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[心肌肌球蛋白与心肌收缩]

[Cardiac myosins and myocardial contraction].

作者信息

Schiaffino S, Gorza L

出版信息

G Ital Cardiol. 1986 Aug;16(8):680-95.

PMID:2947827
Abstract

The contractile properties of cardiac muscle cells are determined by the molecular composition of the contractile apparatus and in particular by the structure of myosin. Three isoforms of myosin heavy chains have been recently identified in the mammalian heart: alpha and beta myosin heavy chains, present in atrial and ventricular myocardium, and nodal myosin heavy chain, present in sino-atrial and atrio-ventricular nodes. The alpha and beta isoforms are coded by two distinct genes whose expression is tissue and developmental stage-specific, and can be regulated by hormonal and mechanical factors. The relative concentration of the two isoforms is correlated with the maximal velocity of shortening and with the energy cost of force generation. In hyperthyroid myocardium the predominant isoform is the alpha, high ATPase myosin heavy chain and the contraction is fast but less economical; in hypothyroid and in mechanically overloaded myocardium the beta, low ATPase isoform is predominant and the contraction is slower and more economical.

摘要

心肌细胞的收缩特性由收缩装置的分子组成决定,尤其由肌球蛋白的结构决定。最近在哺乳动物心脏中鉴定出三种肌球蛋白重链同工型:α和β肌球蛋白重链,存在于心房和心室心肌中;以及节点肌球蛋白重链,存在于窦房结和房室结中。α和β同工型由两个不同的基因编码,其表达具有组织和发育阶段特异性,并且可受激素和机械因素调节。这两种同工型的相对浓度与最大缩短速度以及产生力的能量消耗相关。在甲状腺功能亢进的心肌中,主要的同工型是α,即高ATP酶肌球蛋白重链,收缩速度快但经济性较差;在甲状腺功能减退和机械性负荷过重的心肌中,β,即低ATP酶同工型占主导,收缩较慢且更经济。

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