Neuronal nicotinic receptors (nAchRs) have been isolated or cloned in insect, bird and mammalian neurons, but no information exists on the primary structure of human neuronal nAchRs. By screening a cDNA library from the human neuroblastoma cell line IMR 32 with a cDNA probe corresponding to the full length of rat alpha 3-nicotinic subunit, we have identified an open reading frame encoding a protein of 502 amino acids. This protein shows all the features of members of the ligand-gated receptor superfamily and has two cysteine residues at positions 192, 193 which are typical of the nicotinic alpha-subunits. Because of its high homology to rat alpha 3 (93% amino acid identity), we conclude that we have cloned the human alpha 3-nicotinic subunit.
Molecular cloning of human neuronal nicotinic receptor alpha 3-subunit / D. Fornasari, B. Chini, P. Tarroni, F. Clementi. - In: NEUROSCIENCE LETTERS. - ISSN 0304-3940. - 111:3(1990 Apr 06), pp. 351-356.
Molecular cloning of human neuronal nicotinic receptor alpha 3-subunit
D. FornasariPrimo
;F. ClementiUltimo
1990
Abstract
Neuronal nicotinic receptors (nAchRs) have been isolated or cloned in insect, bird and mammalian neurons, but no information exists on the primary structure of human neuronal nAchRs. By screening a cDNA library from the human neuroblastoma cell line IMR 32 with a cDNA probe corresponding to the full length of rat alpha 3-nicotinic subunit, we have identified an open reading frame encoding a protein of 502 amino acids. This protein shows all the features of members of the ligand-gated receptor superfamily and has two cysteine residues at positions 192, 193 which are typical of the nicotinic alpha-subunits. Because of its high homology to rat alpha 3 (93% amino acid identity), we conclude that we have cloned the human alpha 3-nicotinic subunit.Pubblicazioni consigliate
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