Structural diversity of triadin in skeletal muscle and evidence of its existence in heart.
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.
Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, OH 45267-0575.
M
M
Peng
H
H
Fan
T L
TL
Kirley
A H
AH
Caswell
A
A
Schwartz
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D002352:Carrier Proteins; D017931:DNA Primers; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000032:analysis / Q000737:chemistry*; D009206:Myocardium / Q000737:chemistry*; D011487:Protein Conformation; D011817:Rabbits
D002352:Carrier Proteins; D017931:DNA Primers; D009124:Muscle Proteins; C070048:triadin