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Structural diversity of triadin in skeletal muscle and evidence of its existence in heart
Author(s) -
Peng Mei,
Fan Hongran,
Kirley Terence L.,
Caswell Anthony H.,
Schwartz Arnold
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00556-7
Subject(s) - skeletal muscle , endoplasmic reticulum , gene isoform , sarcoplasm , biology , chemistry , biophysics , microbiology and biotechnology , anatomy , biochemistry , gene
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.