Alternative titles; symbols
HGNC Approved Gene Symbol: ADRA1A
Cytogenetic location: 8p21.2 Genomic coordinates (GRCh38): 8:26,748,150-26,867,379 (from NCBI)
Alpha-1-adrenergic receptors are G protein-coupled transmembrane receptors that mediate actions in the sympathetic nervous system through the binding of the catecholamines, epinephrine and norepinephrine (summary by Chang et al., 1998).
Schwinn et al. (1990) cloned Adra1a from a bovine brain cDNA library.
Hirasawa et al. (1993) cloned ADRA1A, which was initially termed ADRA1C, from a prostate cDNA library. The predicted 466-amino acid ADRA1A protein, which is 92% homologous to the bovine protein, contains 3 N-linked glycosylation sites in its N terminus, 7 transmembrane domains, and phosphorylation sites in its C terminus. RT-PCR analysis detected ADRA1A transcripts in heart, brain, liver, and prostate; no expression was detected in kidney, lung, adrenal, aorta, and pituitary.
Weinberg et al. (1994) also cloned ADRA1A. They determined that the N-terminal region of ADRA1A (18 amino acids) is much shorter than that of ADRA1D (104219; 88 amino acids) or ADRA1B (104220; 38 amino acids). RNase protection analysis showed that ADRA1A is the predominant ADRA1 subtype in liver and heart.
Forray et al. (1994) cloned ADRA1A and determined that it mediates the contraction of prostate smooth muscle.
Schwinn et al. (1995) also cloned ADRA1A from a prostate cDNA library.
Tseng-Crank et al. (1995) cloned ADRA1A and demonstrated expression in prostate stromal and glandular cells and in prostate cancer tissue by PCR, Northern blot, and in situ hybridization analyses. ADRA1A transcript sizes of 6.0, 4.0, 3.0, and 2.0 kb were detected in liver. The 6.0-, 4.0-, and 3.0-kb transcripts were present in heart, and the 6.0- and 4.0-kb transcripts were present in prostate.
Hirasawa et al. (1995) obtained 2 ADRA1A splice variants encoding proteins of 499 and 429 amino acids with differing C-terminal sequences. RT-PCR analysis indicated coexpression with the previously identified 466-amino acid isoform in heart, liver, cerebellum, and cerebrum. Functional analysis showed that the 3 isoforms have similar ligand-binding properties. Chang et al. (1998) identified a fourth ADRA1A isoform encoding a protein of 455 amino acids. Quantitative PCR analysis suggested that this isoform may be more highly expressed in prostate than the other ADRA1A isoforms.
By somatic cell hybrid analysis, Schwinn et al. (1990) mapped the human ADRA1A gene to chromosome 8.
Hoehe et al. (1992) demonstrated a 2-allele PstI RFLP in the ADRA1A gene. Using this probe for the study of DNAs from the CEPH pedigrees, they concluded that the gene is closely linked (theta of 0.03) to NEFL (162280) on 8p21 (maximum lod of 12).
Chang, D. J., Chang, T. K., Yamanishi, S. S., Salazar, F. H. R., Kosaka, A. H., Khare, R., Bhakta, S., Jasper, J. R., Shieh, I.-S., Lesnick, J. D., Ford, A. P. D. W., Daniels, D. V., Eglen, R. M., Clarke, D. E., Bach, C., Chan, H. W. Molecular cloning, genomic characterization and expression of novel human alpha-1A-adrenoceptor isoforms. FEBS Lett. 422: 279-283, 1998. [PubMed: 9490024] [Full Text: https://doi.org/10.1016/s0014-5793(98)00024-6]
Forray, C., Bard, J. A., Wetzel, J. M., Chiu, G., Shapiro, E., Tang, R., Lepor, H., Hartig, P. R., Weinshank, R. L., Branchek, T. A., Gluchowski, C. The alpha-1-adrenergic receptor that mediates smooth muscle contraction in human prostate has the pharmacological properties of the cloned human alpha-1C subtype. Molec. Pharm. 45: 703-708, 1994. [PubMed: 8183249]
Hirasawa, A., Horie, K., Tanaka, T., Takagaki, K., Murai, M., Yano, J., Tsujimoto, G. Cloning, functional expression and tissue distribution of human cDNA for the alpha-1C-adrenergic receptor. Biochem. Biophys. Res. Commun. 195: 902-909, 1993. [PubMed: 8396931] [Full Text: https://doi.org/10.1006/bbrc.1993.2130]
Hirasawa, A., Shibata, K., Horie, K., Takei, Y., Obika, K., Tanaka, T., Muramoto, N., Takagaki, K., Yano, J., Tsujimoto, G. Cloning, functional expression and tissue distribution of human alpha-1C-adrenoceptor splice variants. FEBS Lett. 363: 256-260, 1995. [PubMed: 7737411] [Full Text: https://doi.org/10.1016/0014-5793(95)00330-c]
Hoehe, M. R., Berrettini, W. H., Schwinn, D. A., Hsieh, W.-T. A two-allele PstI RFLP for the alpha-1C adrenergic receptor gene (ADRA1C). Hum. Molec. Genet. 1: 349 only, 1992. [PubMed: 1363873] [Full Text: https://doi.org/10.1093/hmg/1.5.349-a]
Schwinn, D. A., Johnston, G. I., Page, S. O., Mosley, M. J., Wilson, K. H., Worman, N. P., Campbell, S., Fidock, M. D., Furness, L. M., Parry-Smith, D. J., Peter, B., Bailey, D. S. Cloning and pharmacological characterization of human alpha-1 adrenergic receptors: sequence corrections and direct comparison with other species homologues. J. Pharm. Exp. Ther. 272: 134-142, 1995. [PubMed: 7815325]
Schwinn, D. A., Lomasney, J. W., Lorenz, W., Szklut, P. J., Fremeau, R. T., Jr., Yang-Feng, T. L., Caron, M. G., Lefkowitz, R. J., Cotecchia, S. Molecular cloning and expression of the cDNA for a novel alpha-1-adrenergic receptor subtype. J. Biol. Chem. 265: 8183-8189, 1990. [PubMed: 1970822]
Tseng-Crank, J., Kost, T., Goetz, A., Hazum, S., Roberson, K. M., Haizlip, J., Godinot, N., Robertson, C. N., Saussy, D. The alpha-1C-adrenoceptor in human prostate: cloning, functional expression, and localization to specific prostatic cell types. Brit. J. Pharm. 115: 1475-1485, 1995. [PubMed: 8564208] [Full Text: https://doi.org/10.1111/j.1476-5381.1995.tb16640.x]
Weinberg, D. H., Trivedi, P., Tan, C. P., Mitra, S., Perkins-Barrow, A., Borkowski, D., Strader, C. D., Bayne, M. Cloning, expression and characterization of human alpha adrenergic receptors alpha-1A, alpha-1B, and alpha-1C. Biochem. Biophys. Res. Commun. 201: 1296-1304, 1994. [PubMed: 8024574] [Full Text: https://doi.org/10.1006/bbrc.1994.1845]