Molluscan smooth catch muscle contains calponin but not caldesmon

被引:10
|
作者
Dobrzhanskaya, Anna V. [1 ]
Vyatchin, Ilya G. [1 ]
Lazarev, Stanislav S. [1 ]
Matusovsky, Oleg S. [1 ]
Shelud'ko, Nikolay S. [1 ,2 ]
机构
[1] Russian Acad Sci, Lab Cell Biophys, AV Zhirmunsky Inst Marine Biol, Far E Branch, Vladivostok 690022, Russia
[2] Inst Marine Biol, Vladivostok 690059, Russia
基金
俄罗斯基础研究基金会;
关键词
Molluscan smooth catch muscle; Thin filaments; Ca2+-regulation; Calponin; Caldesmon; Myosin MgATPase activity; REGULATED THIN-FILAMENTS; ACTIN-BINDING PROTEIN; TROPONIN-C; MYOSIN; HYPOTHESIS; ACTOMYOSIN; SCALLOP; LOCALIZATION; PURIFICATION; CONTRACTION;
D O I
10.1007/s10974-012-9329-2
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
We isolated Ca2+-regulated thin filaments from the smooth muscle of the mussel Crenomytilus grayanus and studied the protein composition of different preparations from this muscle: whole muscle, heat-stable extract, fractions from heat-stable extract, thin filaments and intermediate stages of thin filaments purification. Among the protein components of the above-listed preparations, we did not find caldesmon (CaD), although two isoforms of a calponin-like (CaP-like) protein, which along with CaD is characteristic of vertebrate smooth muscle, were present in thin filaments. Thus, CaD is not Ca2+-regulator of thin filaments of this muscle. On the other hand, the mussel CaP-like protein is also not such Ca2+-regulator since we have shown that this protein can be selectively removed from isolated mussel thin filaments without loss of their Ca2+-sensitivity. We suggest that thin filaments in the smooth catch muscle possess other type of Ca2+-regulation, different from that in vertebrate smooth muscles.
引用
收藏
页码:23 / 33
页数:11
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