Structural diversity of triadin in skeletal muscle and evidence of its existence in heart

FEBS Letters

Kirley, Terence L.¹  Fan, Hongran²  Schwartz, Arnold¹  Peng, Mei¹  Caswell, Anthony H.² 

[1] Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0575, USA;Department of Molecular and Cellular Pharmacology, University of Miami College of Medicine, Miami, FL 33101, USA

关键词: Calcium release channel;    Sarcoplasmic reticulum;    Calcium;    E-C coupling;    Triad;    E-C coupling;    excitation—contraction coupling;    DHP receptor;    dihydropyridine receptor;    SR;    sarcoplasmic reticulum;    RT;    reverse transcription;    PCR;    polymerase chain reaction;    PAGE;    polyacrylamide gel electrophoresis;    TBP;    tributyl phosphine;    ABD-F;    4-aminosulfonyl-7-fluoro-2;    1;    3-benzoxadiazole;    APRT;    adenosine phosphoribosyl transferase;   

DOI  :  10.1016/0014-5793(94)00556-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Triadin has been characterized as an abundant protein co-localized with the calcium release channel on the terminal cisternae of the sarcoplasmic reticulum of the skeletal muscle. Its localization to terminal cisternae of the sarcoplasmic reticulum and functional studies suggest that it has an important role in excitation-contraction coupling. In this study we identify three triadin isoforms in rabbit skeletal muscle and by Northern blot analysis demonstrate that triadin also exists in the heart.

【 授权许可】

Unknown