FKBP12. 6 binding of ryanodine receptors carrying mutations associated with arrhythmogenic cardiac disease
S Zissimopoulos, NL Thomas… - Biochemical …, 2009 - portlandpress.com
S Zissimopoulos, NL Thomas, WW Jamaluddin, FA Lai
Biochemical Journal, 2009•portlandpress.comIn 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.
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.
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.
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