Myelin Basic Protein Is an Endogenous Inhibitor of the High‐Affinity Cannabinoid Binding Site in Brain
作者： Jeffrey S. Nye , Susan Voglmaier , Russell E. Martenson , Solomon H. Snyder
DOI: 10.1111/J.1471-4159.1988.TB10589.X
关键词:
摘要: Radioligand binding studies with the water-soluble cannabinoid [3H]5'-trimethylammonium delta 8-tetrahydrocannabinol ([3H]TMA) have revealed a saturable high-affinity site in brain that is specific for cannabinoids. To determine whether endogenous compounds of might act upon physiologically, we sought inhibitors extracts brain. An inhibitor has been purified to homogeneity by acid extraction rat followed adsorption reverse-phase matrix and gel filtration chromatography. The subunit molecular mass 14,500 daltons sodium dodecyl sulfate-polyacrylamide electrophoresis (SDS-PAGE). Inhibition [3H]TMA occurs Ki about 4 nM noncompetitive manner. weight, abundance, properties are same as species myelin basic protein (MBP). MBPs rat, rabbit, pig, cow also inhibit noncompetitively similar potencies. comigrates MBP-small form on SDS-PAGE, amino composition, recognized antibody directed against MBP. Studies fragments rabbit MBP suggest determinants affinity contained primarily within C-terminal half Synthetic polycationic peptides such polylysine polyarginine mimic effects MBP, suggesting recognizes large polycations. identification suggests interacts physiologically site.
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