The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme.

Lamouroux, Annie; Vigny, Annette; Biguet, Nicole Faucon; Darmon, Michèle; Franck, R.; Henry, Jean‐Pierre; Mallet, Jacques

doi:10.1002/j.1460-2075.1987.tb02734.x

Cited by 121 publications

(71 citation statements)

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“…The large number of membrane-bound granules present in oocytes (35) may represent the structural component to which DBH is associated. As in neural cells (18,36), some DBH immunoreactivity also was seen in the oocyte's cytoplasm.…”

Section: Discussionmentioning

confidence: 86%

“…The gene-specific oligodeoxynucleotide primers used to isolate an ovarian DBH cDNA consisted of an 18-mer sense primer complementary to nucleotides 846-863 in human DBH mRNA and a 21-mer antisense primer complementary to nucleotides 1087-1107 (18). TH cDNAs were obtained by using the same primers used to isolate testicular TH sequences (16).…”

Section: Methodsmentioning

confidence: 99%

“…(B) Nucleotide and amino acid sequence of a cDNA encoding the mid-portion of DBH mRNA isolated from the rhesus monkey ovary by RT-PCR. The sequence, identical to that isolated from the monkey adrenal, is compared with that of human DBH (18). For other details, see A.…”

Section: Dbh and Th Proteins In Oocytesmentioning

confidence: 99%

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Oocytes are a source of catecholamines in the primate ovary: Evidence for a cell–cell regulatory loop

Mayerhofer

Smith

Danilchik

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Catecholamines, thought to derive from the extrinsic innervation of the ovary, participate in the regulation of ovarian development and mature gonadal function. Recently, intraovarian neurons containing tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, were described in the ovary of nonhuman primates. We now show that the primate ovary expresses both the genes encoding TH and dopamine ␤-hydroxylase (DBH), the key enzymes in norepinephrine (NE) biosynthesis. Ovarian neurons were identified as a site of TH and DBH gene expression, and surprisingly, oocytes were identified as an exclusive site of DBH synthesis. Oocytes contain neither TH mRNA nor protein, indicating that they are unable to synthesize dopamine (DA). They did, however, express a DA transporter gene identical to that found in human brain. The physiological relevance of this transporter system and DBH in oocytes was indicated by the ability of isolated oocytes to metabolize exogenous DA into NE. Isolated follicles containing oocytes-but not those from which the oocytes had been removed-responded to DA with an elevation in cAMP levels; this elevation was prevented by propranolol, a ␤-adrenoreceptor antagonist. The results suggest that oocytes and somatic cells are linked by a neuroendocrine loop consisting of NE synthesized in oocytes from actively transported DA and cAMP produced by somatic follicular cells in response to NE-induced ␤-adrenoreceptor activation.All three major catecholamines used as transmitters by sympathetic neurons of the peripheral nervous system are present in the mammalian ovary (1, 2). Among them, norepinephrine (NE) is the most abundant (1, 3, 4). A variety of experimental approaches have demonstrated that NE, recognized by specific receptors of the ␤ 2 -adrenergic subtype, stimulates ovarian steroidogenesis on its own and facilitates the stimulatory effect of gonadotropins on steroid production (5-7). NE also promotes follicular development (8-10). In contrast to this body of information, very little is known about the potential contribution(s) of dopamine (DA) to ovarian physiology. In one of the few studies on the subject (11), a stimulatory effect of DA on human granulosa cell steroidogenesis was blocked by propranolol, a ␤-adrenoreceptor antagonist, indicating that the effect of the catecholamine was indirect and most likely mediated by NE.It is commonly assumed that catecholamines reach the ovary exclusively via its extrinsic sympathetic innervation (12). However, ovarian denervation reduces, but does not eliminate, the content of NE in the gland (13), implying the existence of an additional source of catecholamine synthesis. That this source may be intrinsic to the ovary has been suggested by the identification of neuronal cell bodies containing immunoreactive tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine biosynthesis, in the ovary of nonhuman primates (14). Whether this is the only, or the more important, intragonadal source of catecholamines in the primate ...

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Section: Discussionmentioning

confidence: 86%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Oocytes are a source of catecholamines in the primate ovary: Evidence for a cell–cell regulatory loop

Mayerhofer

Smith

Danilchik

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…The possible role of DBH as a control point in catecholamine biosynthesis, mechanistic questions regarding the involvement of copper in the hydroxylation reaction, and interactions with other proteins and cofactors within the adrenal chromaffin granule, have generated intense research towards understanding the structure and function of this protein. The recent availability of cDNA-derived protein sequences [2,3] and a complete gene sequence for human DBH [3] are important advances but have not provided direct answers to these questions.…”

Section: Introductionmentioning

confidence: 99%

Sequence similarity between dopamine β‐hydroxylase and peptide α‐amidating enzyme: Evidence for a conserved catalytic domain

Southan¹,

Kruse²

1989

FEBS Letters

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A comparison of human dopamine fl-hydroxylase (EC 1.14.17.1) with bovine peptide C-terminal ~t-amidating enzyme (EC 1.14.17.3), revealed a 28% identity extending throughout a common catalytic domain of approximately 270 residues. The shared biochemical properties of these two enzymes from neurosecretory granules suggests that the sequence similarity reflects a genuine homology and provides a structural basis for a new family of copper type II, ascorbate-dependent monooxygenases.

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“…The human DBH is composed of 603 amino acids. 5,6 Any two amino acids in order can construct a twoamino-acid sequence, thus a total of 602 two-aminoacid sequences can be constructed, ie the first and second, the second and third, the third and fourth, etc. Furthermore, any three amino acids in order can also construct a three-amino-acid sequence, thus a total of 601 three-amino-acid sequences can be constructed, ie the first, second and third; the second, third and fourth; etc.…”

mentioning

confidence: 99%

The first, second, third and fourth order Markov chain analysis on the amino-acid sequence of human dopamine β-hydroxylase

2000

Mol Psychiatry

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The repeated amino-acid sequences in human dopamine ␤-hydroxylase (DBH) may be indispensable for DBH activity, because such repetitions cannot be simply attributed to random chance. The amino acid sequence of human DBH was analysed according to two-, three-, four-and five-amino-acid sequences and their probabilities in human DBH were calculated. The first, second, third and fourth order Markov chain was used to calculate the transition probability for two-, three-, four-and five-amino-acid sequences. The longest repeated sequence is glycine-isoleucine-leucine-glutamic acid-glutamic acid, which appears twice in DBH. The results suggest that the amino acids with a high Markov transition probability may serve as the potential targets of new drugs, because they are unlikely to change into other amino acids. Molecular Psychiatry (2000) 5, 448-451.Human dopamine ␤-hydroxylase (DBH, EC 1.14.17.1) is the enzyme catalysing the conversion of dopamine into noradrenaline, and its activity has been found to be altered in schizophrenia. [1][2][3][4] Further analysis of human DBH primary structure is important for understanding of its activity and its role in schizophrenia. The human DBH is composed of 603 amino acids. 5,6 Any two amino acids in order can construct a twoamino-acid sequence, thus a total of 602 two-aminoacid sequences can be constructed, ie the first and second, the second and third, the third and fourth, etc. Furthermore, any three amino acids in order can also construct a three-amino-acid sequence, thus a total of 601 three-amino-acid sequences can be constructed, ie the first, second and third; the second, third and fourth; etc. Still, a total of 600 sequences can be constructed for four amino-acid sequences, and a total of 599 sequences can be constructed for five amino-acid sequences. The aim of such a study of amino-acid sequences is to view amino-acid sequences as possible 'words' in an unknown 'language' in an abstract sense and to determine: (i) whether an amino acid 'word' can be constructed by three amino acids as a DNA message constructed by three elements. At this stage an amino acid 'word' can be considered to be constructed by any sequence of amino acids; and (ii) whether there are 'punctuation' and 'space' sequences in an amino acid sequence of a protein. We do not know where an amino acid 'word' begins and finishes, consequently an amino acid 'word' can begin and finish anywhere.

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The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme.

Cited by 121 publications

References 70 publications

Oocytes are a source of catecholamines in the primate ovary: Evidence for a cell–cell regulatory loop

Oocytes are a source of catecholamines in the primate ovary: Evidence for a cell–cell regulatory loop

Sequence similarity between dopamine β‐hydroxylase and peptide α‐amidating enzyme: Evidence for a conserved catalytic domain

The first, second, third and fourth order Markov chain analysis on the amino-acid sequence of human dopamine β-hydroxylase

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