期刊
PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES
卷 87, 期 6, 页码 287-327出版社
JAPAN ACAD
DOI: 10.2183/pjab.87.287
关键词
calpain; muscular dystrophy; calpainopathy; gastropathy; intracellular proteolysis; calcium ion
资金
- MEXT.KAKENHI [18076007, 20780106, 22770139]
- JSPS.KAKENHI [20370055]
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [22770139, 18076007, 20780106, 20370055] Funding Source: KAKEN
Calpain is an intracellular Ca2+-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) discovered in 1964. It was also called CANP (Ca2+-activated neutral protease) as well as GASP, CDP, KAF., etc. until 1990. Calpains are found in almost all eukaryotes and a few bacteria, but not in archaebacteria. Calpains have a limited proteolytic activity, and function to transform or modulate their substrates' structures and activities; they are therefore called; modulator proteases. In the human genome, 15 genes-CAPN1, CAPN2, etc.-encode a calpain-like protease domain. Their products are calpain homologs with divergent structures and various combinations of functional domains, including Ca2+-binding and microtubule-interaction domains. Genetic studies have linked calpain deficiencies to a, variety of defects in many different organisms, including lethality; muscular dystrophies, gastropathy, and diabetes. This review of the study of calpains focuses especially on recent findings about their structure-function relationships. These discoveries have been greatly aided by the development of 3D structural studies and genetic models.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据