Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Compared to values obtained in healthy normotensive control subjects, the serum activity of the lysosomal enzymes N-acetyl-beta-D-glucosaminidase (NAG) and beta-glucuronidase, was found to be elevated in patients with mild or borderline hypertension. The serum activity of the cytosolic enzyme lactate dehydrogenase was the same in the two groups. Serum NAG activity in hypertension was inversely correlated with glomerular filtration rate and renal plasma flow. Because of the greater variability of beta-glucuronidase activity, there were no such correlations between the serum levels of this enzyme and the measurements of renal function.
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PMID:Increased serum glycosidase activity in human hypertension. 653 99

Two populations of acid hydrolase-containing particles were distinguished in homogenates of rat epididymis. One of them was rich in acid phosphatase activity, equilibrated at density 1.17 in a sucrose gradient, and it sedimented between 12,000g 2.5 min and 43,000g 60 min (light particles). The other was poor in acid phosphatase activity and rich in N-acetyl-beta-D-glucosaminidase, arylsulphatase, and beta-glucuronidase activity, equilibrated at density 1.20 in a sucrose gradient and it sedimented between 400g 2.5 min and 12,000g 2.5 min (heavy particles). 131I-albumin (RISA) injected into the lumen of the cauda was partially recovered in subcellular particles of homogenates of this region. These particles, incubated at pH 5, were able to digest the engulfed RISA. The subcellular distribution of RISA-containing particles and RISA-digesting particles was similar to that of the heavy hydrolase-containing particles. This suggests that these latter are engaged, at least in part, in heterophagic processes.
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PMID:Two populations of acid hydrolase-containing particles in rat epididymis. 661 99

Occurrence of a renal failure in an infected patient may be referred to various causes: infection, renal toxicity of drugs (for instance aminoglycosides), shock . . . Determination of some urinary enzymatic activities might be helpful in unravelling the mechanism involved in such cases. Therefore a prospective study of the specificity of some urinary enzymatic activities was performed. The whole LDH activity, the LDH isoenzyme 5 (LDH 5), and two lysosomal enzymes, N-acetyl-beta-D-glucosaminidase (NAG) and beta-glucuronidase (beta-GLU) were dosed systematically, in several groups of patients: I (n = 34): healthy control, with normal renal function; II (n = 24): renal impairment, without recent upper urinary-tract infection (UTI) or aminoglycoside treatment; III (n = 27): upper UTI without aminoglycoside treatment, IV (n = 22): patients treated with aminoglycosides (without upper UTI); V (n = 16): upper UTI treated with aminoglycosides. Results showed a rather good specificity of whole LDH and LDH 5 for infectious kidney damage, and of NAG for tubular injury due to aminoglycoside treatments. Values of urinary beta-glucuronidase varied over a wide range; they were little increased in group III, without a great discriminative value. No significant difference was noted between group I and group II, for any enzyme whatever.
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PMID:[Value of the assay of 4 urinary enzyme activities in the diagnosis of the infectious or toxic (aminoglycosides) origin of a renal disease. Preliminary results]. 666 49

Activity of acid phosphatase, beta-glucuronidase and N-acetyl-beta-D-glucosaminidase in peripheral blood neutrophils of 30 women with breast cancer has been studied by means of semiquantitative cytochemical methods. In comparison to 20 healthy women the patients showed an increased activity of acid phosphatase and beta-glucuronidase whereas that of N-acetyl-beta-D-glucosaminidase was significantly lowered. It has been suggested that observed intracellular enzymatic deficiency is of importance with regard to lowered antitumor activity of neutrophils. Analogous deficiency of N-acetyl-beta-D-glucosaminidase within the neutrophils has previously been observed by the authors in women with malignant tumors of reproductive organs.
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PMID:Lysosomal enzymes of neutrophils in women with breast cancer. 666 9

We have studied the regeneration of adenosine triphosphate (ATP) in the glycolytic pathway in platelets with a 75% reduction in hexokinase (HK) activity and have investigated aggregation and Ca2+ secretion. HK-deficient platelets had a normal glycolytic flux in the resting state, but responded insufficiently to stimulation with thrombin (5 U/ml). In contrast, glycogen contents and glycogenolysis were normal. When the metabolic adenine nucleotides were labeled with 14C-adenine, the patient's platelets showed a normal adenylate energy charge and a normal level of 14C-ATP. However, the inhibitor of mitochondrial energy generation, CN-, induced a weaker fall in 14C-ATP in the patient's platelets than in the controls. Analysis of secretion markers revealed decreased amounts of granule-bound ATP and secretable Ca2+, whereas granule-bound adenosine diphosphate (ADP), beta-thromboglobulin, N-acetyl-beta-D-glucosaminidase, and beta-glucuronidase were within the normal range. Aggregation and Ca2+ secretion induced by 5 U/ml thrombin were normal and were not changed in the presence of inhibitors of mitochondrial and glycogenolytic energy generation. Aggregation was also normal at 0.1 U/ml thrombin and was independent of these inhibitors, but Ca2+ secretion was greatly impaired when mitochondrial and glycogenolytic ATP resynthesis was abolished. These findings indicate that a severe reduction in HK activity causes insufficient acceleration of the glycolytic flux during stimulation with thrombin. This leads to impaired dense granule secretion in conditions where secretion depends on concurrent ATP resynthesis and glycolysis is rate limiting.
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PMID:Platelet functions and energy metabolism in a patient with hexokinase deficiency. 668 46

The lysosomal enzymes beta-glucuronidase (EC 3.2.1.31) and N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30) were estimated by biochemical and cytochemical means in the circulating lymphocytes of 20 control subjects, 19 cases of B cell and one case of T cell chronic lymphocytic leukaemia. Significantly lower levels of activity were observed both biochemically and cytochemically for each enzyme in B cell chronic lymphocytic leukaemia lymphocytes, whereas the values obtained for the T cell chronic lymphocytic leukaemic patient fell within the normal range. The absence of staining reaction for both enzymes in the majority of B cell chronic lymphocytic leukemia lymphocytes contrasted with the uniform pattern of polar positivity obtained in T cell chronic lymphocytic leukaemia lymphocytes.
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PMID:An estimation of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase activity in normal and chronic lymphocytic leukaemia lymphocytes. 677 47

The catalytic activities of 4 glycosidases (hyaluronate-4-glycanohydrolase (EC 3.2.1.35), beta-N-acetyl-D-glucosaminidase (EC 3.2.1.30), beta-glucuronidase (EC 3.2.1.31), alpha-L-iduronidase (EC 3.2.1.76)), of the arylsulphatases A and B (EC 3.1.6.1) and of the protease cathepsin D (EC 3.4.23.5) were measured in extracts from hepatocytes and non-parenchymal cells and in serum during the development of thioacetamide-induced rat liver fibrosis (22 weeks). In non-parenchymal liver cells the catalytic activities of beta-N-acetyl-D-glucosaminidase, beta-glucuronidase, alpha-L-iduronidase and cathepsin D were increased significantly during chronic liver damage, but that of hyaluronate-4-glycanohydrolase was reduced by 40 to 65% during the period of application of thioacetamide. The catalytic activities of the arylsulphatases were lowered by 65% compared to control values in the 12th week but with advancing liver damage the catalytic activities returned to nearly normal values. Parenchymal cells of rats, which had been liver-damaged for 6 months, contained strongly elevated activities of beta-glucuronidase, beta-N-acetyl-D-glucosaminidase, arylsulphatases A and B, and cathepsin D but only slightly increased activities of hyaluronate-4-glycanohydrolase and alpha-L-iduronidase, respectively. In the serum of liver-damaged rats the activity of alpha-L-iduronidase was strongly elevated, while that of N-acetyl-beta-D-glucosaminidase was only slightly increased. The activities of beta-glucuronidase and of arylsulphatases A and B were decreased during the whole period of treatment. The catalytic functions of hyaluronate-4-glycanohydrolase and of cathepsin D, respectively, were decreased initially, but both enzyme activities were elevated during the more advanced stages of long term thioacetamide treatment.
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PMID:Changes in the catalytic activities of proteoglycan-degrading lysosomal enzymes in parenchymal and non-parenchymal liver cells and in serum during the development of experimental liver fibrosis. 687 76

The furosemide-induced increase in protein excretion, and its relations to 1) the size of protein molecules as reflected by three enzymes, and 2) glomerular filtration rate (GFR), plasma renin activity (PRA) and prostaglandin (PG) E2 and F2 alpha excretions were studied in 14 outpatients with normal renal function and 13 healthy males. Furosemide (120 mg) was given intravenously, and thereafter the protein excretion and the above parameters were monitored for 1--2 hours. In both groups, furosemide caused a transient increase in protein excretion. The excretion of the largest molecule, beta-glucuronidase, rose to 6.3-fold, while those of N-acetyl-beta-D-glucosaminidase and of the smallest molecule, alpha-amylase, increased by 91 and 37%, respectively. GFR increased, too, but markedly less than the protein excretion. PGE2 and PGF2 alpha excretions increased more than GFR and changed simultaneously with the excretion of proteins. Furosemide also caused a marked increase in PRA. This lasted, however, much longer than the rise in PG and protein excretion or GFR. The results suggest that the furosemide-induced increase in protein excretion is 1) related to the molecular size of proteins, 2) partly due to the rise in GFR, 3) simultaneous with the change in PG excretion. Our findings also agree with the view that furosemide causes changes in glomerular permeability.
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PMID:Increased urinary protein excretion after intravenous injection of furosemide in man. 700 92

Estimation of activity of five hydrolytic enzymes was made in foru histologically different types of human meningiomas derived from surgery. The hydrolytic enzymes examined in 13 tumors included four lysosomal enzymes: beta-glucuronidase, N-acetyl-beta-D-glucosaminidase (hexosaminidase), beta-galactosidase, and acid phosphatase. The fifth enzyme studied was alkaline phosphatase. The one papillary-type meningioma examined appeared to contain generally greater activities of the lysosomal enzymes than the other tumor types. Alkaline phosphatase was decidedly greater in transitional type meningiomas. The correlation of histological types with alkaline phosphatase activity is discussed with regard to previous observations.
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PMID:Hydrolytic enzymes in meningiomal subtypes. 735 74

The activities of five hydrolytic enzymes (acid and alkaline phosphatase, hexosaminidase [N-acetyl-beta-D-glucosaminidase], beta-galactosidase, and beta-glucorinidase) were measured in reconstituted homogenates of lyophilized human brain tissue and primary and metastatic tumors. The linearity of reaction, with respect to incubation time, and optimal pH of each enzyme and in tumor tissues were comparable to those in normal brain tissue. Total enzyme activities of hexosaminidase, beta-glucuronidase, and beta-galactosidase were significantly higher in tumors than in normal cerebral white matter. The ratio of hexosaminidase activity to beta-glucuronidase activity was significantly lower for metastatic than for primary tumors or normal white matter. When histological observations do not clearly establish if a brain tumor is primary or metastatic, this ratio may help. Alteration of hydrolytic enzyme activities as demonstrated here may be indicative of "ket enzymes" that are essential for maintaining the metabolic advantages of tumors.
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PMID:Hydrolytic enzyme activities of the nervous system. 738 65


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