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)

The activities of several glycosidases (beta-galactosidase, beta-glucosidase, N-acetyl-beta-glucosaminidase) were demonstrated in human bile. The enzyme activities are increased about 100 times after exclusion of bile salts and other small molecular compounds by Sephadex G-50 gel filtration. The use of 4-methylumbelliferyl derivatives as substrates was useful as measurement of the bile enzyme activities are not altered in the presence of bile pigments. Enzyme characteristics of bile glycosidases were determined: pH optimum and isoelectric point. The bile glycosidase activities were also measured in various hepatobiliary disorders (cholelithiasis, cancer of gallbladder, acute hepatitis, liver cirrhosis and fatty liver). The glycosidase activities in bile from patients with liver diseases, as well as with cholelithiasis, were generally decreased. Isoelectric focusing patterns of biliary glycosidases were similar for specimens from patients with hepatobiliary disorders as compared to normal.
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PMID:Bile lysosomal enzymes: characteristics and pathological significance for various hepatobiliary disorders. 1 80

beta-Galactosidase and associated activities (beta-glucosidase and beta-fucosidase) have been studied in rabbit and bovine liver and rabbit spleen. The physico-chemical (optimal pH, pI, MW) and kinetical (Km, Vmax, Ki) properties were determined for all the activities. Two enzyme forms were separated in rabbit spleen. beta-Galactosidase, beta-fucosidase and beta-glucosidase activities were catalyzed by the same enzyme in rabbit and bovine liver. The enzyme from bovine liver showed nonlinear double-reciprocal plots, suggesting a substrate-activation model, and the presence of more than one binding site in the enzyme. The enzyme activities of several glycosidases were determined in human sera fom control groups and from patients with diabetes mellitus, pancreatitis, hepatitis, cirrhosis, stomach and breast cancer, myocardial infarction and renal failure. The results show significantly different enzyme levels for several glycosidases in all the studied diseases. Experimentally-induced diabetes mellitus, alcoholism and nephrotoxicity in rats showed different glycosidase levels in several tissues, as compared with control groups.
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PMID:[Glycosidases of mammals: association of activities and changes of levels in some disorders]. 681 36

Liver tissue cirrhosis, developed in rats after long-term administration of CCl4, led to distinct increase in activities of acid phosphatase, acid DNAase, cathepsin D, beta-galactosidase and beta-glucosidase. When the treatment with the hepatotropic toxins was stopped activity of lysosomal enzymes decreased slightly but was maintained at the high level. Within a day after a single administration of choriogonine distinct decrease as compared with the controls in activity of all the acid hydrolases studied was found. Within subsequent periods the lysosomal enzymes activity continued to decrease and within 2 months after the choriogonine treatment it was distinctly lower as compared with control animals.
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PMID:[Effect of choriogonine on the enzymatic activity of lysosomes in the cirrhotic liver in the rat]. 681 64

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

Diagnostic difficulties of Gaucher disease, a disorder resulted from a deficient activity of glucocerebrosidase is reported. Gaucher disease was described in the 16 year old male, 5 years after manifestation of the very first symptoms (fracture and osteomyelitis). At the age of 14, the cirrhosis due to viral hepatitis accompanied with splenomegaly was diagnosed. This findings was not associated with the earlier osseous disorders. Histopathologic examination of the removed spleen facilitate the diagnosis. The second case refers to 20 year old female. Clinical symptoms and additional test pointed to malignant neoplasm of thyroid, the reproductive organs or cancer of indistinguishable primary focus with metastases in the liver. Trepanobiopsy of bone marrow had made an accurate diagnosis possible, while determination of beta-glucosidase activity in peripheral white blood cells, chitotriosidase activity, and molecular investigations of gene specific to beta-glucocerebrosidase proved it.
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PMID:[Diagnostic difficulties in Gaucher disease: report of two cases]. 1033 43