Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019158 (hepatitis)
 30,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The serum activity of alcohol dehydrogenase was determined in healthy controls and in patients with liver diseases. The mean activity in hepatoma (6.4 +/- 1.0U/L) was significantly higher (P less than 0.05) than the mean values in liver cirrhosis (2.7 +/- 0.5U/L); hepatitis (4.3 +/- 1.0U/L), obstructive jaundice (2.9 +/- 0.5U/L) and healthy controls (0.7 +/- 0.1U/L). Alcohol dehydrogenase purified by CM-cellulose chromatography from the sera of patients with hepatoma had a higher affinity for butanol long chain saturated and unsaturated alcohols than the purified enzyme from healthy controls. Similarly, hepatoma alcohol dehydrogenase oxidized ethanol very poorly (KM = 154 microM) when compared with that from healthy controls (KM = 40.2 microM). Hepatoma alcohol dehydrogenase was inhibited by pyrazole while those of other liver diseases and the healthy controls were not. These properties of serum alcohol dehydrogenase may prove useful in the early diagnosis of hepatoma since biochemical changes occur before morphological changes in the development of cancer.
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PMID:Properties of serum alcohol dehydrogenase in Nigerians with primary hepatoma. 166 17

Alcohol is the most significant liver poison. Its degradation takes above all place by the alcohol dehydrogenase and the microsomal alcohol-oxidizing system. In the first step of degradation acetaldehyde develops which in enrichment evokes immediately toxic defects on the mitochondrias of the cells of the liver parenchyma and thus introduces a vicious circle. Furthermore, an increased affection of pharmacometabolites as a sequel of the alcohol-conditioned enzyme induction may lead to a defect. Alcohol influences intermediary metabolic functions: the gluconeogenesis is inhibited, multi-layer disturbances in the lipid metabolism lead to fatty degeneration of the liver. A hyperuricaemia results from overproduction in the liver as well as from decreased renal excretion. The proline formation is increased. Distinct increase of the gamma-GT-activity is an early and relatively specific indicator of the alcoholic liver defect. Morphologic and clinical manifestations are fatty degeneration of the liver, hepatitis based on fatty degeneration of the liver and cirrhosis. Apart from dose and duration of the alcohol intake additional factors require consideration. The author adopts a definite attitude to etiopathogeneis and therapeutic possibilities.
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PMID:[Alcohol and the liver]. 611 57

Ethanol is easily absorbed from the intestine and diffuses quickly throughout body water. The bulk of ethanol is metabolized in the liver, where alcohol dehydrogenase, a complex mixture of isoenzymes, oxidizes ethanol to acetaldehyde. Ethanol abuse produces functional and structural changes in the gastrointestinal tract, such as in the stomach, small intestine, liver, and pancreas. Accumulating evidence suggests direct toxicity of ethanol and possibly of acetaldehyde. Fatty liver, alcoholic hepatitis, liver cirrhosis, acute and chronic gastritis, deranged structure and function of the small intestine, acute and chronic pancreatitis, and pancreatic lithiasis are some of the sequelae of ethanol abuse. Recent investigations have enhanced our understanding of the functional and structural changes of the gastrointestinal tract produced by the abuse of ethanol.
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PMID:Ethanol, the liver, and the gastrointestinal tract. 719 92

The Long-Evans Cinnamon (LEC) rat is a mutant strain established from Long-Evans rats. LEC rats display hereditary hepatitis and spontaneous hepatocellular carcinoma (HCC). We first tried to examine effects of ethanol consumption on the development of HCC, and fed a Lieber's liquid diet containing 5% ethanol to LEC rats. However the rats died within 2 weeks because of acute alcohol intoxication. In LEC rats, the concentration of ethanol and acetaldehyde in blood was significantly higher, and liver alcohol dehydrogenase activity was slightly lower and acetaldehyde dehydrogenase activities were remarkably suppressed compared to those of Wistar rats. These results suggest that LEC rats have hereditary deficiencies of ethanol and acetaldehyde metabolizing enzymes.
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PMID:Abnormal ethanol metabolism in Long-Evans Cinnamon rats, a mutant strain developing spontaneous hepatoma. 800 22

The Long-Evans Cinnamon (LEC) rat is a mutant strain established from Long-Evans rats that displays spontaneous hepatitis and liver cancer. We previously demonstrated that LEC rats died of acute ethanol intoxication after being fed a liquid diet containing 5% ethanol. Furthermore, we found that both alcohol dehydrogenase (ADH) and aldehyde dehydrogenase activities were remarkably suppressed in the liver of LEC rat, compared with Wistar rats. In the present study, we further investigated ethanol metabolism in the non-ADH pathway and what caused the decrease of liver ADH activity in LEC rats. Blood ethanol concentration 5 hr after intraperitoneal administration of ethanol in LEC rats was higher than in the Wistar rats, indicating that ethanol oxidation was impaired in LEC rats. The expression of liver cytochrome P-450IIE1 in the LEC rat was as much as that in Wistar rats. Regarding decreased ADH activity in the liver of LEC rats, we examined an alternating purine-pyrimidine (CA) repeat-length polymorphism in the first intron of a class I ADH gene that would play a role in altering ADH activity. A polymerase chain reaction method was used to amplify the CA repeat in the first intron of this class I ADH gene, a nine CA repeat insertion and a point mutation were detected in LEC rats. These results suggest that this alternating sequence would modify transcription of the class I ADH gene in LEC rats. Thus, LEC rats have abnormal ethanol metabolism in the ADH pathway.
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PMID:Analysis of CA repeats in first intron of class I ADH gene in Long-Evans Cinnamon rats developing fatal intoxication after ethanol intake. 865 85

The effect of ethanol on cells infected with mouse hepatitis virus (MHV) was investigated. After MHV infection of competent cells, NCTC1469, ethanol was added to the culture at various concentrations, and the viability of cells was measured using 3-(4,5-dimethylthiazol-2yl)-2,5-diphenyltetrazolium bromide. To examine the possible involvement of the ethanol metabolite, acetaldehyde, alcohol dehydrogenase activity was measured in NCTC1469 cells. Ethanol alone did not show cytotoxicity against NCTC1469 cells at concentrations from 0.125% to 2%. After infection with MHV, the viability of cells decreased, and this decrease was further enhanced, dose-dependently, by the addition of ethanol. The activity of alcohol dehydrogenase in the cells was below the detectable level. The same phenomena were also demonstrated in cells infected with influenza virus and Herpes simplex virus. These results demonstrate that ethanol enhances MHV-mediated cytotoxicity; this exacerbation of cytotoxicity by ethanol is suggested to be an effect common to cytopathic virus-infected cells.
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PMID:Effect of ethanol on mouse hepatitis virus-induced cytotoxicity. 888 34

The activities of classes I and II alcohol dehydrogenase isoenzymes were determined in the sera of patients with toxic hepatitis using class-specific fluorogenic substrates. The activities of total alcohol dehydrogenase and enzymes indicative of liver damage were also measured. We found a statistically significant increase of class I alcohol dehydrogenase isoenzymes. The increase in class I (two-fold) was similar to the increase of alkaline phosphatase. In a correlated study, we observed a good correlation of the activity of class II isoenzymes with alanine aminotransferase. The total alcohol dehydrogenase activity was enhanced and correlated with lactate dehydrogenase. These results demonstrated that the alcohol dehydrogenase and class I isoenzymes are indicatory enzymes of liver cell damage, and may be diagnostically useful in toxic hepatitis.
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PMID:Serum activities of classes I and II alcohol dehydrogenases in toxic liver damage. 956 31

Groups of patients suffering alcoholism and narcomania were examined for the effect of intoxication on the blood serum enzymes of mainly liver origin: alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), aspartate aminotransferase (AST), alanine aminotransferase (ALT), as well as on thymol test. It has been shown that in patients with the first stage of alcoholism one could observe only functional disturbances in the liver: the increase of ADH activity which evidences for the induction of its synthesis. In patients with the first stage of opium narcomania one can record total hyperenzymenia, decrease of de-Rimis coefficient at the expense of more considerable increase of ALT activity than that of AST, as well as the sharp increase of thymol test--these are the signs of destructive and metabolic disturbances in the liver. In patients with the second stage of alcoholism one can observe the decrease of ALDH activity under the increase of ADH, AST, ALT activity and high thymol test-these are the signs of toxical hepatitis. Destructive and metabolic changes increase in the liver in the patients with the second stage of narcomania.
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PMID:[Comparative analysis of the effects of alcoholism and opium addiction on liver function]. 1139 20

Western blot experiments showed that sera from mice infected with the mouse hepatitis virus strain A59 (MHV-A59) contained autoantibodies (autoAb) that bound to a 40-kDa protein present in liver and kidney extracts. No reaction was observed with extracts of the heart, muscles, spleen, brain and lung. The Ab cross-reacted with a 40-kDa protein from human, rat and sheep liver, but not with liver extracts from the silver side fish (Odontesthes bonariensis). No correlation was found between the development of the hypergammaglobulinemia that followed the viral infection and the occurrence of the autoAb. Reactive immunoglobulins pertained to the IgG1, IgG2a and IgG2b subclasses, recognized cryptic epitopes and were detected from 10 days up to 8 weeks after MHV-infection. The 40-kDa protein was purified from mouse liver extracts by ion-exchange chromatography, gel filtration and SDS-PAGE. Because the N-terminal was blocked, we digested the protein in-gel with trypsin and sequenced various peptides. Results indicated a 100% homology of sequence between the protein recognized by the autoAb and liver fumarylacetoacetate hydrolase (FAH), the enzyme that mediates the last step of tyrosine catabolism. Additionally, a second protein recognized by the autoAb was detected during FAH purification steps and was identified as liver alcohol dehydrogenase.
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PMID:Identification of two liver proteins recognized by autoantibodies elicited in mice infected with mouse hepatitis virus A59. 1146 1

Possible molecular mechanisms underlying changes in catalytical properties of alcohol dehydrogenase (ADH) and lactate dehydrogenase (LDH) were studied at toxic hepatitis. The development of toxic hepatitis is accompanied by significant changes in the activity of ADH and LDH assayed in subcellular fractions and kinetic characteristics of these enzymes. This can result in an increase cellular level of acetylaldehyde and lactate which promotes the development of liver cirrhosis.
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PMID:[Molecular mechanisms of metabolic adaptation in pathological changed liver during toxic hepatitis ]. 1155 17


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