The giant muscle protein titin is an adjustable molecular spring

被引：55

作者：

Granzier, HL

Labeit, S

机构：

[1] Washington State Univ, Dept Vet & Comparat Anat Pharmacol & Physiol, Pullman, WA 99164 USA

[2] Univ Klinikum Mannheim, Inst Anasthesiol & Operat Intens Med, Mannheim, Germany

来源：

EXERCISE AND SPORT SCIENCES REVIEWS | 2006年 / 34卷 / 02期

关键词：

titin; passive force; differential splicing; posttranslational modification; muscle mechanics; mechanosensing;

D O I：

10.1249/00003677-200604000-00002

中图分类号：

Q4 [生理学];

学科分类号：

071003 ;

摘要：

When muscles are stretched, the giant protein titin develops passive force. Titin's force performs important functions that include maintaining the structural integrity of the sarcomere and triggerng signal transduction pathways. We propose that the mechanical properties of titin can be tuned according to the mechanical demands placed on muscle, using mechanisms that include alternative splicing and posttranslational modifications.

引用

收藏

页码：50 / 53

页数：4

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