A survey of in situ sarcomere extension in mouse skeletal muscle

被引:23
作者
Goulding, D [1 ]
Bullard, B [1 ]
Gautel, M [1 ]
机构
[1] EUROPEAN MOL BIOL LAB,STRUCT BIOL DIV,D-69012 HEIDELBERG,GERMANY
关键词
D O I
10.1023/A:1018650915751
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The giant molecule titin/connectin was demonstrated to connect the ends of thick filaments with the Z-disks and thus to provide an elastic connection that seems to be responsible for passive tension in striated muscle. To investigate the physiological limits of I-band titin extension in skeletal muscle, we have measured sarcomere lengths of a number of mouse postural and clonal muscles ii? situ under the constraints imposed by the skeletal, ligamentous and tendinous components of the motile apparatus. These values now give upper limits for the extension of the I-band and therefore for the maximal degree of titin extension under physiological constraints. We find that I-band extension in all muscles investigated does not exceed a factor of approximate to 2.5 in situ, which is well below values obtainable in isolated fibre preparations. Approach to the yield-point is therefore prevented by extramuscular mechanisms. Sarcomere lengths near the tendinous junction and within the muscle are virtually identical in extended muscle, suggesting that a major function of titin in intact muscle is to ensure uniform sarcomere lengths over the entire muscle length and thus to prevent localized myofibril overstretch during isometric contraction.
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收藏
页码:465 / 472
页数:8
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