Peer-Reviewed Journal Details
Mandatory Fields
Mackrill, JJ;O'Driscoll, S;Lai, FA;McCarthy, TV
2001
July
Biochemical and Biophysical Research Communications
Analysis of type 1 ryanodine receptor-12 kDa FK506-binding protein interaction
Validated
WOS: 10 ()
Optional Fields
CALCIUM-RELEASE CHANNEL FK506 BINDING-PROTEIN MUSCLE SARCOPLASMIC-RETICULUM SKELETAL-MUSCLE 1,4,5-TRISPHOSPHATE RECEPTOR CA2+ COMPLEX FKBP12 CALCINEURIN ASSOCIATION
285
52
57
Although dissociation of the 12 kDa FK506 binding protein (FKBP12)-type 1 ryanodine receptor (RyR1) complex by macrolide immunosuppressants is well documented, effects of many solutes and drugs have not been quantitated, In the current study, the influence of these on binding between solubilised RyR1 and an FKBP12-glutathione-S-transferase fusion protein was analysed using a novel assay. Association between these two proteins is stable, and is not greatly altered by changes in temperature, pH, cations, and endogenous solutes over physiological ranges. Ascomycin, an FK506 analogue, was identified for the first time as a drug which can disrupt the FKBP12-RyR1 complex. (C) 2001 Academic Press.
SAN DIEGO
0006-291X
10.1006/bbrc.2001.5125
Grant Details