Involvement of tyrosyl residues in the binding of benzodiazepines to their brain receptors

Sherman-Gold, Rivka; Dudai, Yadin

doi:10.1016/0014-5793(81)80393-6

Cited by 17 publications

(4 citation statements)

References 8 publications

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“…Our data on TNM treatment disagree with a previous report on BZ receptors from bovine cortex (Sherman-Gold and Dudai, 1981). It reported the complete inhibition of [3H]diazepam binding by similar concentrations of TNM and its partial protection by BZs and GABA in a solubilized preparation.…”

Section: Bz Binding Sitescontrasting

confidence: 99%

“…does not require charged residues such as this. Some reports have indicated that the BZ receptors are not sensitive to treatment with sulfhydrylmodifying reagents (Sherman-Gold and Dudai, 1981;Ito et al, 1982). Further, disulfide-reducing reagents did not alter the number of BZ binding sites, but only reduced their affinity (Marangos and Martino, 1981).…”

Section: Bz Binding Sitesmentioning

confidence: 99%

“…N-Acetylimidazole can acylate not only the hydroxyl group of tyrosine, but thiol (Riordan et al, 1965) and amino (Means and Feeney, 1971) groups, too. Previous studies have excluded the possible presence of thiol groups at the BZ site (Marangos and Martino, 1981;Sherman-Gold and Dudai, 1981;Ito et al, 1982). Consequently, the selective protection by flurazepam against N-acetylimidazole inhibition ( Fig.…”

Section: Bz Binding Sitesmentioning

confidence: 99%

“…The inhibitory effect of pyridoxal-5-phosphate (PLP) on 13H]GABA binding and its partial prevention by GABA suggested that GABA receptors contain a lysine residue (Tunicliff, 1979). The inhibitory effect of tetranitromethane (TNM) and N-acetylimidazole on [3H]diazepam binding in both solubilized and membrane-bound BZ receptors of bovine brain suggested the presence of tyrosine residues at this site because it could be partially prevented by pharmacologically active BZs (Sherman-Gold and Dudai, 1981).…”

mentioning

confidence: 99%

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Characterization of γ‐Aminobutyric Acid‐Benzodiazepine Receptor Complexes by Protection Against Inactivation by Group‐Specific Reagents

Maksay

Ticku

1984

Journal of Neurochemistry

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The chemical topography of the gamma-aminobutyric acid (GABA) and benzodiazepine (BZ) receptors was investigated in a thoroughly washed cortical membrane preparation of the rat. Chemical modification by several amino- and tyrosyl-selective reagents and the protection from it by direct and allosteric ligands of the GABA-BZ receptor complex were used to identify the residues at the binding sites. Inhibition of specific GABA binding by p-diazobenzenesulfonic acid (DSA), tetranitromethane (TNM), and N-acetylimidazole and the selective and complete protection from it by GABA and muscimol suggest the presence of a tyrosine residue at the GABAA site. TNM, like DSA, selectively decreased the number of the low-affinity GABA receptors, and this could be completely protected only by GABA concentrations that can saturate the low-affinity sites. TNM pretreatment also abolished the muscimol enhancement of [3H]diazepam binding, which suggests that the low-affinity GABA receptor sites are responsible for this enhancement. Inhibition of GABA binding by pyridoxal-5-phosphate (PLP) and the selective protection by GABA and muscimol support the presence of a lysine residue at the GABAA receptor site. Complete and selective protection from diethylpyrocarbonate (DEP) inhibition of [3H]diazepam binding by flurazepam suggests the presence of a histidine residue at the BZ site. Flurazepam selectively protected from inhibition of [3H]diazepam binding by N-bromosuccinimide and N-acetylimidazole, but not that by DSA and TNM, which does not allow a unanimous conclusion regarding the presence of tyrosine or tryptophan residues at the BZ site.

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Section: Bz Binding Sitescontrasting

confidence: 99%

Section: Bz Binding Sitesmentioning

confidence: 99%

Section: Bz Binding Sitesmentioning

confidence: 99%

mentioning

confidence: 99%

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Characterization of γ‐Aminobutyric Acid‐Benzodiazepine Receptor Complexes by Protection Against Inactivation by Group‐Specific Reagents

Maksay

Ticku

1984

Journal of Neurochemistry

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Glycoprotein properties of benzodiazepine receptors from calf cerebral cortex

Sherman-Gold

Dudai

1983

J of Neuroscience Research

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Several lectins (concanavalin A, wheat germ agglutinin, wax bean agglutinin, and phytohemagglutinin) induce aggregation and precipitation of deoxycholate-solubilized benzodiazepine receptors from calf cerebral cortex. These receptors were also retained on columns of immobilized lectins. Photoaffinity labeling of the soluble benzodiazephine receptors prevented their interaction with lectins. Periodate treatment caused inactivation of benzodiazepine receptors which was partially prevented by diazepam and/or gamma-aminobutyric acid. The possible association of the drug-binding site and the carbohydrate moiety is discussed.

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Recent advances in benzodiazepine receptor (BZR) binding studies

Gupta¹

1995

Progress in Drug Research / Fortschritte Der Arzneimittelforschung / Progrès Des Recherches Pharmaceutiques

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Involvement of tyrosyl residues in the binding of benzodiazepines to their brain receptors

Cited by 17 publications

References 8 publications

Characterization of γ‐Aminobutyric Acid‐Benzodiazepine Receptor Complexes by Protection Against Inactivation by Group‐Specific Reagents

Characterization of γ‐Aminobutyric Acid‐Benzodiazepine Receptor Complexes by Protection Against Inactivation by Group‐Specific Reagents

Glycoprotein properties of benzodiazepine receptors from calf cerebral cortex

Recent advances in benzodiazepine receptor (BZR) binding studies

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