Dopamine β‐Hydroxylase: Biochemistry and Molecular Biology

@article{Joh1987DopamineB,
  title={Dopamine $\beta$‐Hydroxylase: Biochemistry and Molecular Biology},
  author={T. Joh and O. Hwang},
  journal={Annals of the New York Academy of Sciences},
  year={1987},
  volume={493}
}
  • T. Joh, O. Hwang
  • Published 1987
  • Chemistry
  • Annals of the New York Academy of Sciences
Dopamine beta-hydroxylase (DBH) catalyzes the conversion of dopamine to norepinephrine (NE), and is known to exist in two forms: soluble and membrane-bound. It has been reported that the two forms are similar in their immunoreactivity, carbohydrate content, and binding affinities for various substrates, and are apparently dissimilar in subunit structures and hydrophilicity. Furthermore, added structural complexity is observed within sDBH itself. Our results indicate that purified sDBH, which… Expand
The primary structure of human dopamine‐beta‐hydroxylase: insights into the relationship between the soluble and the membrane‐bound forms of the enzyme.
TLDR
Comparative amino acid sequence analysis establishes that DBH shares no homology with the other catecholamine synthesizing enzymes, tyrosine hydroxylase and phenylethanolamine‐N‐methyl transferase, and suggests that the membrane attachment of DBH probably results from a post‐translational modification, glypiation being the most likely candidate. Expand
Antibodies raised against different oligopeptide segments of human dopamine-β-hydroxylase
TLDR
Observations suggest that the antibody raised against the hDBH-C terminal peptide may specifically recognize only human DBH. Expand
Effects of cAMP, glucocorticoids, and calcium on dopamine β-hydroxylase gene expression in bovine chromaffin cells
  • O. Hwang, T. Joh
  • Biology, Medicine
  • Journal of Molecular Neuroscience
  • 2007
TLDR
The results demonstrate the existence of coordinate and differential regulations among the enzymes involved in catecholamine biosynthesis in bovine adrenomedullary cells. Expand
A natural variant of bovine dopamine β‐monooxygenase with phenylalanine as residue 208: purification and characterization of the variant homo‐ and heterotetramers of (F208)4 and (F208)2(L208)2
TLDR
Bovine dopamine β‐monooxygenase was purified from each of 18 individual adrenal glands by the method developed for the rapid purification of the enzyme from a single adrenal gland, indicating an allelic polymorphism and codominant expression of the two alleles of the enzymes gene. Expand
Dopamine beta-hydroxylase participate in the immunoendocrine responses of hypothermal stressed white shrimp, Litopenaeus vannamei.
TLDR
Results indicate that LvDBH possesses the functional domains responsible for CAs synthesis, and therefore, inhibiting DBH contents in haemocytes by disulfiram and byLvDBH-dsRNA resulted in the impaired synthesis of NE from DA in haeemolymph. Expand
Gene expression of catecholamine synthesizing enzymes and β adrenoceptor subtypes during rat embryogenesis
TLDR
Results from the present study indicate that catecholamine synthesis is not limited to the cells of sympathoadrenal lineage, and contradicts the common belief thatcatecholamines are produced only in the cells in sympathoadenal lineage. Expand
Immunohistochemical localization of catecholamine-synthesizing enzymes in human pheochromocytomas
TLDR
Primary culture and immunoelectron microscopy suggested the processing and synthesis of adrenalin and MEAGL in the secretory granules. Expand
Interaction studies on catecholamines to cellular receptors using in silico approach
TLDR
The usage of synthetic catecholamine Isoproterenol is suggested to have more binding affinity with adrenergic receptors which could be further analyzed using in vivo study as a future work. Expand
Ultrastructural localization of neurotensin‐like immunoreactivity within dense core vesicles in perikarya, but not terminals, colocalizing tyrosine hydroxylase in the rat ventral tegmental area
TLDR
A direct synaptic basis for modulation of dopaminergic neurons is established in both paranigral and parabrachial pigmentosus subdivisions of the VTA by terminals containing NTLI and further establish a greater coexistence between TH and N TLI in the parabRachial pigmentationosus subdivision by electron microscopy. Expand
Gene expression and the contents of noradrenaline synthesis enzymes in the rat brain during the critical period of morphogenesis
TLDR
The aim of this study was to investigate the molecular-genetic mechanisms of noradrenaline synthesis in the rat brain during the critical period of morphogenesis and it is shown that the mRNA level of these enzymes remains at a stable high level in the perinatal period of ontogeny and decreases slightly by the end of the first month of life. Expand
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References

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Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase☆
Abstract Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose.Expand
Isolation and reconstitution of the membrane-bound form of dopamine beta-hydroxylase.
TLDR
The isolation of a membrane-bound form of dopamine beta-hydroxylase which is structurally different from the soluble form is reported which has a large apparent molecular weight on gel filtration, is amphiphilic, and contains bound phospholipid which is predominantly phosphatidylserine. Expand
Purification and Characterization of Dopamine β ‐Hydroxylase from Bovine Adrenal Medulla
A new purification procedure that permits large-scale purification of dopamine β-hydroxylase from bovine adrenal medulla was developed. Whole adrenal medullas were extracted with 0.1 Triton X- 100,Expand
Evidence that most of the dopamine β-hydroxylase is not membrane bound in purified large dense cored noradrenergic vesicles
Abstract The compartmentalization of dopamine β-hydroxylase was studied in a purified fraction of large, dense-cored noradrenergic vesicles from bovine splenic nerve. A correlative biochemical andExpand
Dopamine β‐Hydroxylase and Other Glycoproteins from the Soluble Content and the Membranes of Adrenal Chromaffin Granules: Isolation and Carbohydrate Analysis
TLDR
Chromogranin A and two other proteins of the soluble proteins of bovine chromaffin granules were isolated by extraction from polyacrylamide gels after electrophoresis and it was shown that all four subunits of dopamine β‐hydroxylase possess carbohydrate chains with an affinity for Con A. Expand
Sulfation and constitutive secretion of dopamine beta-hydroxylase from rat pheochromocytoma (PC12) cells.
TLDR
It is proposed that in addition to the dopamine beta-hydroxylase which is found in catecholamine storage vesicles and released during stimulus-coupled exocytosis, PC12 cells also have a constitutive secretory pathway for dopamine Beta-hydrogenase and that the enzyme released by this second pathway is sulfated. Expand
NH2-Terminal sequence of dopamine β-hydroxylase from bovine adrenal medulla
Abstract Sequence analysis by the automated Edman degradation shows that dopamine β -hydroxylase (dopamine β -monooxygenase; EC 1.14.17.1) from bovine adrenal medulla contains equal amounts ofExpand
Membrane proteins of chromaffin granules, dopamine -hydroxylase, a major constituent.
TLDR
A comparison of the membrane-bound and soluble dopamine beta-hydroxylases revealed the identity of these two preparations, both were activated by N-cetylpyridinium chloride, they migrated identically in polyacrylamide-gel electrophoresis, their amino acid composition was very similar and an immunological cross-reaction could be demonstrated. Expand
In vitro translation of human pheochromocytoma messenger RNAs: characterization of tyrosine-hydroxylase and dopamine-beta-hydroxylase.
mRNAs extracted from human pheochromocytoma were translated in vitro in a lysate of a rabbit reticulocytes. Two enzymes of the biosynthetic pathway of the catecholamines, tyrosine-hydroxylase (TH)Expand
Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase.
TLDR
Immunoelectrophoretic analysis in the presence of Triton X-100 plus the cationic detergent cetyltrimethylammonium bromide indicates additional heterogeneity of the membrane-bound dopamine-beta-hydroxylase. Expand
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