Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle

被引:99
作者
Fukuda, N
Wu, YM
Farman, G
Irving, TC
Granzier, H [1 ]
机构
[1] Washington State Univ, Dept Vet & Comparat Anat Pharmacol & Physiol, Pullman, WA 99164 USA
[2] IIT, Dept Biol Chem & Phys Sci, Chicago, IL 60616 USA
来源
JOURNAL OF PHYSIOLOGY-LONDON | 2003年 / 553卷 / 01期
关键词
D O I
10.1113/jphysiol.2003.049759
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
We have explored the role of the giant elastic protein titin in the Frank-Starling mechanism of the heart by measuring the sarcomere length (SL) dependence of activation in skinned cardiac muscles with different titin-based passive stiffness characteristics. We studied muscle from the bovine left ventricle (BLV), which expresses a high level of a stiff titin isoform, and muscle from the bovine left atrium (BLA), which expresses more compliant titin isoforms. Passive tension was also varied in each muscle type by manipulating the pre-history of stretch prior to activation. We found that the SL-dependent increases in Ca2+ sensitivity and maximal Ca2+-activated tension were markedly more pronounced when titin-based passive tension was high. Small-angle X-ray diffraction experiments revealed that the SL dependence of reduction of interfilament lattice spacing is greater in BLV than in BLA and that the lattice spacing is coupled with titin-based passive tension. These results support the notion that titin-based passive tension promotes actomyosin interaction by reducing the lattice spacing. This work indicates that titin may be a factor involved in the Frank-Starling mechanism of the heart by promoting actomyosin interaction in response to stretch.
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页码:147 / 154
页数:8
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