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软体动物“抓握”肌肉的高效保持功能不是基于肌球蛋白头部减速的横桥循环。

The highly efficient holding function of the mollusc 'catch' muscle is not based on decelerated myosin head cross-bridge cycles.

机构信息

Department of Cell Biology, University of Salzburg, , Hellbrunnerstr. 34, A-5020 Salzburg, Austria.

出版信息

Proc Biol Sci. 2010 Mar 7;277(1682):803-8. doi: 10.1098/rspb.2009.1618. Epub 2009 Nov 11.

DOI:10.1098/rspb.2009.1618
PMID:19906664
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2842747/
Abstract

Certain smooth muscles are able to reduce energy consumption greatly when holding without shortening. For instance, this is the case with muscles surrounding blood vessels used for regulating blood flow and pressure. The phenomenon is most conspicuous in 'catch' muscles of molluscs, which have been used as models for investigating this important physiological property of smooth muscle. When the shells of mussels are held closed, the responsible muscles enter the highly energy-efficient state of catch. According to the traditional view, the state of catch is caused by the slowing down of the force-generating cycles of the molecular motors, the myosin heads. Here, we show that catch can still be induced and maintained when the myosin heads are prevented from generating force. This new evidence proves that the long-held explanation of the state of catch being due to the slowing down of force producing myosin head cycles is not valid and that the highly economic holding state is caused by the formation of a rigid network of inter-myofilament connections based on passive molecular structures.

摘要

某些平滑肌在不缩短的情况下能够大大降低能量消耗。例如,血管周围用于调节血流量和血压的肌肉就是这种情况。这种现象在软体动物的“捕捉”肌肉中最为明显,这些肌肉被用作研究平滑肌这一重要生理特性的模型。当贻贝的贝壳被紧紧关闭时,负责的肌肉进入高度节能的捕捉状态。根据传统观点,捕捉状态是由产生力的分子马达,肌球蛋白头部的运动速度减慢引起的。在这里,我们表明,即使阻止肌球蛋白头部产生力,也可以诱导和维持捕捉状态。这一新的证据证明,长期以来关于捕捉状态是由于产生力的肌球蛋白头部循环速度减慢的解释是不正确的,而高度经济的保持状态是由基于被动分子结构的肌丝间连接的刚性网络的形成引起的。

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Proc Biol Sci. 2010 Mar 7;277(1682):803-8. doi: 10.1098/rspb.2009.1618. Epub 2009 Nov 11.
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本文引用的文献

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The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk.肌联蛋白-伴肌动蛋白复合体是肌肉Z盘处一种定向的、超稳定分子键。
Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13307-133310. doi: 10.1073/pnas.0902312106. Epub 2009 Jul 21.
2
Twitchin of mollusc smooth muscles can induce "catch"-like properties in human skeletal muscle: support for the assumption that the "catch" state involves twitchin linkages between myofilaments.软体动物平滑肌的抽搐可以在人体骨骼肌中引起类似“捕获”的特性:这支持了“捕获”状态涉及肌丝之间的抽搐连接的假设。
J Comp Physiol B. 2009 Nov;179(8):945-50. doi: 10.1007/s00360-009-0375-z. Epub 2009 Jun 20.
3
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J Muscle Res Cell Motil. 2008;29(2-5):73-99. doi: 10.1007/s10974-008-9149-6. Epub 2008 Nov 28.
4
Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.未磷酸化的肌动蛋白结合蛋白与肌动蛋白和肌球蛋白形成复合物,这可能有助于维持强直收缩中的张力。
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9
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