Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1332347 (ADH)
 2,230 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Toad urinary bladder epithelial cells respond to the hormone ADH by increasing the water permeability of their luminal membrane. This action is mediated by insertion into the apical membrane of specific water channels. In the absence of ADH these channels appear to be present in tubular cytoplasmic vesicles as morphologically distinctive intramembrane structures called particle aggregates. ADH induces these vesicles to fuse with the apical membrane, transferring their aggregate-water channels into the apical membrane. When ADH stimulation is removed (ADH reversal), aggregates and fluid-phase markers from the mucosal bath appear in water-permeable vesicles in the cytoplasm. We have examined the fate of fluid-phase markers and aggregates with time after ADH reversal. Although the fluid-phase markers horseradish peroxidase and colloidal gold are initially found predominantly in tubular vesicles near the apical surface, by 30 min the markers were found in perinuclear multivesicular bodies (MVBs) of heterogeneous size and shape. These MVBs appear to be nonacidic since they fail to accumulate DAMP. Acid phosphatase (AcPase) was undetectable in these structures. After 60 min, labeled MVBs tended to be smaller, and some of these structures displayed DAMP accumulation and AcPase activity. By evaluation of uncleaned replicas it was possible to localize recycled aggregate-water channels with respect to internalized fluid-phase markers. Thirty minutes after retrieval from the apical surface in tubular vesicles, aggregates could be localized to both the central body and tubular projections of labeled MVBs. At 60 min following reversal, most MVBs had a reduced number of aggregates compared with 30 min, and compact structures could be identified that contained markers but no detectable aggregates. These observations show that aggregates and fluid-phase markers enter a nonacidic endosomal compartment with an MVB morphology following ADH reversal. At extended times following reversal, labeled MVBS having lysosomal characteristics and labeled MVBs having no detectable aggregates can be found, suggesting that aggregates are sorted or degraded prior to this stage.
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PMID:Role of nonacidic endosomes in recycling of ADH-sensitive water channel structures. 137 33

The tissue specific patterns for Drosophila melanogaster alcohol dehydrogenase (Adh) mRNA and protein expression were determined using in situ hybridization and immunocytochemical techniques. Alcohol dehydrogenase mRNAs were localized in thin sections of frozen tissue using the hybridization of single stranded RNA probes. Alcohol dehydrogenase protein was identified in frozen tissue samples using ADH antisera, a biotinylated secondary antibody, and streptavidin conjugated to horseradish peroxidase. In tissues such as fat body, gastric caeca, and adult cardiac valve, the patterns of expression for ADH protein and mRNA were identical. Other tissues such as oocytes, nurse cells, imaginal disks, and brain show levels of Adh mRNA that are lower than or equivalent to those observed in the previously mentioned tissues, but they exhibit little or no ADH protein. The lack of concordance between Adh mRNA and ADH protein expression in oocytes and nurse cells may reflect the packaging of maternal mRNAs (but not ADH protein) for use in early development. The reason(s) for the other discrepancies in protein and mRNA expression are not known at this time but may be due to post-transcriptional regulation in these specific tissues.
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PMID:Tissue specific expression of the Drosophila Adh gene: a comparison of in situ hybridization and immunocytochemistry. 175 67

The presence of secretory protein-I (SP-I) or chromogranin A (CGA) in granules isolated from the granular cells of the amphibian urinary bladder epithelium was investigated using ultraimmunohistochemistry. Granules were isolated by cell fractionation using Percoll density gradients. SP-I was isolated and purified from bovine parathyroid glands. Antibodies were raised in rabbits and purified by affinity chromatography. Ultraimmunocytochemistry, employing the avidin-biotin-peroxidase (ABC-complex) procedure, was used to localize SP-I on thin sections of isolated granules. About 27% of the granules from control (-ADH) cells were SP-I+, while 51% of the granules fractionated from hormone treated (+ADH) cells were positive for this protein (p less than 0.0001). Accordingly, granules from ADH-treated cells also showed a significant (p less than 0.0001) increase in total protein.
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PMID:Immunolocalization of secretory protein-I or chromogranin A in amphibian urinary bladder granular cell granules. 211 25

This study concerns the timing and magnitude of exocytosis and endocytosis in the granular cells of toad bladder during the hydroosmotic response to antidiuretic hormone. Granule exocytosis at the luminal cell surface is extensive within 5 min of the administration of a physiological dose of hormone. Hydroosmosis becomes detectable during this time period. The amount of membrane added to the luminal surface by exocytosis during 60 min of exposure to hormone can be of the same order of magnitude as the extent of the luminal plasma membrane. Endocytosis, demonstrated by peroxidase uptake from the luminal surface, becomes extensive during the period 15-45 min after hormone administration. Thus, maximal endocytic activity occurs later than the period of most extensive exocytosis and seems to correlate with the onset of the decline in water movement. The amount of membrane retrieved from the luminal surface by endocytosis during 60 min of stimulation is at least three quarters of that added by exocytosis. The bulk membrane movement in ADH stimulated preparations does not require the presence of an osmotic gradient. Colchicine inhibits the hydroosmotic response, the exocytosis of granules, and endocytosis at the luminal surface. These results strengthen our view that the bulk circulation of membrane at the cell surface, via exocytosis and endocytosis, is closely related to the permeability changes occurring at the surface.
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PMID:Quantitative analysis of exocytosis and endocytosis in the hydroosmotic response of toad bladder. 677 96

Human liver alcohol dehydrogenase (ADH, EC 1.1.1.1) was purified by double ternary complex affinity chromatography on Sepharose-4-(3-[N-6 aminocaproyl]aminopropyl) pyrazole. The purified enzyme preparation still contains several isoenzymes reflecting the isoenzyme composition of the starting material. Antibodies against this mixture of isoenzymes were elicited in rabbits. The specificity of the antiserum was tested by double immunodiffusion, enzyme-linked immunosorbent assay, immunoprecipitation of ADH enzymatic activity, and adsorption to ADH, which was immobilized to Ultrogel AcA 44 by the use of glutardialdehyde as the coupling agent. Protein-A peroxidase with diaminobenzidine or amino ethyl carbazole as substrate, served to detect binding of anti-human liver ADH antibodies in human liver thin sections, cultured human skin and lung fibroblasts, and HeLa cells. Fluorescein-conjugated antibodies were also used in direct immunofluorescence on liver tissue. In the human liver, ADH was found to be localized in the cytoplasm of hepatocytes. Differences in the staining intensity of hepatocytes may reflect differences in ADH content. Strongly stained hepatocytes were localized mainly around the central veins. Perinuclear staining is often seen, especially in the more lightly stained cells. Human skin and lung fibroblasts, as well as HeLa cells, all exhibited positive staining for ADH. The pattern was identical to that found in hepatocytes, although the staining intensity was much weaker, indicating a lower ADH content.
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PMID:Immunohistochemical localization of human liver alcohol dehydrogenase in liver tissue, cultured fibroblasts, and HeLa cells. 704 56

Antidiuretic hormone (ADH; 2.5 x 10(-8) M vasotocin) produces a stimulation of apical fluid phase endocytosis, protein secretion and NaCl reabsorption in Xenopus laevis A6 distal nephron cell epithelia pretreated with aldosterone (10(-6) M). The increase of NaCl transport is mediated by a sequential opening of apical Cl and Na conductances. The aim of this study was to characterize the actin and tubulin cytoskeleton of A6 cells and to assess the impact of its disruption on baseline and ADH-induced apical vesicular membrane movements and ion transport to test for possible functional links. The microfilament (MF) and microtubule (MT) networks and their disruption were visualized by confocal laser microscopy. Conditions of depolimerization were selected, by cytochalasin D or cold and nocodazole, respectively. MF disruption produced an increase in baseline apical protein secretion (exocytic movements) (plus 18%) and a decrease of its induction by ADH (minus 35%). MF disruption also increased baseline horseradish peroxidase uptake (endocytic movements) (plus 21%), however, without affecting its ADH-induced increase. In the case of MT disruption, the ADH-induced stimulation of both protein secretion and fluid phase endocytosis was decreased by 70 and 44%, respectively. At the ion transport level, MF and MT disruption only insignificantly affected the ADH-induced Cl conductance, while they decreased the ADH-induced stimulation of Na transport (amiloride-sensitive short-circuit current and conductance) by a factor of 2 to 4. In conclusion, both MT and MF disruption decrease ADH-induced apical protein secretion and Na conductance, while the ADH-induced apical Cl conductance is not significantly affected. Taken together the data support the hypothesis that the modulation of Na channel expression by apical vesicular membrane movements plays a role in Na transport expression and its regulation by ADH.
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PMID:Cytoskeletal disruption in A6 kidney cells: impact on endo/exocytosis and NaCl transport regulation by antidiuretic hormone. 756 21

One step competitive enzyme linked immunosorbent assay (ELISA) for direct estimation of testosterone in human serum is described. Testosterone-3-O-carboxymethyl-oxime-bovine serum albumin (testosterone-3-O-CMO-BSA), was used as immunogen and testosterone-3-O-carboxymethyl-oxime-adipic-acid dihydrazide-horseradish peroxidase (testosterone-3-O-CMO-ADH-HRP) was used as tracer. To the testosterone antibody coated microtiter wells, standard or serum samples (100 microL), along with testosterone-3-O-CMO-ADH-HRP conjugate (100 microL) were incubated for 1 h at 37 degrees C. Bound enzyme activity was measured by using tetra methyl benzidine/hydrogen peroxide (TMB/H2O2) as a substrate. In this new strategy, charcoal stripped pooled human serum spiked with non-cross reactive C18, C19, C21, and C27 steroids, used for preparing the standards and blocking the sex hormone binding globulin (SHBG)/and other steroid binding globulins (SBG). The sensitivity of the assay was 0.015 ng/mL. The intra-assay and inter-assay coefficients of variation (CVs) were ranged from 7.8 to 11.8 and 4.8 to 10.4, respectively. The serum testosterone values, obtained by this method, were correlated well with those obtained by radioimmunoassay r = .98 (n = 100).
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PMID:One step enzyme linked immunosorbent assay for direct estimation of serum testosterone. 1277 72

Preparation of horseradish peroxidase (HRP) hydrazide that is HRP linked to adipic acid dihydrazide (HRP-ADH) and its use in enzyme immunoassay (EIA) is described. In this new strategy, horseradish peroxidase was conjugated to adipic acid dihydrazide using a carbodiimide coupling method. The resulting HRP-ADH was then coupled to cortisol-21-hemisuccinate (Cortisol-21-HS) to prepare enzyme conjugate. The prepared cortisol-21-HS coupled ADH-HRP (Cortisol-21-HS-ADH-HRP) enzyme conjugate was used for the development of an enzyme linked immunosorbent assay (ELISA) for direct estimation of cortisol. To the cortisol antibody coated microtiter wells, standard or serum samples (50 microL), along with cortisol-21-HS-ADH-HRP enzyme conjugate (100 microL) were incubated for 1 h at 37 degrees C. Bound enzyme activity was measured by using tetramethyl benzidine/hydrogen peroxide (TMB/H2O2) as substrate. The sensitivity of the assay was 0.05 microg/dL and the analytical recovery ranged from 92.9 to 101.7%.
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PMID:Preparation of horseradish peroxidase hydrazide and its use in immunoassay. 1295 74

The effects of catalase regulators (aminotriazole, lead acetate, taurine, di-2-ethylhexylphthalate) on the preference for ethanol, its pharmacokinetics, and activities of rat liver and brain ethanol and acetaldehyde-metabolizing enzymes were studied. Lead acetate (100 mg/kg, i.p., 7 days), aminotriazole (1 g/kg, i.p., 7 days), and taurine (650 mg/kg, i.g., 14 days) decreased ethanol consumption under conditions of free choice (10% ethanol water), whereas di-2-ethylhexylphthalate (300 mg/kg, i.g., 7 days) did not exert any effect on this parameter. Taurine, lead acetate and di-2-ethylhexylphthalate significantly activated liver ADH, MEOS and catalase peroxidase activity. Aminotriazole also activated ADH and MEOS, but inhibited liver catalase. The activities of liver and brain A1DH as well as catalase were insignificantly changed by this treatment. The 7-day administration of lead acetate, di-2-ethylhexylphthalate and aminotriazole administrations significantly influenced the ethanol (2 g/kg., i.p.) pharmacokinetic parameters: the area under the pharmacokinetic curve and the elimination half-life time were significantly reduced, whereas the elimination constant and clearance were increased. This unequivocally indicates accelerated ethanol elimination. The 14-day ingestion of taurine insignificantly changed the parameters of ethanol pharmacokinetics in rats.
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PMID:[Effects of catalase activators and inhibitors on ethanol pharmacokinetic characteristics and ethanol and aldehyde-metabolizing enzyme activities in the rat liver and brain]. 2103

Seeds and sprouts from legume crop plants have received attention as functional foods, because of their nutritive values including amino acid, fiber, trace elements, vitamins, flavonoids, and phenolic acids. Consumption of seeds and sprouts has become increasingly popular among people interested in improving and maintaining their health status by changing dietary habits. The seeds and sprouts are excellent examples of functional food defined as lowering the risk of various diseases and/or exerting health promoting effects in addition to its nutritive value. Phenolic compounds are considered as secondary metabolites that are synthesized by plants during normal development and in response to stress conditions, and the compounds occur ubiquitously in plants as the diversified group of phytochemicals derived from phenylalanine and tyrosine. Plant phenolics include simple phenols, phenolic acids, coumarins, flavonoids, stilbenes, hydrolyzable and condensed tannins, lignans, and lignins. In plant, phenolics may act as phytoalexins, antifeedants, attractants for pollinators, contributors to the plant pigmentation, antioxidants, and protective agents against UV light, among others. In food, phenolics may contribute to the bitterness, astringency, color, flavor, odor, and oxidative stability of products. In addition, health-protecting capacity of some and antinutritional properties of other plant phenolics are of great importance to producers, processors and consumers. Several researches were conducted to compare the content of phenolics and flavonoids, antioxidant activity and antioxidant enzyme activity from seeds and sprouts of legume plants. Total phenolics (TP) content and total flavonoids (TF) level were highest in soybean sprout extracts, followed by cowpea and mungbean sprout extracts (p < 0.05). DPPH (1, 1-diphenyl-2-picryl hydrazyl radical) free radical scavenging activity was higher in cowpea or mungbean sprouts than in soybean sprouts. Among antioxidant enzymes, ascorbate peroxidase (APX) and peroxidase (POX) activities were highest in cowpea sprouts and catalase (CAT) and superoxide dismutase (SOD) activities in soybean sprouts. During sprouting in mungbean, TP and TF levels significantly increased and improved free radical scavenging, tyrosinase inhibition, anticancer, and ADH (alcohol dehydrogenase) activities, showing higher contents and activities in sprouts than in seeds. Sprouting of seeds is known to increase the nutritive value such as phenolics and flavonoids and the health qualities of foods in a natural way. Phasic bioactive responses from dry seeds to 7-day-old seedlings of cowpea showed differential growth, contents of TP and TF, antioxidant activity and antioxidant enzyme activity. Plant length and weight of cowpea sprouts were significantly increased until 7 days after seeding. TP content, however, was highest in dry seed (DS) extracts of cowpea (63.9 mg kg(1)), followed by imbibed seed (IS) (56.8 mg kg(1)) and 1-day-old sprout (1DOS) (46.4 mg kg(1)) extracts, and significantly reduced with increase of sprout age (p < 0.05). DPPH free radical scavenging activity was higher in DS or IS than in cowpea sprouts. APX, POX, and POX activities were highest in 7DOS and lowest in DS. SOD activity was lowest in DS and much higher in additional sprouting days.
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PMID:Total polyphenols and bioactivity of seeds and sprouts in several legumes. 2344 41


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