Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:1.1.1.1 (alcohol dehydrogenase)
9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A rapid electrochemical measurement of blood ethanol is proposed. Alcohol is oxidized by NAD+ in the presence of alcohol dehydrogenase; and the NADH produced is aerobically oxidized by horseradish peroxidase. The rate of depletion of buffer-carried oxygen, which is directly proportional to the alcohol concentration in the sample, is amperometrically monitored with a membrane oxygen-sensing electrode. Only a 5-microliter sample of whole blood is required, with no deproteinization, incubation, extraction, or dilution. Results, obtained in less than 1 min, correlate well with those obtained by gas-chromatographic and spectrophotometric methods.
...
PMID:Enzymatic determination of blood ethanol, with amperometric measurement of rate of oxygen depletion. 2 44

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.
...
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.
...
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.
...
PMID:Immunolocalization of secretory protein-I or chromogranin A in amphibian urinary bladder granular cell granules. 211 25

Testicular ethanol-metabolizing enzymes (alcohol dehydrogenase, microsomal ethanol-oxidizing system, catalase) were investigated. Alcohol dehydrogenase was purified to homogeneity and its main kinetic parameters were analyzed. It was shown that alcohol dehydrogenase corresponds to class III isozymes and does not participate in ethanol oxidation. The testicular microsomal ethanol-oxidizing activity does not exceed 0.02 nmol/min/mg of protein. The activity of catalase and its peroxidase component is far lower in the testes than in the liver. On the whole, testicular tissue is rather inactive in respect of ethanol oxidation.
...
PMID:[Ethanol-metabolizing enzymes from human testis]. 228 86

The proteins of soybean roots undergoing anaerobiosis can be grouped into three classes. Class 1 proteins are induced severalfold and at least 28 of these were identified by in vivo labeling. These proteins include the enzymes alcohol dehydrogenase (ADH), fructose aldolase, pyruvate decarboxylase, phosphoglucomutase, and lactate dehydrogenase. Class 2 proteins include such enzymes as glucose phosphate isomerase, sucrase, and malate dehydrogenase; their specific activity remains constant in aerobiosis or anaerobiosis. The third class of proteins includes those enzymes such as peroxidase whose activity decreases more than 90% after just 1 day in anaerobiosis. Immunoblotting coupled with two-dimensional chromatography of in vitro translated plant extracts demonstrated that ADH level during anaerobiosis is controlled by its mRNA concentration. Little or no mRNA for ADH was detected in aerobically grown roots. This suggests that the increased level of ADH activity is due to de novo synthesis of the mRNA rather than activation of a sequestered mRNA or superactivation of the protein.
...
PMID:Gene regulation during anaerobiosis in soya roots. 262 97

A sensitive immunocytochemical method for the localization of alcohol dehydrogenase (ADH) in the rat brain is described. The method employs rat liver ADH isolated and purified with Cap-Gapp affinity chromatography. Antiserum to rat liver ADH is generated in rabbits, and used in the peroxidase-antiperoxidase immunocytochemical method. The method is compatible with both light and electron microscopic methods of tissue preparation. In the present report we describe the identification of ADH in neurons of the mammillary bodies, periaqueductal gray, and the cerebral and cerebellar cortices of normal adult rats. In all brain tissues examined, the enzyme is limited to neuronal cytoplasm, and only to some neurons. The restriction of the enzyme to a limited percentage of neurons in the central nervous system may help to account for the difficulty in demonstrating the enzyme in whole brain homogenates, as the dilution of enzyme-bearing cytoplasm with a large volume of enzymatically inactive tissue would reduce the specific activity of the enzyme to near the limit of detectability. In the cerebellar cortex, the enzyme is found only in Purkinje cell cytoplasm. In the other regions examined, we are unable to identify by other criteria a specific neuronal class that consistently displays ADH reactivity. The reactive cells seem to be generally midrange in size and bipolar or multipolar in configuration. The presence of ADH in certain neurons leads us to speculate that intraneuronal ethanol metabolism may lead to focal accumulation of acetaldehyde. The intracellular presence of this toxin may in turn help to account for brain dysfunction in acute ethanol intoxication, and the neuropathology of chronic alcohol abuse.
...
PMID:Immunocytochemistry of alcohol dehydrogenase in the rat central nervous system. 269 Jun 54

We have previously reported the detection of a 37 kD liver protein-acetaldehyde adduct in rats fed alcohol chronically with the AIN'76 diet. It was surprising that only one liver protein-acetaldehyde adduct was found. In this report, we have tried to detect additional protein-acetaldehyde adducts by electroimmunotransblot with rabbit anti-hemocyanin-acetaldehyde adduct IgG and to further characterize the 37 kD liver protein-acetaldehyde adduct. Sensitivity of electroimmunotransblot increased 10- to 20-fold when alkaline phosphatase-linked antibody was used in place of horseradish peroxidase, but only one protein-acetaldehyde adduct band was detected in liver. Feeding rats the Lieber-DeCarli alcohol diet also did not produce more protein-acetaldehyde adduct bands in electroimmunotransblot. Addition of cyanamide, an aldehyde dehydrogenase inhibitor, to the AIN'76 alcohol diet greatly increased the intensity of the 37-kD protein-acetaldehyde adduct band on electroimmunotransblot but did not produce other bands. The 37 kD protein-acetaldehyde adduct decayed in vivo with a half-life of 4 days when alcohol was removed from the diet. The 37 kD protein-acetaldehyde adduct in liver is cytosolic. Its interaction with anti-hemocyanin-acetaldehyde adduct IgG was blocked by polylysine-acetaldehyde adduct and polytyrosine-acetaldehyde adduct. It could be removed by immunosorption with anti-hemocyanin-acetaldehyde adduct IgG-bound immunoresin. When immunoblotted with anti-alcohol dehydrogenase and anti-aldehyde dehydrogenase antibodies, the alcohol dehydrogenase and aldehyde dehydrogenase bands in liver of alcohol-fed rats showed identical intensities before and after immunosorption.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Further studies on the 37 kD liver protein-acetaldehyde adduct that forms in vivo during chronic alcohol ingestion. 280 59

We have previously shown that the rapid clearance of intravenously injected lactate dehydrogenase M4 from plasma is mainly due to endocytosis by macrophages in liver, spleen, and bone marrow. We have now studied endocytosis of lactate dehydrogenase M4 in detail, using freshly isolated rat liver macrophages (Kupffer cells) in vitro. 125I-lactate dehydrogenase M4 rapidly accumulated in the cells and was subsequently degraded to trichloroacetic acid-soluble material. Degradation was inhibited by leupeptin, an inhibitor of lysosomal proteases. Breakdown of the protein was also greatly diminished by treatment of the cells with chloroquine, a weak base which inhibits proteolysis by raising the pH in endosomes and lysosomes. High concentrations of chloroquine inhibited uptake. Lactate dehydrogenase M4 was not endocytosed by liver endothelial cells, although, under the same conditions, these cells were shown to accumulate horse radish peroxidase via a mannose-specific receptor. Uptake of lactate dehydrogenase M4 by Kupffer cells was strongly reduced after pretreatment of the cells with low concentrations of proteases. Endocytosis of lactate dehydrogenase M4 exhibited saturation kinetics (Km = 0.8 microM) and was competitively inhibited by mitochondrial and cytosolic malate dehydrogenase, alcohol dehydrogenase, adenylate kinase, and creatine kinase MM, enzymes which are rapidly cleared in vivo. Enzymes with long half-lives in plasma, namely lactate dehydrogenase H4, alanine aminotransferase, and cytosolic aspartate aminotransferase did not compete at concentrations up to 10 microM. Our results indicate that Kupffer cells contain a receptor that is involved in the clearance of lactate dehydrogenase M4 and a number of other tissue-derived enzymes from plasma. Uptake of lactate dehydrogenase M4 does not occur via a receptor that recognizes carbohydrate residues, for the enzyme is not a glycoprotein.
...
PMID:Receptor-mediated endocytosis of lactate dehydrogenase M4 by liver macrophages: a mechanism for elimination of enzymes from plasma. Evidence for competition by creatine kinase MM, adenylate kinase, malate, and alcohol dehydrogenase. 282 Sep 61

Plasma contains many enzymes that are probably derived from damaged cells. These enzymes are cleared at characteristic rates. We showed previously that in rats the rapid clearance of alcohol dehydrogenase, lactate dehydrogenase M4 and the mitochondrial and cytosolic isoenzymes of malate dehydrogenase is largely due to endocytosis by macrophages in liver, spleen and bone marrow. We now demonstrate that uptake of each of the enzymes by these tissues is in general decreased by simultaneous injection of a high dose of one of the other dehydrogenases or a high dose of adenylate kinase or creatine kinase. A similar dose of colloidal albumin did not significantly decrease uptake of the four dehydrogenases. Nor was uptake of colloidal albumin, apo-peroxidase from horseradish or multilamellar liposomes influenced by a high dose of mitochondrial malate dehydrogenase. These results indicate that the four dehydrogenases and the two kinases are specifically endocytosed via the same receptor. We suggest that this receptor contains a group, possibly a nucleotide, with affinity for the nucleotide-binding sites of the enzymes.
...
PMID:Several dehydrogenases and kinases compete for endocytosis from plasma by rat tissues. 299 34


1 2 3 4 5 6 7 Next >>

---