Morphine enhances the phosphorylation of a 58 kDa protein in mouse brain membranes.

Abstract

Morphine and [D-Ala2,D-Leu5]enkephalinamide enhance the phosphorylation of a 58 kDa protein in mouse brain synaptosomal membranes. The enhancement of phosphorylation was inhibited by naloxone, an antagonist of morphine. The phosphorylated 58 kDa protein was retained on wheat-germ-agglutinin-agarose and morphinone-Affi-Gel 401 columns and biospecifically eluted out from the columns with N-acetyl-D-glucosamine and naloxone respectively. These results suggest a strong possibility that the opiate-binding protein undergoes phosphorylation by endogenous protein kinase. Since the molecular mass of a mu-type opioid receptor in mouse brain is suggested to be 58 kDa, coincident with those of rat brain and neuroblastoma x glioma hybrid cells, it is conceivable that the phosphorylated 58 kDa protein is a mu-type receptor.

Cite this paper

@article{Nagamatsu1989MorphineET, title={Morphine enhances the phosphorylation of a 58 kDa protein in mouse brain membranes.}, author={Keiji Nagamatsu and Kazuo Suzuki and Reiko Teshima and Hideharu Ikebuchi and Takeshi Terao}, journal={The Biochemical journal}, year={1989}, volume={257 1}, pages={165-71} }