Polarity and length of actin filaments at the fascia adherens of the cardiac intercalated disk

M. Yamaguchi, S. Yamano, M. Muguruma, R.M. Robson
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引用次数: 18

Abstract

Digestion of canine and bovine intercalated disks with a calcium-activated protease (CAF) removes the electron-dense material similar to that found at the Z-line and presumably consisting primarily of α-actinin. The major filaments exposed by CAF are actin, andthe polarity is away from the intercalated disk, as was confirmed by decoration with heavy meromyosin. The length of actin filaments associated with the fascia adherens region at the concave region is 1.2- to 2.2-fold that of actin filaments (I-filaments) in the sarcomere and varies depending on the interdigitation of the membrane at the cell junction. Actin filaments at the intercalated disk seem to be attached (or very close) to the membrane in a direct, rather than looping, manner.

肌动蛋白丝的极性和长度在心脏间插盘的筋膜粘附
用钙活化蛋白酶(CAF)消化犬和牛的插片,去除类似于在z线上发现的电子密集物质,可能主要由α-肌动蛋白组成。CAF暴露的主要纤维是肌动蛋白,其极性远离嵌入的椎间盘,这是由大量的肌凝蛋白装饰证实的。与凹区筋膜粘附区相关的肌动蛋白丝的长度是肌节中肌动蛋白丝(i -丝)的1.2- 2.2倍,并根据细胞连接处膜的交错而变化。嵌入盘上的肌动蛋白丝似乎以一种直接而非环状的方式附着(或非常接近)在膜上。
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