Calpain:新的家族成员、激活和生理功能。

K Suzuki, H Sorimachi, T Yoshizawa, K Kinbara, S Ishiura
{"title":"Calpain:新的家族成员、激活和生理功能。","authors":"K Suzuki,&nbsp;H Sorimachi,&nbsp;T Yoshizawa,&nbsp;K Kinbara,&nbsp;S Ishiura","doi":"10.1515/bchm3.1995.376.9.523","DOIUrl":null,"url":null,"abstract":"<p><p>The current status of calpain research is summarized on the basis of the most recent results. The main points are as follows. (i) Calpain constitutes a large family. (ii) Ca2+ ions cause the dissociation of calpain into subunits and the resulting free 80 kDa subunit is the active form of the enzyme. This dissociation corresponds to the activation of calpain. (iii) Some powerful clues have been obtained that will be helpful for analyzing the physiological function.</p>","PeriodicalId":8963,"journal":{"name":"Biological chemistry Hoppe-Seyler","volume":"376 9","pages":"523-9"},"PeriodicalIF":0.0000,"publicationDate":"1995-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm3.1995.376.9.523","citationCount":"214","resultStr":"{\"title\":\"Calpain: novel family members, activation, and physiologic function.\",\"authors\":\"K Suzuki,&nbsp;H Sorimachi,&nbsp;T Yoshizawa,&nbsp;K Kinbara,&nbsp;S Ishiura\",\"doi\":\"10.1515/bchm3.1995.376.9.523\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The current status of calpain research is summarized on the basis of the most recent results. The main points are as follows. (i) Calpain constitutes a large family. (ii) Ca2+ ions cause the dissociation of calpain into subunits and the resulting free 80 kDa subunit is the active form of the enzyme. This dissociation corresponds to the activation of calpain. (iii) Some powerful clues have been obtained that will be helpful for analyzing the physiological function.</p>\",\"PeriodicalId\":8963,\"journal\":{\"name\":\"Biological chemistry Hoppe-Seyler\",\"volume\":\"376 9\",\"pages\":\"523-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1995-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/bchm3.1995.376.9.523\",\"citationCount\":\"214\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biological chemistry Hoppe-Seyler\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/bchm3.1995.376.9.523\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biological chemistry Hoppe-Seyler","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/bchm3.1995.376.9.523","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 214

摘要

本文在总结最新研究成果的基础上,对钙蛋白酶的研究现状进行综述。主要观点如下。(i) Calpain是一个大家庭。(ii) Ca2+离子导致钙蛋白酶解离成亚基,产生的游离80 kDa亚基是酶的活性形式。这种解离对应于钙蛋白酶的激活。(三)获得了有助于分析生理功能的有力线索。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Calpain: novel family members, activation, and physiologic function.

The current status of calpain research is summarized on the basis of the most recent results. The main points are as follows. (i) Calpain constitutes a large family. (ii) Ca2+ ions cause the dissociation of calpain into subunits and the resulting free 80 kDa subunit is the active form of the enzyme. This dissociation corresponds to the activation of calpain. (iii) Some powerful clues have been obtained that will be helpful for analyzing the physiological function.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Sialic acids structure-analysis-metabolism-occurrence-recognition. Glycyl-tRNA synthetase. Rapid purification and characterization of two distinct N-deoxyribosyltransferases of Lactobacillus leichmannii. Purification of the CIC-0 chloride channel from Torpedo california electroplax identification of a phosphorylation site for cAMP-dependent protein kinase. Selective inhibition of cyclic AMP-dependent protein kinase by isoquinoline derivatives.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1