FKBP12.6 binding of ryanodine receptors carrying mutations associated with arrhythmogenic cardiac disease.
In the present paper we show that distinct human RyR2 (ryanodine receptor type 2) inherited mutations expressed in mammalian cells exhibit either unaltered or increased FKBP12.6 (12.6 kDa FK506-binding protein) binding compared with the wild-type. Oxidizing conditions result in decreased FKBP12.6 binding, but to the same extent as for the wild-type. Our findings suggest that FKBP12.6 regulation of RyR2 is unlikely to be the primary defect in inherited arrhythmogenic cardiac disease.
Zissimopoulos
Spyros
S
Wales Heart Research Institute, Department of Medicine-Cardiology, Cardiff University School of Medicine, Cardiff CF14 4XN, Wales, UK. zissimopouloss@cf.ac.uk
Thomas
N Lowri
NL
Jamaluddin
Wan W
WW
Lai
F Anthony
FA
D001145:Arrhythmias, Cardiac / Q000235:genetics* / Q000378:metabolism; D002460:Cell Line; D003958:Diamide / Q000494:pharmacology; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D047468:Immunoprecipitation; D009154:Mutation; D011485:Protein Binding / Q000187:drug effects; D019837:Ryanodine Receptor Calcium Release Channel / Q000235:genetics* / Q000378:metabolism*; D022021:Tacrolimus Binding Proteins / Q000378:metabolism*
D019837:Ryanodine Receptor Calcium Release Channel; D003958:Diamide; D006861:Hydrogen Peroxide; D022021:Tacrolimus Binding Proteins; C403484:tacrolimus binding protein 1B