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pubmed-article:1780036pubmed:abstractTextHuman endozepine, an 86 amino acid polypeptide, was originally isolated from human brain tissue as a putative ligand of the benzodiazepine receptor. Complete amino acid sequencing of the human and bovine proteins revealed significant homology with the partial sequence of diazepam binding inhibitor (DBI), a protein from rat brain. Both endozepine and DBI have been shown to elicit behavioral effects, suggesting that they function as pharmacologically-active ligands of the GABA (gamma-aminobutyric acid) receptor complex. Subsequent cDNA cloning of human and bovine endozepine, rat DBI and human DBI has shown that these proteins are encoded by the same gene. A related cDNA, encoding a transmembrane protein of 533 amino acids with a domain homologous to DBI, has also been cloned from bovine brain.lld:pubmed
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pubmed-article:1780036pubmed:articleTitleHuman DBI (endozepine): relationship to a homologous membrane associated protein (MA-DBI).lld:pubmed
pubmed-article:1780036pubmed:affiliationFred Hutchinson Cancer Research Center, Seattle, WA 98104.lld:pubmed
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