The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein. Dissociation and reconstitution of FKBP-12 to the calcium release channel of skeletal muscle sarcoplasmic reticulum.
作者： A.P. Timerman , E Ogunbumni , E Freund , G Wiederrecht , A.R. Marks
DOI: 10.1016/S0021-9258(19)49416-7
关键词:
摘要: The ryanodine receptor/calcium release channel (CRC) of rabbit skeletal muscle terminal cisternae (TC) sarcoplasmic reticulum (SR) has been found to be tightly associated with FK-506 binding protein (FKBP-12), the cytosolic receptor (immunophilin) for immunosuppressant drug (Jayaraman, T., Brillantes, A. M., Timerman, P., Fleischer, S., Erdjument-Bromage, H., Tempst, and Marks, (1992) J. Biol. Chem. 267, 9474-9477). In this study, a procedure is described dissociate FKBP from TC reconstitute human recombinant FKBP-12 back so that role immunophilin on CRC activity can assessed. Titration vesicles dissociates receptor. Sedimentation FK-506-treated effectively separates soluble FKBP-FK506 complex which remains in supernatant. FKBP-deficient have altered functional characteristics: 1) ATP-stimulated calcium uptake rate reduced 2-fold; 2) threshold concentration caffeine required induce decreased. These changes appear reflect modification since: severalfold higher concentrations do not alter either longitudinal tubules SR, or presence ruthenium red; reassociates but control SR; 3) Ca2+ restored values FKBP-reconstituted TC. studies demonstrate modulates reticulum.
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