Molecular cloning of human neuronal nicotinic receptor alpha 3-subunit.
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.
Fornasari
D
D
Department of Medical Pharmacology, University of Milan, Italy.
Chini
B
B
Tarroni
P
P
Clementi
F
F
D000595:Amino Acid Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D015342:DNA Probes; D006801:Humans; D008969:Molecular Sequence Data; D009447:Neuroblastoma / Q000235:genetics*; D009474:Neurons / Q000378:metabolism; D012333:RNA, Messenger / Q000032:analysis; D011978:Receptors, Nicotinic / Q000235:genetics*; D015183:Restriction Mapping; D014407:Tumor Cells, Cultured
D015342:DNA Probes; D012333:RNA, Messenger; D011978:Receptors, Nicotinic