Mathematical modeling of opiate binding to mouse brain membrane

1985 ◽  
Vol 47 (4) ◽  
pp. 503-512 ◽  
Author(s):  
Herbert D. Landahl ◽  
Javier Garzón ◽  
Nancy M. Lee
Keyword(s):  
Mathematical Modeling ◽  
Mouse Brain ◽  
Brain Membrane ◽  
Opiate Binding

Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase

2003 ◽  
Vol 18 (7) ◽  
pp. 1837-1847 ◽  
Author(s):  
Noel A. Perrier ◽  
Sonia Kherif ◽  
Anselme L. Perrier ◽  
Sylvie Dumas ◽  
Jacques Mallet ◽  
...  
Keyword(s):  
Mouse Brain ◽  
Brain Membrane ◽  
Membrane Anchoring

Cyproterone acetate displaces opiate binding in mouse brain

1997 ◽  
Vol 328 (1) ◽  
pp. 99-102 ◽  
Author(s):  
Mercedes Gutiérrez ◽  
Luis Menéndez ◽  
Mariano Ruiz-Gayo ◽  
Agustı́n Hidalgo ◽  
Ana Baamonde
Keyword(s):  
Mouse Brain ◽  
Cyproterone Acetate ◽  
Opiate Binding

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

1989 ◽  
Vol 257 (1) ◽  
pp. 165-171 ◽  
Author(s):  
K Nagamatsu ◽  
K Suzuki ◽  
R Teshima ◽  
H Ikebuchi ◽  
T Terao
Keyword(s):  
Protein Kinase ◽  
Molecular Mass ◽  
Mouse Brain ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Synaptosomal Membranes ◽  
Hybrid Cells ◽  
Endogenous Protein ◽  
Opiate Binding ◽  
Type Receptor

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.

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