione monoxime (BDM), which inhibits myosin ATPase, disrupts myofibrillogenesis in amphibian myocytes, consistent with results from avian studies. However, BDM is a weak myosin inhibitor and it is non-specific; concentrations that inhibit contraction and disrupt myofibrillogenesis also disrupt calcium signaling. Therefore, we also used the recently identified skeletal muscle myosin II inhibitor, N-benzyl-p-toluenesulphonamide (BTS), which has high affinity and specificity for skeletal muscle fast myosin. BTS inhibits contraction and results in myofibrillar disruption that phenocopies our results with BDM. However, BTS does not affect either spontaneous or induced calcium transients. Furthermore, BTS is reversible and does not significantly affect the expression levels of myosin or actin. Thus, our convergent results with BDM and BTS suggest that sarcomere assembly depends on active regulation of tension in the forming myofibril. (C) 2003 Wiley-Liss, Inc.
引用
收藏
页码:61 / 72
页数:12
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