Phosphorylation of brain muscarinic receptor: Evidence of receptor regulation

Muscarinic receptor, from porcine synaptic membrane, was purified by affinity chromatography. Molecular weight analysis by SDS-gel electrophoresis revealed one major peptide with an apparent Mr of 68 ± 2 Kda. The purified receptor was phosphorylated by the catalytic subunit of cAMP-dependent protein...

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Veröffentlicht in:	Biochemical and biophysical research communications 1987-02, Vol.142 (3), p.911-918
Hauptverfasser:	Ho, Andrew K.S., Ling, Qi-Lang, Duffield, Rose, Lam, Peter H., Wang, Lerry H.
Format:	Artikel
Sprache:	eng
Schlagworte:	acetylcholine Adenosine Triphosphate - metabolism Animals Applied sciences brain Brain Chemistry Calcium - pharmacology Calmodulin - pharmacology Calmodulin-Binding Proteins - pharmacology Cyclic AMP - pharmacology Electrophoresis, Polyacrylamide Gel Exact sciences and technology Molecular Weight Other techniques and industries Phosphorylation Propylbenzilylcholine Mustard - metabolism Protein Kinases - metabolism Quinuclidinyl Benzilate - metabolism Receptors, Muscarinic - metabolism Swine synaptic membranes Synaptic Membranes - analysis
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Zusammenfassung:	Muscarinic receptor, from porcine synaptic membrane, was purified by affinity chromatography. Molecular weight analysis by SDS-gel electrophoresis revealed one major peptide with an apparent Mr of 68 ± 2 Kda. The purified receptor was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase resulting in a concomitant loss in specific binding, and this loss was reversed by calcineurin.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(87)91500-2