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J. Biol. Chem., Vol. 265, Issue 14, 8183-8189, May, 1990
DA Schwinn, JW Lomasney, W Lorenz, PJ Szklut, RT Fremeau Jr, TL Yang-Feng, MG Caron, RJ Lefkowitz and S Cotecchia
A novel alpha 1-adrenergic receptor subtype has been cloned from a bovine
brain cDNA library. The deduced amino acid sequence is that of a
466-residue polypeptide. The structure is similar to that of the other
adrenergic receptors as well as the larger family of G protein-coupled
receptors that have a presumed seven-membrane-spanning domain topography.
The greatest sequence identity of this receptor protein is with the
previously cloned hamster alpha 1B-adrenergic receptor being approximately
72% within the presumed membrane-spanning domains. Localization on
different human chromosomes provides evidence that the bovine cDNA is
distinct from the hamster alpha 1B-adrenergic receptor. The bovine cDNA
clone expressed in COS7 cells revealed 10-fold higher affinity for the
alpha 1-adrenergic antagonists WB4101 and phentolamine and the agonist
oxymetazoline as compared with the alpha 1B receptor, results similar to
pharmacologic binding properties described for the alpha 1A receptor.
Despite these similarities in pharmacological profiles, the bovine alpha
1-adrenergic receptor is sensitive to inhibition by the alkylating agent
chloroethylclonidine unlike the alpha 1A-adrenergic receptor subtype. In
addition, a lack of expression in tissues where the alpha 1A subtype exists
suggests that this receptor may actually represent a novel alpha
1-adrenergic receptor subtype not previously appreciated by pharmacological
criteria.
Molecular cloning and expression of the cDNA for a novel alpha 1- adrenergic receptor subtype
Department of Anesthesiology, Duke University Medical Center, Durham, North Carolina 27710.
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