Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Twenty transformed lines have been isolated as a result of the germ line insertion of a 3.2 kb alcohol dehydrogenase (Adh) gene fragment into an Adh negative strain of Drosophila melanogaster by P element-mediated transformation. More than half of these lines exhibited abnormal ADH expression. The level of ADH expression ranges from zero in some lines to near normal levels in others, and the pattern of ADH expression in the larval gut is also abnormal in many of these lines. Each of the abnormal tissue-specific patterns is stable and characterized by the absence or reduction of ADH expression in certain tissues. High levels of ectopic expression were not observed. In two of these lines, the pattern of ADH staining is highly restricted: it is limited to the medial midgut in line MM-50, and to the gastric caecae and the proventriculus in line GC-1. In heterozygotes between these two lines ADH is expressed in both of these tissues. To test the hypothesis that this abnormal expression is due to position effects, inserts were mobilized to new locations. The mobilized inserts exhibited new patterns of tissue-specific expression associated with new cytological insert locations, showing that the abnormal expression in lines MM-50 and GC-1 is due to tissue-specific position effects and not to mutations. The results are discussed in the context of chromatin structure as a possible cause of these position effects.
 ...
PMID:Tissue-specific position effects on alcohol dehydrogenase expression in Drosophila melanogaster. 131 45

The use of monoclonal antibodies against Drosophila alcohol dehydrogenase (ADH) provides a powerful tool in the analysis of the tissue and temporal patterns of Adh gene expression. Immunocytochemical techniques at the light- and electron-microscopic levels have been used to determine the distribution of ADH in the ovarian follicles of D. melanogaster during oogenesis. In the early stages of oogenesis, small amounts of ADH are detectable in the cystocytes. At the beginning of vitellogenesis (S7), ADH appears to be located mainly in the nurse cells. From stage S9 onwards, the ADH protein is evenly distributed in the ooplasm until the later stages of oogenesis (S13-14), when multiple ADH-positive bodies of varying size appear in the ooplasm. This change in distribution is a result of the compartmentalization of the ADH protein within the glycogen yolk or beta-spheres. Yolk becomes enclosed within the lumen of the primitive gut during embryonic development, and thus our results suggest a mechanism for the transfer of maternally-inherited enzymes to the gut lumen via yolk spheres.
 ...
PMID:Progressive redistribution of alcohol dehydrogenase during vitellogenesis in Drosophila melanogaster: characterization of ADH-positive bodies in mature oocytes. 161 95

The enzyme alcohol dehydrogenase of Drosophila melanogaster is encoded by a single structural gene (Adh) with two promoters, distal and proximal (PD and PP). During development these two promoters are used differently: the major Adh transcript of larvae is from PP, the major transcript of adult flies is from PD. At a few discrete times in development transcription occurs simultaneously from both promoters. In situ hybridization has been used to investigate the spatial and temporal aspects of promoter activity at these stages of development. Maternally inherited Adh transcripts are not localized in the embryo; they decay very rapidly after fertilization. Zygotic expression of Adh RNA begins after germ-band retraction, 10.5 hr after fertilization. Expression is confined to the fat body, but occurs from both distal and proximal promoters. By 15 hr expression is first seen in the gut, from PP. By the same time fat body expression from PD has ceased, and transcription in this tissue is exclusively from PP for the next 4 days. The steady-state level of Adh transcript begins to decline at the end of larval development. There is then the transient accumulation of transcripts from PD, but predominantly in the larval fat body, rather than in the gut. These data illustrate a surprising complexity in the tissue and temporal regulation of Adh expression in D. melanogaster. Moreover, they show that transcripts from two different promoters of the same gene can, at certain well-defined stages of development, accumulate in the same cells.
 ...
PMID:Temporal and spatial utilization of the alcohol dehydrogenase gene promoters during the development of Drosophila melanogaster. 250 Nov 28

To elucidate the possible role of alcohol dehydrogenase in the generation of damages caused by alcohol abuse, it is important to know the exact localization of this enzyme. Anti-alcohol dehydrogenase antibodies were used to localize the enzyme in human gastrointestinal tissues. Alcohol dehydrogenase was detectable in the mucosa of all parts of the gastrointestinal tract. There is a notable decrease in the amount of alcohol dehydrogenase with increasing distance from the stomach. In the stomach, the reaction for alcohol dehydrogenase was strongest in the mucus-producing cells, moderate in the parietal cells, and weak in the chief cells. Throughout the gut, alcohol dehydrogenase was present in cells exposed to the lumen in amounts comparable to that of the parietal cells. Crypt cells and goblet cells were negative. The results strongly indicate that alcohol dehydrogenase is an intrinsic component of gastrointestinal epithelial cells.
 ...
PMID:Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract. 619 36

These studies report the existence of multiple forms of alcohol dehydrogenase in extracts of Drosophila mojavensis. The existence of these forms can be best explained by the hypothesis of a duplication for the Adh locus in D. mojavensis. Electrophoretic variants at each locus have been identified and crosses between individuals carrying alternative alleles at each locus result in F1 progeny with six bands of ADH. This pattern is consistent with these individuals being heterozygous at two loci. The loci have been named Adh-1 and Adh-2. Examination of the isozyme content during development shows that the two Adh genes are not coordinately controlled but have separate developmental programs. In embryos and first and second instar larvae only Adh-1 is expressed. At about the time of the second molt Adh-2 expression commences in some of the same cells that previously expressed and continue to express Adh-1. This is evidenced by the existence of an interlocus heterodimer in third instar larvae. Both genes are expressed throughout pupation. Shortly after emergence Adh-1 expression declines. In mature males only ADH-2 is present. In mature females both Adh-1 and Adh-2 are expressed but not in the same cells since the interlocus heterodimer is absent. Examination of specific tissues reveals that most of the larval ADH is found in fat body cells and as in most tissues of third instar larvae both Adh-1 and Adh-2 are expressed. The single exception appears to be larval gut which contains ADH-1 but little if any ADH-2. In mature males and female flies all ADH containing tissues have only ADH-2. However, mature ovaries contain substantial quantities of ADH-1 which is apparently deposited into eggs. Given the extensive amount of available information on the Adh gene-enzyme system of D. melanogaster and the tools that can be applied to the analysis of homologous systems, the ADH duplication of D. mojavensis, and its regulation may be a useful one for studying differential gene regulation in specific cell types.
 ...
PMID:Differential regulation of duplicate alcohol dehydrogenase genes in Drosophila mojavensis. 633 97

Alcohol dehydrogenase (ADH; EC 1.1.1.1) activity in Xenopus laevis was highest in liver tissue, with decreasing activities in kidney, heart, and gut tissues, respectively. Essentially no activity was found among other tissues screened, including lung, ovary, eye, and testes. Also, there was no apparent sexual dimorphism of ADH activity in either liver or kidney tissue. All ADH isozymes were inhibited by 10 mM pyrazole, and no eye-specific retinol dehydrogenase activity was detected on starch gel electropherograms. Isozyme patterns from 418 offspring from 11 different crosses could be explained genetically assuming the presence of two structural genes coding for ADH production: one carrying two electrophoretically separable variants and the other showing quantitative variation in its expression. The ADH system in X. laevis should be useful for studies concerning the molecular mechanisms governing the expression of ADH activity in vertebrate development.
 ...
PMID:Alcohol dehydrogenase isozymes in the clawed frog, Xenopus laevis. 636 54

The effects of vasoactive intestinal polypeptide (VIP) on several enzymes of glycogen metabolism in rat hepatocytes were compared with those of glucagon and of vasopressin (ADH). VIP caused phosphorylase activation and glycogenolysis in hepatocytes from fed rats. In hepatocytes from fasted rats incubated with glucose, lactate, and pyruvate, VIP inhibited net glycogen deposition, inactivated glycogen synthase, and activated phosphorylase. VIP was about 100-fold less potent than glucagon and 1,000-fold less potent than ADH in causing activation of phosphorylase. The ability of VIP to activate phosphorylase was not altered by chelation of the calcium in the medium. The half maximal effective doses of VIP for both phosphorylase activation and stimulation of glycogenolysis were 10-30 nM. Treatment with VIP, ADH, or glucagon did not decrease phosphorylase phosphatase activity. Each of these hormones, however, lengthened the lag time before synthase phosphatase activity was expressed in vitro. Other gut hormones tested did not affect hepatocyte glycogen metabolism. These results do not support the concept of physiologic control of hepatic glycogen metabolism by VIP or by other gut hormones.
 ...
PMID:Effect of vasoactive intestinal polypeptide on glycogen metabolism in rat hepatocytes. 680 98

Metabolic acidosis and hypopotassemia after whole gut irrigation (WGI) with 0.9% sodium chloride are probably caused by the following effects: 1. Sodium, chloride and fluid resorption with following renal compensatory mechanisms and inhibition of the ADH incretion and the renin-angiotensin-aldosterone System--2. Washing-out effect of the intestinal mucosa with loss of potassium-rich intestinal juice and protein. At the beginning of anaesthesia, 20 h after WGI, compensatory mechanisms did not reach a reconstitution of the balanced initial situation. Therefore, patients whose state is critical should be monitored carefully during WGI. Further investigations will develop an indifferent irrigation fluid to avoid serious complications of massive water resorption during WGI.
 ...
PMID:[Changes in water-electrolyte balance after orthograde intestinal irrigation]. 729 9

The Adh-1 gene product, ADH-A2, the only known murine class I alcohol dehydrogenase, is able to oxidize retinol (vitamin A) into retinaldehyde, the first enzymatic step in the conversion of retinol into its biologically active metabolite retinoic acid. We have investigated the developmental expression pattern of Adh-1 transcripts by in situ hybridization. Transcripts were first detected by embryonic day 10.5 in the mesonephros mesenchyme. During the following gestational days, Adh-1 transcripts were detected in several mesenchymal areas, such as nasal, laterocervical, and genital regions. Adh-1 transcripts were also detected in a small ectodermal domain at the anterior margins of both forelimbs and hindlimbs. During late fetal development. Adh-1 transcripts were found essentially in the epidermis and in a number of tissues which continue to express the gene after birth, such as liver, kidney, gut epithelium, adrenal cortex, testis interstitium, and ovarian stroma. In contrast, a strong expression of Adh-1 was found in the mesenchyme of developing lungs, but not in the adult organ. This highly regulated expression of Adh-1 is discussed with respect to the local synthesis of retinoic acid during development. Although the promoter of the human counterpart of Adh-1 contains a retinoic acid response element (Duester et al. [1991] Mol. Cell. Biol. 11:1638-1646), we report that this element is not conserved in the murine gene. Consistently, Adh-1 promoter-containing reporter constructs were not retinoic acid-inducible in cotransfections assays with RARs and/or RXRs, suggesting that retinoic acid regulation of Adh-1 differs from that of the human gene.
 ...
PMID:Stage and tissue-specific expression of the alcohol dehydrogenase 1 (Adh-1) gene during mouse development. 801 87

The midgut of Drosophila melanogaster is a site of alcohol dehydrogenase (ADH) activity, the enzyme that catalyzes the first step in the major pathway for ethanol degradation. The effects of different levels of dietary ethanol on the ultrastructures of the guts of larvae of the Canton-S wild-type strain and the ADH-deficient, Adhn2, strain were ascertained. In wild-type larvae fed an ethanol-free, defined medium, the foregut epithelium was characterized by few glycogen rosettes and sparse microvilli that protruded into the gut's thick lumen lining. The midgut epithelium was typical of cells involved in absorption and active transport with abundant microvilli on the apical surface and membrane infoldings on the basal surface. In place of microvilli, the apical surface of the hindgut had membrane infoldings. The apical surfaces of both the mid- and hindgut epithelium were covered by a thick, electron-dense peritrophic membrane consisting of chitin. In both strains the subcellular damage that was correlated with ethanol levels in the diet was confined to the midgut and hindgut regions. Damage to gut cells in the form of disrupted mitochondria, dilated rough endoplasmic reticulum, low densities of glycogen rosettes and protein granules, high numbers of autophagic vacuoles, and the presence of myelin whirls was extensive in Canton-S strain larvae fed a high ethanol diet. A low dietary concentration of ethanol induced changes in gut ultrastructure of Adhn2 larvae similar to the changes that were observed in wild-type larvae fed the higher ethanol concentrations, but the basal infoldings were more dilated in the Adhn2 larvae. At high dietary concentrations the disruption of mid- and hindgut cells by ethanol appeared great enough to interfere with the digestion and absorption of nutrients.
 ...
PMID:At high dietary levels ethanol alters the structure of mid- and hindgut epithelial cells of Drosophila melanogaster larvae. 827 Aug 92


1 2 3 4 Next >>