Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle
作者： Lan Wei , Amy D. Hanna , Nicole A. Beard , Angela F. Dulhunty
DOI: 10.1016/J.CECA.2009.03.006
关键词: Biophysics 、 Calcium signaling 、 Skeletal muscle 、 RYR1 、 Chemistry 、 Ryanodine receptor 、 Myocyte 、 Calsequestrin 、 Biochemistry 、 Ryanodine receptor 2 、 Calcium buffering
摘要: Abstract Calcium signaling in myocytes is dependent on the cardiac ryanodine receptor (RyR2) calcium release channel and buffering protein sarcoplasmic reticulum, calsequestrin (CSQ2). The overall properties of CSQ2 its regulation RyR2 have not been explored detail or directly compared with skeletal CSQ1 RyR1, physiological ionic strength Ca2+ concentrations. We find that there are major differences between two isoforms under these conditions. binding to 50% lower than CSQ1. Only ∼30% bound junctional face membrane (JFM), ∼70% ratio only CSQ1/RyR1 ratio. Chemical crosslinking shows mostly monomer/dimer, while polymerized. In single lipid bilayer experiments, monomers and/or dimers increase open probability both RyR1 channels, polymers decrease activity RyR1. speculate facilitates high rates through during systole, curtails opening response a action potential maintain allow repeated graded activation increased stimulation frequency.
elsevier.com
sci-hub.se 参考文章(50)
Albert R. Behnke, Physiologic Studies Pertaining to Deep Sea Diving and Aviation, Especially in Relation to the Fat Content and Composition of the Body: The Harvey Lecture, March 19, 1942. Bulletin of the New York Academy of Medicine. ,vol. 18, pp. 561- 585 ,(1942)
B Cozens, R A Reithmeier, Size and shape of rabbit skeletal muscle calsequestrin. Journal of Biological Chemistry. ,vol. 259, pp. 6248- 6252 ,(1984) , 10.1016/S0021-9258(20)82133-4
Larry Fliegel, M. Michalak, K. Burns, E. Newton, Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum. Journal of Biological Chemistry. ,vol. 265, pp. 15496- 15502 ,(1990) , 10.1016/S0021-9258(18)55423-5
B T Scott, H K Simmerman, J H Collins, B Nadal-Ginard, L R Jones, Complete amino acid sequence of canine cardiac calsequestrin deduced by cDNA cloning. Journal of Biological Chemistry. ,vol. 263, pp. 8958- 8964 ,(1988) , 10.1016/S0021-9258(18)68401-7
Brenda R. Eisenberg, Aileen M. Kuda, Stereological analysis of mammalian skeletal muscle. II. White vastus muscle of the adult guinea pig. Journal of Ultrastructure Research. ,vol. 51, pp. 176- 187 ,(1975) , 10.1016/S0022-5320(75)80146-8
Dmitry Terentyev, Serge Viatchenko-Karpinski, Srikanth Vedamoorthyrao, Sridhar Oduru, Inna Györke, Simon C. Williams, Sandor Györke, Protein–protein interactions between triadin and calsequestrin are involved in modulation of sarcoplasmic reticulum calcium release in cardiac myocytes The Journal of Physiology. ,vol. 583, pp. 71- 80 ,(2007) , 10.1113/JPHYSIOL.2007.136879
H Towbin, J Gordon, T Staehelin, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. 1979. Biotechnology (Reading, Mass.). ,vol. 24, pp. 145- 149 ,(1992)
Gerard P. Ahern, Pauline R. Junankar, Angela F. Dulhunty, Single channel activity of the ryanodine receptor calcium release channel is modulated by FK-506 FEBS Letters. ,vol. 352, pp. 369- 374 ,(1994) , 10.1016/0014-5793(94)01001-3
Csaba SZEGEDI, Sándor SÁRKÖZI, Anke HERZOG, István JÓNA, Magdolna VARSÁNYI, Calsequestrin: More than 'only' a luminal Ca2+ buffer inside the sarcoplasmic reticulum Biochemical Journal. ,vol. 337, pp. 19- 22 ,(1999) , 10.1042/BJ3370019
Shuren Wang, William R. Trumble, Hong Liao, Carla R. Wesson, A. Keith Dunker, ChulHee Kang, Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nature Structural & Molecular Biology. ,vol. 5, pp. 476- 483 ,(1998) , 10.1038/NSB0698-476