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Cloning and expression of a novel rat GABA A receptor
Author(s) -
Lolait Stephen J.,
O'Carroll Anne-Marie,
Kusano Kiyoshi,
Muller Jean-Marc,
Brownstein Michael J.,
Mahan Lawrence C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80271-6
Subject(s) - protein subunit , complementary dna , gamma aminobutyric acid receptor subunit alpha 1 , interleukin 10 receptor, alpha subunit , amino acid , microbiology and biotechnology , biology , receptor , interleukin 5 receptor alpha subunit , xenopus , messenger rna , biochemistry , interleukin 12 receptor, beta 1 subunit , cloning (programming) , cdna library , g alpha subunit , gene , computer science , programming language
Two full‐length cDNA clones encoding α‐ and β‐subunits of a GABA A receptor have been isolated from a rat cerebral cortex cDNA library. The mature α‐subunit protein consists of 428 amino acids with a calculated M r of 48680. This protein is highly homologous (∼99% amino acid identity) with the bovine brain α 1 ‐subunit receptor [(1988) Nature 335, 76–79]. The mature rat β‐subunit receptor is a 448 amino acid polypeptide and shares ∼ 80% amino acid identity with the previously characterized bovine GABA A receptor β‐subunit [(1987) Nature 328, 221–227]. Co‐expression of the cloned DNA in Xenopus oocytes produces a functional receptor and ion channel with pharmacological characteristics of a GABA A receptor. GABA A α‐ and β‐subunit mRNA is detectable in the cortex, cerebellum and hippocampus.