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- W2116716993 abstract "Acetylcholine receptors at the neuromuscular junction of innervated vertebrate muscle (called Rs AChRs) have a stable degradation rate (t1/2 approximately 8-12 days) which accelerates after denervation to a half-life of approximately 3 days, but can be restabilized by reinnervation or by cAMP. We examined the mechanism by which cAMP regulates the Rs degradation rate. When dibutyryl cAMP (DB-cAMP) was applied to denervated mouse diaphragms in organ culture, it stabilized the accelerated degradation rate of the Rs. We found that this stabilization is reversible upon removal of the DB-cAMP, is cAMP specific and is mediated by intracellular cAMP. A major observation of this study is that the cAMP-induced stabilization of Rs AChRs is via protein kinase A (PKA), since H89, a PKA inhibitor, blocked the DB-cAMP induced stabilization of Rs, and H85, an analog of H89, which does not inhibit PKA but does inhibit other kinases as efficiently as H89, did not prevent the DB-cAMP-induced stabilization of Rs degradation. These results suggest that the cAMP messenger system via a PKA-dependent pathway could be among the mechanisms whereby the nerve regulates AChR degradation." @default.
- W2116716993 created "2016-06-24" @default.
- W2116716993 creator A5027557441 @default.
- W2116716993 creator A5085294521 @default.
- W2116716993 date "1995-10-01" @default.
- W2116716993 modified "2023-09-27" @default.
- W2116716993 title "Protein kinase A regulates the degradation rate of Rs acetylcholine receptors" @default.
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- W2116716993 doi "https://doi.org/10.1002/jcp.1041650105" @default.
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