Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023890 (cirrhosis)
 42,195 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

beta-Hexosaminidase (Hex) activity has been shown to be increased in the sera of patients with chronic liver diseases as well as in rats with CCl4-induced liver cirrhosis. In this study, serum and liver Hex activity was determined in rats during the acute phase of CCl4 poisoning, a widely used animal model of acute necrotic liver damage. The results showed a statistically significant decrease of Hex activity in the sera of rats 36 h after CCl4 poisoning (5.84 +/- 2.90 U/l), as compared to controls (11.58 +/- 1.35 U/l; p less than 0.001). No significant change was observed in liver tissue of CCl4-treated animals and controls. A significant correlation between the decrease in Hex and the increase in serum aspartate aminotransferase in serum was found. The results are consistent with the hypothesis that this lysosomal enzyme could be released by non-parenchymal liver cells, such as activated macrophages; its increased activity could be the expression of macrophage activation, as demonstrated in patients with chronic liver diseases.
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PMID:beta-Hexosaminidase activity in the acute phase of CCl4 poisoning in the rat. 215 17

beta-Hexosaminidase (Hex) activity was previously found to be increased in the sera of patients with liver cirrhosis, cholestasis and acute alcohol intoxication, as well as in rats with CCl4-induced liver cirrhosis. We studied this enzymatic activity in the sera and liver tissue of rats with alcoholic fatty liver due to prolonged alcohol intake and CCl4-induced liver fibrosis in association with moderate alterations in liver function tests. Serum and liver Hex activity did not show any significant change in both experimental models. These data suggest that Hex is not an alcohol-induced enzyme, and that severe, but not moderate, liver damage can determine the increase in this lysosomal enzymatic activity.
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PMID:Beta-hexosaminidase activity in alcoholic fatty liver and in CCl4-induced liver fibrosis of the rat. 257 5

Total serum bile acid levels and beta-hexosaminidase activity were studied in 22 normal subjects, 35 non-cirrhotic patients with acute alcohol intoxication, 45 patients with alcoholic liver cirrhosis and 11 patients with alcoholic liver cirrhosis and surgical portal-systemic shunts. Comparison was made with traditional liver function tests. beta-Hexosaminidase was most frequently elevated in acute alcohol intoxication (94%) while total serum bile acids were elevated in all patients with alcoholic liver cirrhosis. Total serum bile acid levels were found to discriminate most efficiently between acute alcohol intoxication and liver cirrhosis. The combined determination of serum beta-hexosaminidase and total serum bile acids is proposed for evaluating alcoholic liver disease.
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PMID:Total fasting serum bile acids and beta-hexosaminidase in alcoholic liver disease. 622 67

Homogenates of liver from cases of hepatic cirrhosis due to alpha 1-antitrypsin deficiency (PiZZ) alcoholism were analyzed for their content of various lysosomal enzymes. Also determined were the specific activities of lactate dehydrogenase, glutamate-oxaloacetate transaminase, glutamate-pyruvate transaminase, and creatine phosphokinase in the extracts of liver from cases of both kinds of hepatic cirrhosis: all of these activities were within the range of control values. Similarly, the specific activities of the following lysosomal hydrolases were unremarkable: acid phosphatase, beta-mannosidase, beta-fucosidase, beta-glucuronidase and beta-glucosidase. Hexosaminidase specific activity was increased twofold in livers from the cases of cirrhosis due to alpha 1-antitrypsin deficiency. The specific activity of alpha-mannosidase (measured at pH 4.5) in homogenates of livers from PiZZ individuals with cirrhosis and those with alcoholic cirrhosis was increased two- to four-fold. Chromatography of the high-speed supernatant fraction from homogenates of livers of cirrhotic and noncirrhotic individuals on columns of DEAE-cellulose resolved alpha-mannosidase activity into two components: under the conditions employed, acid pH optimum (pH 4.5) alpha-mannosidase did not bind to the resin, whereas intermediate pH optimum (pH 5.5) alpha-mannosidase could be eluted with 0.1 mol/l NaCl. Liver from one case of (PiZZ) alpha 1-antitrypsin deficiency and emphysema, without demonstrable cirrhosis, was found to contain normal levels of both acid alpha-mannosidase and intermediate alpha-mannosidase. However, cases of cirrhosis due to alpha 1-antitrypsin deficiency contained twice as much acid alpha-mannosidase and only one third to one fourth as much intermediate alpha-mannosidase as controls. The deficiency in hepatic intermediate alpha-mannosidase was also observed in 5 of 5 cases of alcoholic cirrhosis.
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PMID:Altered alpha-mannosidase isoenzymes in the liver in hepatic cirrhosis. 697 51