The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

DBH  -  dopamine beta-hydroxylase (dopamine beta...

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of DBH

  • The mature protein sequence was 84% homologous to that of human pheochromocytoma DBH, including preservation of four potential copper ligand sites (HH or HXH) and substrate binding domains [1].
  • The disappearance curve of heterologous enzyme (bovine DBH) was more rapid than that of the rat, yielding an MCR of about 8 ml/hr/100 g body weight [2].
  • Circulatory dopamine-beta-hydroxylase (DBH) activity was increased as much as 6-fold in rats with streptozotocin-induced diabetes mellitus [3].

High impact information on DBH


Chemical compound and disease context of DBH


Biological context of DBH

  • The clone hybridizes to two oligonucleotide probes, one based on a previously reported active site peptide [DeWolf, W. E., Jr., et al. (1988) Biochemistry 27, 9093-9101] and the other based on the human DBH sequence [Lamouroux, A., et al. (1987) EMBO J. 6, 3931-3937] [8].
  • The longest cDNA had an open reading frame encoding an entire mature DBH 578 amino acid (64,808 dalton) polypeptide chain, though lacking a portion of the signal peptide [1].
  • We isolated DBH cDNA clones from a bovine adrenal medulla cDNA library in the vector lambda gt10 [1].
  • Prokaryotic DBH expression yielded a 65-kilodalton DBH-immunoreactive peptide that differed from eukaryotic adrenal DBH only in N-linked, endoglycosidase F-sensitive glycosylation in the latter [1].
  • Similar results were obtained with glycosylated and deglycosylated DBH, suggesting that the anti-BAR antibodies recognize specific portions of DBH amino acid sequence and not associated carbohydrate [9].

Anatomical context of DBH

  • A cDNA clone encoding bovine dopamine beta-hydroxylase (DBH) has been isolated from bovine adrenal glands [8].
  • Nevertheless, quantitation of labeled DBH using [125I] streptavidin suggested that it remained undegraded over a period of 24 h, a time during which secretory granule stores of catecholamines were being replenished [10].
  • Significant levels of DBH activity were measured in neural crest cell cultures grown in 10% embryo extract containing medium or in NTCM, while only low levels were present in cultures grown in medium containing 2% embryo extract [11].
  • Subcellular fractionation of the cultured cells suggested that, after 3 or 4 h, the biotinylated DBH, which was still membrane-bound, was located in particulate material that also contained cytochrome b561, another major secretory granule membrane component [10].
  • The present results provide pharmacological evidence for a parallel release of catecholamines, AChE, and DBH from cultured adrenal chromaffin cells, and the stoichiometry of the release evoked by different secretagogues suggests that AChE and catecholamines are released from different cellular compartments [12].

Associations of DBH with chemical compounds

  • Dopamine-beta-hydroxylase (DBH), the enzyme that catalyzes the conversion of dopamine to norepinephrine, remains the topic of many unanswered questions [1].
  • The anion-activated DBH was inhibited when assayed with ferrocyanide and activated when assayed with TMPD as electron donors by increasing the pH (5.1 to 6.0) [13].
  • The glucose analogue, 2-deoxy-D-glucose, has a similar effect on plasma DBH activity levels, eliciting high glycemia values [14].
  • Other sugars that can compete for glycoprotein catabolic receptors can also modulate the plasma DBH activity levels [14].
  • The heterologous half-life of DBH in STZ-diabetic rats is significantly increased compared with that of control animals [14].

Regulatory relationships of DBH

  • In the absence of the growth factor, the mRNA levels of TH and DBH were decreased to 45 +/- 10% and 35 +/- 12% of the time-zero control within 48 h while PNMT mRNA was decreased to 82 +/- 5% only after 72 h [15].
  • The Ca++ ionophore A23187 (100nM) specifically reduced DBH mRNA to 15 +/- 10% of the untreated control while tyrosine hydroxylase was induced (142 +/- 15%) and phenylethanolamine N-methyltransferase was unchanged (107 +/- 11%) [16].
  • These results indicate that NPY has the ability to inhibit the catalytic action of DBH [17].

Other interactions of DBH

  • Further analysis by RNA blot hybridization revealed that the DBH cDNA probe hybridized predominantly to a 5500 nucleotide mRNA and less strongly to a 1100 nucleotide species, and the PNMT cDNA probe hybridized strongly to the 1100 nucleotide mRNA and weakly to the 5500 nucleotide message [18].
  • DBH up-regulation by PACAP was reduced by H-89 and not further increased by forskolin showing involvement of cAMP/PKA [19].
  • When the cells were cotreated with the protein tyrosine kinase inhibitor genistein, DBH induction by IGF-I was suppressed, confirming that the effect is mediated by tyrosine kinase [15].
  • A pharmacological study was made of the effects of veratridine and lasalocid on the release of catecholamines, acetylcholinesterase (AChE) and dopamine-beta-hydroxylase (DBH) from cultures of isolated bovine adrenal chromaffin cells [12].
  • NPY (20-80 pmol/ml) produced a dose-dependent depression of NE formation catalysed by the purified bovine adrenal DBH [17].

Analytical, diagnostic and therapeutic context of DBH


  1. Molecular cloning, structure, and expression of dopamine-beta-hydroxylase from bovine adrenal medulla. Wu, H.J., Parmer, R.J., Koop, A.H., Rozansky, D.J., O'Connor, D.T. J. Neurochem. (1990) [Pubmed]
  2. Metabolic clearance rate of dopamine beta-hydroxylase in the rat. Stolk, J.M., Hurst, J.H., Guchhait, R.B., Vantini, G., Lefort, G.P., Nisula, B.C. Mol. Pharmacol. (1983) [Pubmed]
  3. Circulating dopamine-beta-hydroxylase in the rat: importance of altered disposal pathways in experimental diabetes. Hurst, J.H., Nisula, B.C., Stolk, J.M. J. Pharmacol. Exp. Ther. (1982) [Pubmed]
  4. Functional and morphological characterization of isolated bovine adrenal medullary cells. Fenwick, E.M., Fajdiga, P.B., Howe, N.B., Livett, B.G. J. Cell Biol. (1978) [Pubmed]
  5. Kinetic evidence for channeling of dopamine between monoamine transporter and membranous dopamine-beta-monooxygenase in chromaffin granule ghosts. Wimalasena, D.S., Wimalasena, K. J. Biol. Chem. (2004) [Pubmed]
  6. Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species. Evans, J.P., Ahn, K., Klinman, J.P. J. Biol. Chem. (2003) [Pubmed]
  7. Inhibition of dopamine beta-hydroxylase by 4-hydroxypyrazole: ethanol-pyrazole effects on serum dopamine beta-hydroxylase in vivo. Harralson, J.D., Wolfe, B.I., Brown, F.C. J. Pharmacol. Exp. Ther. (1978) [Pubmed]
  8. Bovine dopamine beta-hydroxylase, primary structure determined by cDNA cloning and amino acid sequencing. Wang, N., Southan, C., DeWolf, W.E., Wells, T.N., Kruse, L.I., Leatherbarrow, R.J. Biochemistry (1990) [Pubmed]
  9. Immuno cross-reactivity suggests that catecholamine biosynthesis enzymes and beta-adrenergic receptors may be related. Shorr, R.G., Minnich, M.D., Varrichio, A., Strohsacker, M.W., Gotlib, L., Kruse, L.I., DeWolf, W.E., Crooke, S.T. Mol. Pharmacol. (1987) [Pubmed]
  10. The recycling of a secretory granule membrane protein. Hunter, A., Phillips, J.H. Exp. Cell Res. (1989) [Pubmed]
  11. Neural tube-derived factors influence differentiation of neural crest cells in vitro: effects on activity of neurotransmitter biosynthetic enzymes. Howard, M.J., Bronner-Fraser, M. Dev. Biol. (1986) [Pubmed]
  12. Parallel but separate release of catecholamines and acetylcholinesterase from stimulated adrenal chromaffin cells in culture. Mizobe, F., Iwamoto, M., Livett, B.G. J. Neurochem. (1984) [Pubmed]
  13. Anion- and pH-dependent activation of the soluble form of dopamine beta-hydroxylase. Terland, O., Flatmark, T. Biochem. J. (2003) [Pubmed]
  14. Effect of diabetic hyperglycemia and other sugars on plasma dopamine-beta-hydroxylase activity. Muñoz, A., Serrano, C., García-Estañ, J., Quesada, T., Miras Portugal, M.T. Diabetes (1984) [Pubmed]
  15. Induction of gene expression of the catecholamine-synthesizing enzymes by insulin-like growth factor-I. Hwang, O., Choi, H.J. J. Neurochem. (1995) [Pubmed]
  16. Reduction of dopamine beta-hydroxylase gene expression by calcium in bovine chromaffin cells. Hwang, O., Lee, J.D. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  17. Inhibitory effect of neuropeptide Y (NPY) on the in vitro activity of dopamine-beta-hydroxylase. Cheng, J.T., Chang, C.L., Tsai, C.L. Neurosci. Lett. (1992) [Pubmed]
  18. Molecular biology of catecholamine neurons. Similar gene hypothesis. Joh, T.H., Baetge, E.E., Reis, D.J. Hypertension (1984) [Pubmed]
  19. Differential involvement of PKA and PKC in regulation of catecholamine enzyme genes by PACAP. Choi, H.J., Park, S.Y., Hwang, O. Peptides (1999) [Pubmed]
  20. Purification and properties of bovine brain dopamine beta-hydroxylase. Matsui, H., Yamamoto, C., Nagatsu, T. J. Neurochem. (1982) [Pubmed]
  21. Release of catecholamines and dopamine beta-hydroxylase from the perfused adrenal gland of the cat. Dixon, W.R., Garcia, A.G., Kirpekar, S.M. J. Physiol. (Lond.) (1975) [Pubmed]
WikiGenes - Universities