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Hydrogen sulfide regulates muscle RING finger‐1 protein S‐sulfhydration at Cys 44 to prevent cardiac structural damage in diabetic cardiomyopathy
Author(s) -
Sun Xiaojiao,
Zhao Dechao,
Lu Fangping,
Peng Shuo,
Yu Miao,
Liu Ning,
Sun Yu,
Du Haining,
Wang Bingzhu,
Chen Jian,
Dong Shiyun,
Lu Fanghao,
Zhang Weihua
Publication year - 2020
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.14601
Subject(s) - endoplasmic reticulum , myosin , ubiquitin ligase , cystathionine beta synthase , ubiquitin , chemistry , diabetic cardiomyopathy , endocrinology , cardiac muscle , medicine , biochemistry , cardiomyopathy , cysteine , enzyme , heart failure , gene
Hydrogen sulfide (H 2 S) plays important roles as a gasotransmitter in pathologies. Increased expression of the E3 ubiquitin ligase, muscle RING finger-1 (MuRF1), may be involved in diabetic cardiomyopathy. Here we have investigated whether and how exogenous H 2 S alleviates cardiac muscle degradation through modifications of MuRF1 S-sulfhydration in db/db mice.