Open AccessSmall Heat Shock Protein 20 Interacts With Protein Phosphatase-1 and Enhances Sarcoplasmic Reticulum Calcium Cycling
Author(s) -
Qian Jiang,
Elizabeth Vafiadaki,
Stela Florea,
Vivek Singh,
Weizhong Song,
Chi Keung Lam,
Yigang Wang,
Qunying Yuan,
Tracy J. Pritchard,
Wenfeng Cai,
Kobra Haghighi,
Patricia Rodríguez,
Hongsheng Wang,
Despina Sanoudou,
GuoChang Fan,
Evangelia G. Kranias
Publication year - 2011
Publication title -
circulation research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.899
H-Index - 336
eISSN - 1524-4571
pISSN - 0009-7330
DOI - 10.1161/circresaha.110.237644
Subject(s) - endoplasmic reticulum , calcium , heat shock protein , sarcoplasm , shock (circulatory) , microbiology and biotechnology , chemistry , phosphatase , biophysics , biochemistry , biology , medicine , enzyme , gene , organic chemistry
Heat shock proteins (Hsp) are known to enhance cell survival under various stress conditions. In the heart, the small Hsp20 has emerged as a key mediator of protection against apoptosis, remodeling, and ischemia/reperfusion injury. Moreover, Hsp20 has been implicated in modulation of cardiac contractility ex vivo. The objective of this study was to determine the in vivo role of Hsp20 in the heart and the mechanisms underlying its regulatory effects in calcium (Ca) cycling.
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