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)

The histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.
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PMID:Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 0 44

The histochemistry of the neural cells was studied in the submandibular ganglia of 5 Callithrix jacchus (3 males and 2 females) and 4 Callithrix penicillata (2 males and 2 females). These cells contain neutral mucopolysaccharides, nucleoproteins and lipidic materia, but are apparently devoid of glycogen. It is impossible to demonstrate in them any reactivity for UDPG-GT, phosphorylases, ATPase at pH 6.3, leucine aminopeptidase and alanyl aminopeptidas. The reaction for the other searched enzymes was as follows: weak (F-1,6-P Ald and cytochrome oxidase), weak to moderate (ADH, 6-P-GDH, ICDH, SDH, MDH, alpha-GPDH and beta-OHBDH), moderate (G-6-PDH, F-1,6-PA, LDH and GDH), moderate to strong (ATPase at pH 7.4, nonspecific esterase and acid phosphatase) and strong (G-6-PA, NADH2,-TR, NADPH2-TR, ATPase at pH 8.5 and 9.4 and alkaline phosphatase).
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PMID:Histochemical studies on the submandibular ganglia of marmosets (Callithrix jacchus and Callithrix penecillata). 14 13

The structure and histochemistry of the palmar and plantar skin were studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). In this skin there exist well-developed epidermal ridges, to which are attached one or two ducts of sweat glands. A thick stratum corneum can be seen in the epidermis, while a distinct stratum lucidum cannot be isolated from the other layers. The stratum granulosum is constituted by one or three layers of cells containing keratohyalin granules. Melanin granulations are mainly concentrated in the basal cells of the epidermal ridges. Dendritic melanocytes and amelanotic melanocytes containing alkaline phosphatase are found among the epidermal cells. Glycogen, UDPG-GT and phosphorylases are mainly present in the middle and lower Malpighian cells of the epidermal ridges. Alkaline phosphatase, ATPase, alanyl amino-peptidase and leucine aminopeptidase were absent in the epidermal cells. SDH, cytochrome oxidase, MAO and a certain number of NAD-dependent dehydrogenases (LDH, ADH, MDH, alpha-GPDH, beta-OHBDH and GDH) showed a stronger reactivity in the basal cells and Malpighian layer. The NADP-dependent enzymes (G-6-PDH, 6-PGDH, cis-aconistase and ICDH) were more reactive in the upper Malpighian layer and stratum granulosum. The stratum corneum showed some acid phosphatase and nonspecific esterase reactivity. The collagenous fibers intertwined with a small number of very thin elastic ones and a larger amount of reticular fibers run almost parallel to the epidermal ridges in the papillary body. In the reticular dermis some fibers are disposed transversely to the epidermal ridges. Meissner corpuscles reactive to butyrylcholinesterase, acetylcholinesterase, nonspecific esterase and G-6-PA are disposed at regular intervals and frequently at each side of the epidermal ridges. Pacinian corpuscles were found only in the hypodermis. The eccrine sweat glands contain glycogen, UDPG-GT and phosphorylase in their secretory, ductal and myoepithelial cells. The secretory part shows a uniform reactivity for every dehydrogenase because it contains only one type of cells (clear cells). The intraepidermal segment of the ducts shows a stronger reactivity to nonspecific esterase and NADP-dependent dehydrogenases than the epithelial cells around it.
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PMID:The skin of the palms and soles of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 86

Infusions (20 microliter/min) of hypertonic (0.3 M) NaCl and angiotensin II (1 ng/kg min-1) in isotonic (0.15 M) NaCl were made for 1 h in the hydrated goat during fully developed water diruesis. Either H2O or deuterium (D2O) WAS USED AS SOLVENT. A pronounced antidiuretic response, outlasting the infusion period by 30 min or more, was seen when the substances were dissolved in H2O. Only a weak inhibition of the water diuresis, which was extinguished during the infusion period, was obtained when D2O was used as the solvent. The infusion of 0.3 M NaCl/H2O invariably induced drinking in one of the goats, which, however, showed no drinking response to the infusions of 0.3 M NaCl/D2O. The possibility is discussed that D2O (perhaps by its inhibitory effect on (Na+-K+)-ATPase activity) reduced the sensitivity of juxtaventricular receptors regulating ADH-release and water intake.
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PMID:Deuterium induced extinction of ADH-release in response to intracerebroventricular infusions of hypertonic NaCl and angiotensin. 89 28

1. The effect of T-2 toxin on active sodium transport across frog skin both in the presence and in the absence of stimulants of sodium transport, such as Amphotericin B and ADH, was studied using the short circuit current technique with the following results. 2. T-2 toxin produces inhibition of active sodium transport in a dose-response correlation. 3. This effect is irreversible since the washing out of the tissue does not restore its functionality. This indicates that the micotoxin may cross the cellular membrane and act on the internal site. 4. ADH partially removes the inhibitory effect of T-2 toxin. 5. The increase of the sodium pool in the cell as determined by Amphotericin B does not reverse the inhibitory effect of T-2 toxin. 6. The biological significance of these data is discussed in regard to the possible effect of T-2 toxin on Na+, K+-ATPase activity either directly or by a reduction in the metabolic supply of substrates, or by a modified stoichiometry of the pump reaction.
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PMID:The effect of T-2 toxin on active sodium transport across frog skin in the presence of ADH and amphotericin B. 256 25

The calcium-regulating enzyme calcium adenosine triphosphatase (Ca-ATPase) was localized in the epithelium of amphibian urinary bladder by the one-step electron microscopic cytochemical procedure. The enzyme was identified along the basolateral border of the epithelial cells that comprise the bladder mucosa. The electron-dense precipitate indicating Ca-ATPase activity was seen in association with the outer leaflet of the basolateral plasmalemmae. Intracellularly, Ca-ATPase activity was seen in association with the mitochondrial matrix of the mitochondria-rich cells. Ca-ATPase was not seen along the apical microvillated border. Enzyme activity was also not seen after incubation in substrate-free media, calcium-free media, or incubation in the presence of vanadate. However, Ca-ATPase activity was evident when the calcium in the standard reaction medium was deleted in favor of magnesium. Addition of antidiuretic hormone (ADH; vasopressin) increased both the basolateral Ca-ATPase reaction and the mitochondrial reaction. Such data appear to indicate further that changes in cytosolic calcium ion concentration take place during the response of amphibian urinary bladder to the polypeptide hormone vasopressin.
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PMID:Electron microscopic cytochemical localization of Ca-ATPase in toad urinary bladder. 294 49

There appears to be two distinct natriuretic factors. One group, suspected since 1951 in overloaded dogs, had a low molecular weight: it belongs great affinity for ouabain, binds to digoxin antibodies and inhibits NA-K ATPase; this group seems heterogeneous in spite of the extraction of an amino glucosteroid-like substance from human urines. These factors are vasoconstrictor; the source is not still well known (hypothalamus ?). The atrial natriuretic factor (ANF) is a peptide about 20 to 25 amino acids and comes from a precursor of 152 amino acids, its synthesis was successful; secreted in the plasma from endocrine atrial granules, it causes striking natriuresis and diuresis and relaxes vascular and intestinal smooth muscle; it acts on guanylate cyclase but its renal mechanism of action is not well known; it constitutes an antagonist axe to ADH and RAA system. The relations between the two groups of natriuretic factors do not seem still very clear.
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PMID:[Natriuretic factors]. 295 21

The medullary thick ascending limb (MAL), but not the medullary collecting tubule (MCT), has been shown to have an impaired adenylate cyclase (AC) responsiveness to ADH and a selective hypoplasia in Brattleboro diabetes insipidus (DI) rats. Since chronic ADH administration has been found to increase epithelium volume and basolateral membrane surface area in MAL but not in MCT, we investigated whether chronic ADH infusion would affect the hormone-sensitive AC and the Na-K-ATPase activity--two markers of the basolateral membrane--in single micro-dissected portions of thick ascending limb and collecting tubule in DI rats. Results indicate that 1. in MAL of ADH-treated rats, AC responses to in vitro AVP and glucagon and Na-K-ATPase activity increased to the same extent as did epithelium volume (60-80%); 2. changes in the other segments were independent of any morphological alteration. In the cortical thick ascending limb, AVP and glucagon-sensitive AC decreased by 30-40% whereas Na-K-ATPase activity did not change. In the collecting tubule, AC response to in vitro AVP was not altered by ADH-treatment but glucagon-sensitive AC dropped by 50% and Na-K-ATPase activity doubled, independently of any variation in plasma aldosterone and glucagon levels. These results show that, in the MAL, the ADH-induced variations in enzyme activity are a reflection of the enlargement of the basolateral membrane surface area. Further studies are needed to clarify the origin of enzymatic alterations in the other segments.
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PMID:Influence of chronic ADH treatment on adenylate cyclase and ATPase activity in distal nephron segments of diabetes insipidus Brattleboro rats. 299 94

The effect on transepithelial Na transport of tizolemide was investigated in isolated frog skin (Rana temporaria). It was found that tizolemide (2-5 mM, serosal side) decreased transepithelial Na transport (measured as short circuit current and as net sodium flux) within 60 min to 25-40% of the control level resulting from reduction of the unidirectional sodium influx. Intracellular recording with microelectrodes revealed that these changes were associated with depolarization of the intracellular space to less than 40% of the control values (averaging - 71.7 +/- 5.1 mV) which is a consequence of a decrease in conductance of the basolateral border to about 25% of the control values. The conductance of the apical border was only slightly reduced. It is suggested that tizolemide blocks the partial conductance of potassium at the basolateral border which secondarily diminishes transepithelial Na transport due to a decrease of the driving force for apical border Na entry. A certain degree of inhibition of the Na-K-ATPase by tizolemide cannot be excluded. When vasopressin (ADH) was added to frog skin after treatment with tizolemide, the response was markedly reduced compared to that of untreated control preparations. Under these conditions, the conductance of the basolateral border increased while the apical border remained little influenced by the hormone--opposite to the response of frog skins under control conditions. It is concluded that the mode of action of ADH is more complex than has been recognized hitherto and includes effects at the basolateral border.
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PMID:Tizolemide-induced changes of passive transport components across the basolateral membrane of isolated frog skin. 628 44

Maternal ethanol consumption produces a reduction in postnatal growth. We have studied especially changes of liver and brain. This reduction is more marked if the alcoholic offspring are maintained with their biological mothers than if they are kept with surrogate mothers. Rats exposed prenatally to alcohol show a marked accumulation of fat in the liver and a significant proliferation of liver endoplasmic reticulum. No change in the postnatal development of liver alcohol (ADH) and acetaldehyde dehydrogenases (ALDH) (high and low Km) is observed in offspring from alcoholic mothers, with the exception of slightly higher ALDH (low Km) for the offspring that remain with alcoholic mothers. The postnatal development of the liver (Na+-K+) ATPase is also similar in control and alcoholic groups. However, in the case of the enzyme from the brain, a lower ATPase activity is observed in the group derived from alcoholic mothers. Interestingly, at 20 days of postnatal period, an induction of the ATPase (from liver and brain) was observed when the group of offspring from alcoholic mothers were kept on an alcohol diet.
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PMID:Effects of prenatal and postnatal exposure of rats to alcohol: changes in (Na+-K+) ATPase. 629 87


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