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J. Biol. Chem., Vol. 269, Issue 11, 7963-7969, 03, 1994
RJ Wojcikiewicz, T Furuichi, S Nakade, K Mikoshiba and SR Nahorski
Stimulation of SH-SY5Y human neuroblastoma cells with carbachol, a
muscarinic agonist, down-regulates the type I inositol 1,4,5- trisphosphate
(InsP3) receptor by > 90% with maximal and half-maximal effects after
approximately 6 h and approximately 1 h, respectively. Examination of the
mechanistic basis of this down-regulation revealed that carbachol increased
the rate of type I InsP3 receptor degradation (radiolabeled
immunoprecipitable receptor was lost from cells with half- times of > 8
h and approximately 1 h in the absence and presence of carbachol,
respectively) and that the concentration of type I InsP3 receptor mRNA,
despite a transient decrease after 3 h, did not correlate with levels of
the receptor. Only those muscarinic receptor subtypes coupled to
stimulation of phosphoinositide hydrolysis were capable of causing type I
InsP3 receptor down-regulation. Ca2+ mobilization was pivotal to the
mechanisms of receptor down-regulation, since perturbation of Ca2+
homeostasis with either EGTA or thapsigargin blocked the ability of
carbachol to accelerate receptor degradation. Studies with thapsigargin
also revealed that both functional InsP3- sensitive Ca2+ stores and
persistent elevation of InsP3 concentration were required for
down-regulation to occur. In conclusion, phosphoinositidase C-linked
muscarinic receptors down-regulate the type I InsP3 receptor by
accelerating its degradation. It appears that this process is initiated by
persistent discharge of intracellular Ca2+ stores via the channels formed
by tetramerically complexed type I InsP3 receptors.
Muscarinic receptor activation down-regulates the type I inositol 1,4,5- trisphosphate receptor by accelerating its degradation
Department of Cell Physiology and Pharmacology, University of Leicester.
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