Biochemical Characterization and Molecular Cloning of Cardiac Triadin

• DOI: 10.1074/jbc.271.1.458
• Publication Date: 2002-07-26T15:15:23Z
• Authors: Wei Guo; Annelise O. Jorge...; Larry R. Jones; Kevin P. Campbell
• Keywords: Cloning (programming); Characterization

Triadin is an intrinsic membrane protein first identified in the skeletal muscle junctional sarcoplasmic reticulum and considered to play important role excitation-contraction coupling. Using polyclonal antibodies triadin, we have characterized three isoforms rabbit cardiac muscle. The cDNAs encoding these of triadin been isolated by reverse transcription-polymerase chain reaction cDNA library screening. deduced amino acid sequences show that proteins are identical their N-terminal sequences, whereas C-terminal distinct from each other triadin. Based upon both biochemical analysis, all share similar topology with Immunofluorescence staining purified homologous region shows primarily confined I-band myocytes, where corbular located. Furthermore, demonstrate conserved luminal domain able bind ryanodine receptor calsequestrin These results suggest colocalizes binds carries out a function lumen for