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ADRA1D  -  adrenoceptor alpha 1D

Homo sapiens

Synonyms: ADRA1, ADRA1A, ADRA1R, ALPHA1, Alpha-1A adrenergic receptor, ...
 
 
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Disease relevance of ADRA1D

  • alpha 1-Adrenergic receptors play important roles in mediating a wide range of important cellular responses; regulation of expression of these receptors may have pathophysiological significance in diseases such as hypertension [1].
  • Loss-of-function mutations in a calcium-channel alpha1-subunit gene in Xp11.23 cause incomplete X-linked congenital stationary night blindness [2].
  • Hereditary hyperekplexia, an autosomal dominant neurologic disorder characterized by an exaggerated startle reflex and neonatal hypertonia, can be caused by mutations in the gene encoding the alpha 1 subunit of the inhibitory glycine receptor (GLRA1) [3].
  • Elevated serum thymosin alpha 1 levels associated with evidence of immune dysregulation in male homosexuals with a history of infectious diseases or Kaposi's sarcoma [4].
  • The transcription rate of genes like albumin and alpha1-antitrypsin is reduced, while the gene coding for phenylalanine hydroxylase is totally silent, giving rise to phenylketonuria [5].
 

Psychiatry related information on ADRA1D

  • Addition of either alpha 1-anti-chymotrypsin or apoE to the A beta peptide promoted a 10- to 20-fold increase in filament formation, with apoE-4, the isoform recently linked to the development of late-onset Alzheimer's disease, showing the highest catalytic activity [6].
  • BACKGROUND: Persons with posttraumatic stress disorder (PTSD) whose trauma-related nightmares improve or resolve with bedtime administration of the alpha-1 adrenergic antagonist prazosin often continue to experience PTSD symptoms during the day [7].
  • This reduction of prepulse inhibition is consistent with the synergistic effect of D1 and D2 DA receptor stimulation noted in studies of dopaminergic influences on stereotyped behavior in rats [8].
  • PURPOSE: We determined whether an extract from the bark of the tree Aspidosperma quebracho blanco, which is used as a prescription drug to treat erectile dysfunction in some countries, can bind to human penile alpha1 and alpha2-adrenoceptors, and cloned human alpha-adrenoceptor subtypes [9].
  • The results suggest that presynaptic alpha 2- or postsynaptic alpha 1-beta-adrenoceptor sensitivity is impaired in panic disorder [10].
 

High impact information on ADRA1D

  • We report that an Ala322Asp mutation in GABRA1, encoding the alpha1 subunit of the gamma-aminobutyric acid receptor subtype A (GABA(A)), is found in affected individuals of a large French Canadian family with juvenile myoclonic epilepsy [11].
  • All 87 patients with the deletional type of hemoglobin H were double heterozygotes in whom there was a deletion of both alpha-globin genes from one chromosome, plus a deletion of the alpha1 or alpha2 gene from the other chromosome (--/alpha- or --/-alpha) [12].
  • Bax consists of 9 alpha helices where the assembly of helices alpha1 through alpha 8 resembles that of the apoptosis inhibitor, Bcl-x(L) [13].
  • Mutation analysis of this new alpha1-subunit gene, CACNA1F, in 20 families with incomplete CSNB revealed six different mutations that are all predicted to cause premature protein truncation [2].
  • The beta- and alpha 1-binding motifs are conserved, and all beta subunits can stimulate current amplitude, voltage dependence, and kinetics when coexpressed with various alpha 1 subunits [14].
 

Chemical compound and disease context of ADRA1D

 

Biological context of ADRA1D

  • Localization of the cDNA for an alpha 1-adrenergic receptor subtype (ADRA1D) to chromosome band 20p13 [20].
  • alpha 1-Adrenergic receptor subtypes differentially control the cell cycle of transfected CHO cells through a cAMP-dependent mechanism involving p27Kip1 [21].
  • In an effort to bridge the gap between molecular biology and pathophysiology, we have chosen a model smooth muscle system, the human prostate, and investigated the role of alpha 1 subtypes in this tissue [22].
  • Radioligand binding results revealed that there were no significant differences in the K(d) between ureteral regions, while a heterogeneous distribution of alpha1 AR binding sites was detected, with the highest density of alpha1 ARs in the distal ureter and a lower similar density in the medial and proximal ureters [23].
  • Nucleotide sequence analysis revealed clone H318/3 was 78% homologous to a rat alpha 1A adrenergic receptor with homology being 95% when comparisons were made in the region that lies between the first to the seventh transmembrane domains [24].
 

Anatomical context of ADRA1D

  • CONCLUSIONS: Human ureter was endowed with each alpha1 AR subtype, although alpha1D and alpha1A ARs were prevalent over alpha1B ARs [23].
  • The current study investigates the role of the alpha-1 adrenoceptor on human mesangial cell scarring [25].
  • We wondered if glucocorticoids might induce expression of alpha 1 adrenergic receptors, which could contribute to the increased sensitivity of vascular smooth muscle to catecholamines that may occur with glucocorticoid excess [26].
  • Taken together, these results show that in differentiated human adipocytes: (1) alpha 1- and beta-adrenergic stimulations induce [Ca2+]i increases with different kinetics and amplitudes; (2) there is a beta 3-adrenergic response similar to the beta 1- or beta 2-adrenergic responses; and (3) there is a marked adrenoceptor heterogeneity [27].
  • In the present work we studied cell-specific localizations of alpha1 adrenergic receptor subtype mRNA (alpha 1a, alpha 1b, alpha 1d), and alpha2 adrenergic receptor subtype mRNA (alpha 2a, alpha 2b, alpha 2c) by in situ hybridization on cryostat sections of human cerebellum (cortical layers and dentate nucleus) [28].
 

Associations of ADRA1D with chemical compounds

 

Physical interactions of ADRA1D

  • We generated alanine substitution mutants of hIFNAR2-IgG and determined that regions of hIFNAR2 are important for the binding of these blocking mAbs and hIFN-alpha2/alpha1 [31].
  • These findings indicate that the carboxy-terminal third of Gi alpha 1 interacts with SSTR3 and is important in transmitting the signal of SSTR3 activation to adenylyl cyclase [32].
  • Human alpha1-acid glycoprotein binds to CCR5 expressed on the plasma membrane of human primary macrophages [33].
  • The AMP-activated protein kinase (AMPK) is a heterotrimer composed of different isoforms of the alphabetagamma subunits, where the alpha1 catalytic subunit binds CFTR [34].
  • These results indicate that human SSTR2 is functionally coupled to Gi alpha 1 protein but not to Gi alpha 2 or Gi alpha 3 when expressed in CHO cells [35].
 

Enzymatic interactions of ADRA1D

  • In the thigh muscle, the alpha AMPK subunits became progressively more phosphorylated on Thr(172) during exercise eliciting a parallel increase in alpha2 but not alpha1 AMPK activity [36].
  • In addition, I alone or in the presence of C4-bp fails to cleave the alpha 1-chain of C4b in the stabilized C4b, 2a complex [37].
  • Sil cells had decreased sialyltransferase activity that catalyzed the transfer of sialic acid residues from CMP-N-acetylneuraminic acid to glycoprotein acceptors containing Gal beta 1 leads to 3GalNAc alpha 1 leads to O-Ser(Thr) chain [38].
  • Reaction dynamics of G-protein catalyzed hydrolysis of GTP as viewed by X-ray crystallographic snapshots of Gi alpha 1 [39].
  • While numerous studies have demonstrated that the myeloperoxidase system found in neutrophils can oxidize and functionally inactivate alpha 1-proteinase inhibitor in vitro, there is little direct evidence that this phenomenon is relevant in vivo [40].
 

Co-localisations of ADRA1D

 

Regulatory relationships of ADRA1D

 

Other interactions of ADRA1D

 

Analytical, diagnostic and therapeutic context of ADRA1D

References

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  4. Elevated serum thymosin alpha 1 levels associated with evidence of immune dysregulation in male homosexuals with a history of infectious diseases or Kaposi's sarcoma. Hersh, E.M., Reuben, J.M., Rios, A., Mansell, P.W., Newell, G.R., McClure, J.E., Goldstein, A.L. N. Engl. J. Med. (1983) [Pubmed]
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  21. alpha 1-Adrenergic receptor subtypes differentially control the cell cycle of transfected CHO cells through a cAMP-dependent mechanism involving p27Kip1. Shibata, K., Katsuma, S., Koshimizu, T., Shinoura, H., Hirasawa, A., Tanoue, A., Tsujimoto, G. J. Biol. Chem. (2003) [Pubmed]
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