Titin: A Tunable Spring in Active Muscle

被引：56
作者：
Nishikawa, Kiisa [1 ]
机构：
[1] No Arizona Univ, Dept Biol Sci, Box 5640, Flagstaff, AZ 86011 USA
来源：
PHYSIOLOGY | 2020年 / 35卷 / 03期
基金：
美国国家科学基金会;
关键词：
muscle activation; muscle mechanics; stiffness; shortening; stretch; RESIDUAL FORCE ENHANCEMENT; NON-CROSS-BRIDGE; SKELETAL-MUSCLE; FROG-MUSCLE; IMMUNOELECTRON MICROSCOPY; STRIATED-MUSCLE; PASSIVE TENSION; PEVK DOMAIN; CONTRACTILE PROPERTIES; CALCIUM SENSITIVITY;
D O I：
10.1152/physiol.00036.2019
中图分类号：
Q4 [生理学];
学科分类号：
071003 ;
摘要：
Muscle has conventionally been viewed as a motor that converts chemical to kinetic energy in series with a passive spring, but new insights emerge when muscle is viewed as a composite material whose elastic elements are tuned by activation. New evidence demonstrates that calcium-dependent binding of N2A titin to actin increases titin stiffness in active skeletal muscles, which explains many long-standing enigmas of muscle physiology.
引用
收藏
页码：209 / 217
页数：9
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