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在缓步动物(水熊虫)的非横纹肌中检测到一种肌钙蛋白I样蛋白。

Detection of a troponin I-like protein in non-striated muscle of the tardigrades (water bears).

作者信息

Obinata Takashi, Ono Kanako, Ono Shoichiro

机构信息

Department of Biology; Faculty of Science; Chiba University; Chiba, Japan.

出版信息

Bioarchitecture. 2011 Mar;1(2):96-102. doi: 10.4161/bioa.1.2.16251.

Abstract

Tardigrades, also known as water bears, have somatic muscle fibers that are responsible for movement of their body and legs. These muscle fibers contain thin and thick filaments in a non-striated pattern. However, the regulatory mechanism of muscle contraction in tardigrades is unknown. In the absence of extensive molecular and genomic information, we detected a protein of 31 kDa in whole lysates of tardigrades that cross-reacted with the antibody raised against nematode troponin I (TnI). TnI is a component of the troponin complex that regulates actin-myosin interaction in a Ca(2+)-dependent and actin-linked manner. This TnI-like protein was co-extracted with actin in a buffer containing ATP and EGTA, which is known to induce relaxation of a troponin-regulated contractile system. The TnI-like protein was specifically expressed in the somatic muscle fibers in adult animals and partially co-localized with actin filaments in a non-striated manner. Interestingly, the pharyngeal muscle did not express this protein. These observations suggest that the non-striated somatic muscle of tardigrades has an actin-linked and troponin-regulated system for muscle contraction.

摘要

缓步动物,也被称为水熊虫,其体肌纤维负责身体和腿部的运动。这些肌纤维含有呈非横纹模式的细肌丝和粗肌丝。然而,缓步动物肌肉收缩的调节机制尚不清楚。在缺乏广泛的分子和基因组信息的情况下,我们在缓步动物的全细胞裂解物中检测到一种31 kDa的蛋白质,它与针对线虫肌钙蛋白I(TnI)产生的抗体发生交叉反应。TnI是肌钙蛋白复合体的一个组成部分,它以钙依赖和肌动蛋白连接的方式调节肌动蛋白-肌球蛋白的相互作用。这种类TnI蛋白在含有ATP和EGTA的缓冲液中与肌动蛋白共同提取,已知该缓冲液可诱导肌钙蛋白调节的收缩系统松弛。类TnI蛋白在成年动物的体肌纤维中特异性表达,并以非横纹的方式与肌动蛋白丝部分共定位。有趣的是,咽肌不表达这种蛋白质。这些观察结果表明,缓步动物的非横纹体肌具有一个肌动蛋白连接和肌钙蛋白调节的肌肉收缩系统。

相似文献

2
Regulation of contraction in striated muscle.横纹肌收缩的调节。
Physiol Rev. 2000 Apr;80(2):853-924. doi: 10.1152/physrev.2000.80.2.853.

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