Calponin

被引：43

作者：

ElMezgueldi, M

机构：

[1] Cardiac Medicine, Imp. Coll. Sch. of Med. at the Natl., London SW3 6LY, Dovehouse Street

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 1996年 / 28卷 / 11期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/S1357-2725(96)00085-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calponin is a troponin-T like protein purified from chicken gizzard smooth muscle. It binds to actin, myosin, Ca2+-binding proteins and tropomyosin and inhibits the actomyosin ATPase as well as the movement of actin filaments over myosin in vitro. These properties have led to the proposal that calponin may be involved in the Ca2+-dependent regulation of actin-myosin interaction and consequently of smooth muscle contraction. Calponin is localized in both the contractile;md the cytoskeletal parts of the smooth muscle cell and may have a structural function in smooth muscle cells. It may also regulate the pool of free actin available for cytoskeleton organization. In vitro calponin function is modulated by its interaction with a Ca2+-binding protein and/or by its phosphorylation. This suggests that calponin may play an important role in signal transduction from the membrane receptor to the contractile proteins in smooth muscle. Copyright (C) 1996 Elsevier Science Ltd

引用

页码：1185 / 1189

页数：5

共 11 条

[1]

APPLEGATE D, 1994, J BIOL CHEM, V269, P10683

[2] Expressing functional domains of mouse calponin: Involvement of the region around alanine 145 in the actomyosin ATPase inhibitory activity of calponin [J].