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温度或离子强度变化对分离的兔和鱼骨骼肌粗肌丝的影响。

The effects of changes in temperature or ionic strength on isolated rabbit and fish skeletal muscle thick filaments.

作者信息

Kensler R W, Peterson S, Norberg M

机构信息

Division of Cell Biology and Biophysics, School of Biological Sciences, University of Missouri at Kansas City 64108.

出版信息

J Muscle Res Cell Motil. 1994 Feb;15(1):69-79. doi: 10.1007/BF00123834.

DOI:10.1007/BF00123834
PMID:8182111
Abstract

Although the skeletal muscles of different vertebrate species have been assumed to be generally similar, recent X-ray diffraction and mechanical studies have demonstrated differences in the responses of these muscles to changes in physiological conditions. X-ray diffraction studies have indicated that lowering the temperature and lowering ionic strength may affect the crossbridge arrangement of rabbit thick filaments. Similar X-ray diffraction studies on the structural effects of lowering ionic strength in frog and fish muscles are less clear in interpretation, while lowering the temperature appears to have little effect in these muscles. In the present study we have compared the effects of lowering the temperature or ionic strength on the crossbridge order of isolated rabbit and fish thick filaments as observed in the electron microscope. In agreement with the X-ray results, rabbit filaments show a distinct loss of crossbridge order when stained at 4 degrees C compared to 25 degrees C, whereas fish thick filaments appear similar at both temperatures. Rabbit thick filaments, when diluted to one-fourth of the normal ionic strength (while maintaining constant EGTA and ATP concentration), showed a strong tendency to bind to actin filaments, while similarly-treated fish filaments showed little tendency to aggregate or become disordered. These results appear to support the X-ray diffraction results of other investigators, and the idea that effects of ionic strength or temperature on muscle may vary with species.

摘要

尽管不同脊椎动物物种的骨骼肌通常被认为是相似的,但最近的X射线衍射和力学研究表明,这些肌肉对生理条件变化的反应存在差异。X射线衍射研究表明,降低温度和降低离子强度可能会影响兔粗肌丝的横桥排列。关于降低青蛙和鱼类肌肉离子强度的结构效应的类似X射线衍射研究,其解释不太明确,而降低温度在这些肌肉中似乎影响不大。在本研究中,我们比较了降低温度或离子强度对电子显微镜下观察到的分离兔和鱼粗肌丝横桥排列的影响。与X射线结果一致,与25℃相比,兔肌丝在4℃染色时横桥排列明显丧失,而鱼粗肌丝在两个温度下看起来相似。兔粗肌丝在稀释至正常离子强度的四分之一时(同时保持EGTA和ATP浓度恒定),表现出强烈的与肌动蛋白丝结合的倾向,而经过类似处理的鱼肌丝几乎没有聚集或变得无序的倾向。这些结果似乎支持了其他研究者的X射线衍射结果,以及离子强度或温度对肌肉的影响可能因物种而异的观点。

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Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.肌球蛋白头部有助于维持兔肌肉松弛时的纤维秩序。

本文引用的文献

1
High-resolution equatorial x-ray diffraction from single skinned rabbit psoas fibers.来自单根去皮肤兔腰大肌纤维的高分辨率赤道X射线衍射
Biophys J. 1986 Jan;49(1):133-5. doi: 10.1016/S0006-3495(86)83623-2.
2
Polypeptide chains of intermediate molecular weight in myosin preparations.肌球蛋白制剂中中等分子量的多肽链。
FEBS Lett. 1971 Jun 2;15(1):40-44. doi: 10.1016/0014-5793(71)80075-3.
3
Structural changes in the actomyosin cross-bridges associated with force generation.与力产生相关的肌动球蛋白横桥的结构变化。
Biophys J. 2010 Sep 22;99(6):1827-34. doi: 10.1016/j.bpj.2010.06.072.
4
Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.哺乳动物心肌粗肌丝:其周期性及与肌动蛋白的相互作用。
Biophys J. 2002 Mar;82(3):1497-508. doi: 10.1016/S0006-3495(02)75503-3.
5
Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments.肌球蛋白轻链磷酸化影响兔骨骼肌粗肌丝的结构。
Biophys J. 1996 Aug;71(2):898-907. doi: 10.1016/S0006-3495(96)79293-7.
6
Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers.在去皮肤肌纤维中ATP光释放后肌球蛋白调节轻链的取向变化
Biophys J. 1996 Apr;70(4):1847-62. doi: 10.1016/S0006-3495(96)79750-3.
7
The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement.鸡的肌肉粗肌丝:温度与松弛状态下的横桥排列
J Muscle Res Cell Motil. 1995 Feb;16(1):79-90. doi: 10.1007/BF00125312.
Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5252-6. doi: 10.1073/pnas.90.11.5252.
4
The relaxed crossbridge pattern in isolated rabbit psoas muscle thick filaments.分离的兔腰大肌粗肌丝中的松弛横桥模式。
J Cell Sci. 1993 Jul;105 ( Pt 3):841-8. doi: 10.1242/jcs.105.3.841.
5
Evidence for cross-bridge attachment in relaxed muscle at low ionic strength.低离子强度下松弛肌肉中横桥附着的证据。
Proc Natl Acad Sci U S A. 1982 Dec;79(23):7288-91. doi: 10.1073/pnas.79.23.7288.
6
A model of myosin crossbridge structure consistent with the low-angle x-ray diffraction pattern of vertebrate muscle.一种与脊椎动物肌肉的低角度X射线衍射图谱相符的肌球蛋白横桥结构模型。
J Muscle Res Cell Motil. 1980 Jun;1(2):177-91. doi: 10.1007/BF00711798.
7
Determination of the handedness of the crossbridge helix of Limulus thick filaments.鲎粗肌丝横桥螺旋手性的测定。
J Muscle Res Cell Motil. 1982 Sep;3(3):349-61. doi: 10.1007/BF00713042.
8
Frog skeletal muscle thick filaments are three-stranded.青蛙骨骼肌粗肌丝由三股组成。
J Cell Biol. 1983 Jun;96(6):1797-802. doi: 10.1083/jcb.96.6.1797.
9
X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths.在不同离子强度下,松弛肌纤维中横桥形成的X射线衍射证据。
Biophys J. 1984 Sep;46(3):299-306. doi: 10.1016/S0006-3495(84)84026-6.
10
H-protein and X-protein. Two new components of the thick filaments of vertebrate skeletal muscle.H蛋白和X蛋白。脊椎动物骨骼肌粗肌丝的两种新成分。
J Mol Biol. 1983 Nov 5;170(3):675-98. doi: 10.1016/s0022-2836(83)80127-2.