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Human galanin (hGal) is an important neuro-modulator present in the brain, gastrointestinal system and the hypothalamo-pituitary axis. A specific receptor for hGal has been identified in various areas in human brain. A single class of high affinity binding sites was found on plasma membranes of the amygdala (K_d 0·23 nM, B_max 44 fmol/mg), the hypothalamus (K_d 0·20 nM, B_max 25 fmol/mg) and the cortex cerebri (K_d0·11 nM, B_max 8·2 fmol/mg). Other brain areas, i.e. cerebellum, thalamus or pons, expressed binding sites of identical high affinity in lower quantities (B_max <3 fmol/mg). Specific binding of ¹²⁵I-labelled hGal was found to be reversible, time- and temperature-dependent and inhibited by Ca²⁺, Na⁺ and K⁺ ions at a concentration of 5 mM. Non-hydrolysable guanosine nucleotides potently reduced specific binding of ¹²⁵I-labelled hGal by more than 80%. Synthetic hGal analogues substituted in the N-terminal region exhibited strongly reduced binding affinity for the hGal receptor. Using 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-1-propanesulphonate, hGal receptors were successfully solubilized from human cortical membranes, exhibiting no significant loss of binding affinity. Affinity cross-linking to ¹²⁵I-labelled hGal revealed a labelled band of approximately 60 kDa sensitive to unlabelled Gal. This putative hGal receptor is glycosylated since its molecular size was reduced after treatment with endoglycosidase F. Receptors bound to ¹²⁵I-labelled hGal could be specifically adsorbed to wheat germ agglutinin and ricinus communis agglutinin, suggesting that receptor glycosylation involves N-acetyl glucosamine and galactose respectively.

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