FEBS Letters | |
Complex formation between calsequestrin and the ryanodine receptor in fast‐ and slow‐twitch rabbit skeletal muscle | |
Ohlendieck, Kay1  Murray, Brendan E.1  | |
[1] Department of Pharmacology, University College Dublin, Belfield, Dublin 4, Ireland | |
关键词: Calsequestrin; Ryanodine receptor; Excitation-contraction coupling; Triad; Skeletal muscle; CSQ; calsequestrin; DHPR; dihydropyridine receptor; DSP; dithiobis-succinimidyl propionate; EC; excitation-contraction; mAb; monoclonal antibody; RyR; ryanodine receptor; SR; sarcoplasmic reticulum; | |
DOI : 10.1016/S0014-5793(98)00621-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Linkage between the high-capacity Ca2+-binding protein calsequestrin and the ryanodine receptor is proposed to be essential for proper Ca2+-release during skeletal muscle excitation-contraction coupling. However, no direct biochemical evidence exists showing a connection between these high-molecular-mass complexes in native skeletal muscle membranes. Here, using immunoblot analysis of chemically crosslinked membrane vesicles enriched in triad junctions, we have demonstrated that a very close neighborhood relationship exists between calsequestrin and the ryanodine receptor in both main fiber types. Hence, the luminal Ca2+-reservoir complex appears to be directly coupled to the membrane Ca2+-release complex and oligomerization seems to be of functional importance.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020306080ZK.pdf | 242KB | download |