Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0432222 (SEM)
 47,337 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Serum dopamine beta-hydroxylase activity was determined in normotensive control subjects and patients with labile or established essential hypertension. The enzyme activity was 25-9 +/- 1-9 (SEM) 29-6 +/- 2-5 and 25-1 +/- 1-9 micronmol min-1 1-1, for control, labile and established hypertensive subjects respectively. 2. Neither blood pressure nor serum dopamine beta-hydroxylase activity was changed in normotensive control subjects by administration of phentolamine; however, in patients with essential hypertension blood pressure was significantly decreased (P is less than 0-01) and serum dopamine beta-hydroxylase activity was slightly increased. With propranolol administration, blood pressure and the serum enzyme activity were not significantly changed in normotensive or hypertensive subjects. 3. Our results suggest that there is no correlation between serum dopamine beta-hydroxylase activity and blood pressure.
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PMID:Serum dopamine beta-hydroxylase activity in essential hypertension. 107 65

The diagnosis of recurrent hereditary polyserositis (RHP; also known as familial Mediterranean fever) remains one of exclusion since there has been no specific diagnostic laboratory test. A previous study suggested that the disorder is related to abnormal catecholamine metabolism. Plasma dopamine beta-hydroxylase (DBH) activity was assayed spectrophotometrically in 91 RHP patients and 162 controls. The activity was significantly higher in untreated symptom-free patients and in patients with acute attacks, than in controls (mean [SEM] 155.8 [14.1] vs 43.3 [1.9] mumol/min/1 p less than 0.0001). Colchicine treatment reduced DBH activity to control levels. The test showed a high diagnostic accuracy and specificity for RHP, whether the patient was symptom-free or having an acute attack. Moreover, it is easy to carry out.
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PMID:Plasma dopamine beta-hydroxylase: rapid diagnostic test for recurrent hereditary polyserositis. 290 7

Clonal variants of PC12 cells with respect to catecholamine biosynthesis were isolated, and the catecholamine content was measured by high performance liquid chromatography with electrochemical detection. The dopamine content of 13 subclones, which were selected and isolated in tyrosine-free medium, was substantially higher than the control level: 0.91 +/- 0.10 nmol/mg protein (mean +/- SEM; n = 3). In contrast, the noradrenaline content showed a marked heterogeneity: only two subclones contained noradrenaline levels similar to or higher than the control level: 0.40 +/- 0.05 (n = 5). The rest of them contained below the level of 0.20, and only negligible amounts of noradrenaline were found in four subclones. Thus, the noradrenaline-to-dopamine ratio varied widely between 0.003:1 and 0.53:1. This divergence of the noradrenaline content appears to be related to differing levels of dopamine beta-monooxygenase activity. The administration of ascorbate to the medium alone, however, did not restore the level of noradrenaline to the normal level in a subclone. Heterogeneity of the response to applied glucocorticoid was also demonstrated.
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PMID:Clonal variability of PC12 pheochromocytoma cells with respect to catecholamine biosynthesis. 670 45

Changes in adrenal hormones during the complete developmental cycle from egg to juvenile were investigated in the amphibian Xenopus laevis. Whole-body concentrations of the adrenal steroids corticosterone (B), and aldosterone (Aldo) were determined by radioimmunoassay and those of the adrenal catecholamines epinephrine (E), norepinephrine (NE), and dopamine (D) were determined by HPLC. In addition, the catecholamine-synthesizing enzymes tyrosine hydroxylase, dopamine beta-hydroxylase, and phenylethanolamine N-methyltransferase were immunocytochemically localized for the characterization of chromaffin adrenal cells. B and Aldo were not detectable in the whole body before hatching. B levels rose earlier than Aldo levels from stage 36 onward. B had already peaked at stage 46, whereas the largest amounts of Aldo were found at stage 54. After peaking, both steroids decreased gradually to 2.7 +/- 0.62 (B) and 0.4 +/- 0.1 (Aldo) ng/g body wt (mean +/- SEM, n = 10) in juvenile animals. E, NE, and D were detected just after hatching, when E and D showed an early peak at stage 40. E and NE increased moderately during development and demonstrated a sharp increase at the end of metamorphosis from stages 62 onward to 14.4 +/- 1.7 (E) and 34.1 +/- 4.67 (NE) ng/g body wt (mean +/- SEM, n = 6). Interestingly, D levels had a distinct pattern, because concentrations of D remained lower than those of NE and E over nearly the complete development, but showed a dramatic rise during the latest stages, reaching 707 +/- 54 ng/g body wt in juveniles. This dramatic shift in catecholamine levels was confirmed by immunocytochemistry in parallel. A large increase in chromaffin cells labeled with tyrosine hydroxylase immunoreactivity occurred in the latest developmental stages. The catabolic rates for all catecholamines in vivo were similar, which indicates that the different levels are due to various rates of synthesis. Thus, adrenal corticosteroids as well as catecholamines may have regulatory effects during premetamorphosis and metamorphic climax.
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PMID:Stage-dependent changes in adrenal steroids and catecholamines during development in Xenopus laevis. 940 18

Mesangial cells (MC) participate in the control of the glomerular function due to their ability to synthesize hormones and induce cell contraction. Since MC can produce various kinds of hormones, the purpose of the present study was to determine if they are able to synthesize catecholamines. For this evaluation, the levels of norepinephrine, epinephrine, dopamine, and biopterin, the enzymatic cofactor of tyrosine hydroxylase (TH), were analyzed by HPLC in the intracellular compartment and in the medium of primary cultured MC. To identify and locate the enzymes responsible for monoamine synthesis, TH, dopa decarboxylase, and dopamine beta-hydroxylase, Western blotting and immunocytochemistry were employed using monoclonal and polyclonal antibodies. Concentrations of NE = 57 +/- 8, EPI = 82 +/- 10, and DA = 52 +/- 9 pg/mg protein (X +/- SEM) were found in the cell homogenate. The culture medium showed concentrations of NE = 25 +/- 3, EPI = 33 +/- 3, and DA = 62 +/- 15 pg/mg protein. Western blotting analysis and immunocytochemistry evidenced the presence of all enzymes. Moreover, biopterin was also detected in the intracellular compartment and in the medium (0.28 +/- 0.03 and 5.70 +/- 2 nmol/mg cell protein, respectively). Overall, the data indicate that MC have the biosynthetic machinery necessary to produce catecholamines, suggesting that they can act as a paracrine/autocrine hormone system, contributing to the regulation of glomerular hemodynamic and renal microcirculation.
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PMID:Mesangial cells are able to produce catecholamines in vitro. 1268 15

The growth hormone (GH) axis is sensitive to alteration in body weight and there is evidence that central noradrenergic systems regulate neurones that produce growth hormone-releasing hormone (GHRH) and somatostatin (SRIF). This study reports semiquantitative estimates of the noradrenergic input to neuroendocrine GHRH and SRIF neurones in the sheep of different body weights. We also studied the effects of altered body weight on expression of dopamine beta-hydroxylase (DBH), the enzyme that produces noradrenalin from dopamine. Ovariectomised ewes were made Lean (39.6 +/- 2.6 kg; Mean +/- SEM) by dietary restriction, whereas Normally Fed animals (61.2 +/- 0.8 kg) were maintained on a regular diet. Brains were perfused for immunohistochemistry and in situ hybridisation. The Mean +/- SEM number of GHRH-immunoreactive (-IR) cells was lower in Normally Fed (65 +/- 7) than in Lean (115 +/- 14) animals, whereas the number of SRIF-IR cells was similar in the two groups (Normally Fed, 196 +/- 17; Lean 230 +/- 21). Confocal microscopic analysis revealed that the percentage of GHRH-IR cells (Normally Fed 36 +/- 1.5% versus Lean 32 +/- 4.6%) and percentage of SRIF-IR cells (Normally Fed 30 +/- 40.4% versus Lean 32 +/- 2.3%) contacted by noradrenergic fibres did not change with body weight. FluoroGold retrograde tracer injections confirmed that noradrenergic projections to the arcuate nucleus are from ventrolateral medulla and noradrenergic projections to periventricular nucleus arise from the ventrolateral medulla, nucleus of solitary tract, locus coeruleus (LC) and the parabrachial nucleus (PBN). DBH expressing cells were identified using immunohistochemistry and in situ hybridisation and the level of expression (silver grains/cell) quantified by image analysis. The number of DBH cells was similar in Normally Fed and Lean animals, but the level of expression/cell was lower (P < 0.02) in the PBN and LC of Lean animals. These results provide an anatomical basis for the noradrenergic regulation of GHRH and SRIF cells and GH secretion. Altered activity or noradrenergic neurones in the PBN and LC that occur with reduced body weight may be relevant to the control of GH axis.
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PMID:Noradrenergic regulation of hypothalamic cells that produce growth hormone-releasing hormone and somatostatin and the effect of altered adiposity in sheep. 1592 40

The present work proposes an extra neural site of catecholamine production along the nephron. LLC-PK(1), MDCK, and mIMCD-3 (proximal and distal tubules and inner medullary collecting duct, respectively) presented the following amine concentrations in the cell homogenates: Norepinephrine = 275+/-34, 56+/-16 and 255+/-21; Epinephrine = 161+/-20, 83+/-17 and 53+/-7; and Dopamine = 63+/-15, 39+/-6 and 36+/-7 pg/mg cell protein (Means +/- SEM), respectively. The culture medium showed Norepinephrine = 168+/-25, 22+/-3 and 135+/-8; Epinephrine = 32+/-6, 152+/-17 and 39+/-5; and Dopamine = 27+/-9, 241+/-34 and 26+/-5 pg/mg cell protein, respectively. The synthesis enzymes as tyrosine hydroxylase, dopa decarboxylase and dopamine beta-hydroxylase were detected by Western blotting. Biopterin, the enzymatic cofactor of tyrosine hydroxylase, was quantified in the intracellular and medium of mIMCD-3 cells (17+/-4 and 24+/-3 nmol/mg cell protein, respectively) and in the medium of MDCK cells (19+/-4 nmol/mg cell protein). The data confirmed that the proximal tubule is an important source of dopa decarboxilase and Dopamine and epithelial cell along the nephron express the biochemical pathway for catecholamine production.
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PMID:Catecholamine production along the nephron. 1798 74

A sandwich enzyme immunoassay (EIA) was established by using purified human serum dopamine-?-hydroxylase (DBH) as a standard protein and a monospecific polyclonal antibody raised against human DBH purified from human pheochromocytoma. The EIA was applied to measuring DBH levels in human CSF from Parkinsonian patients and control patients devoid of neurological diseases. The control group had DBH content of 21.1 +/- 3.1 ng/ml CSF and DBH activity of 24.0 +/- 3.7 ? U/ml CSF, and Parkinsonian group 3.3 ? 0.7 ng/ml CSF (16% of control) and 4.6 +/- 0.7 ?U/ml CSF (19% of control) (mean +/- SEM). Thus, both DBH content and DBH activity in CSF were reduced in Parkinsonian patients to less than 20% of the control values (P $ ? 0.005 ). However, the specific activity (units of enzyme activity/mg of DBH protein) in CSF of Parkinsonian patients was similar to that of control patients. These results suggest that the reduced DBH activity in CSF from Parkinsonian patients is caused by a reduction in DBH protein content, and is not due to production of an inactive form of DBH, for example, by combining with endogenous inhibitor(s). These data support our previous findings that DBH activities in the Parkinsonian brain and CSF are decreased.
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PMID:Sandwich enzyme immunoassay of dopamine-?-hydroxylase in cerebrospinal fluid from control and parkinsonian patients. 2050 Dec 20