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

Twelve acid hydrolases, 4 near-neutral hydrolases, and alkaline phosphatase were demonstrated in 0.34 M sucrose homogenates of Trypanosoma cruzi strain Y: p-nitrophenylphosphatase and alpha-naphthylphosphatase, with optimum pH at approximately 6.0; alpha=ga;actpsodase. beta=ga;actpsodase. beta=g;icpsodase, N-acetyl-beta-glucosaminidase, cathepsin A and peptidase I and III, with optimum pH between 5.0 and 6.0; and arylsulfatase, cathepsin D, alpha-arabinase and alpha-mannosidase with optimum pH at approximately 4.0. alpha-Glucosidase, glucose-6-phosphatase and peptidase II had optimum pH at approximately 7.0. beta-Glycerophosphatase had a broad pH-activity curve from 4,0 to 7.4, with maximum activity at pH 7.0. The main kinetic characteristics of these enzymes and their quantitative assay methods were studied. No activity was detected for alpha-fucosidase, beta-xylosidase, beta-glucuronidase, elaidate esterase, acid lipase, and alkaline phosphodiesterase.
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PMID:Acid and neutral hydrolases in Trypanosoma cruzi. Characterization and assay. 4 19

For human mammary and ovarian carcinomas and transplantation tumours of rats clear hints found for an enzymatic-lytic effects of infiltrating tumour cells as a premise of the invasive tumour growth. In contrast in malignant melanomas there is no functional sign for a specific enzymatic-lytic effect of the living tumour cells to the surrounding tissue. In the mamma carinomas and ovarian carcinomas infiltratively growing tumour districts were characterized by an increased activity of the NADH-D, LDH, G-6-P-DH, IDH, MDH, SPase, UE, LAP and beta-GD. The transplantation tumours showed a high number of tumour cells with a high leucine amino-peptidase- and beta-glucuronidase-activity in a middle zone that was localized under the tumour edge district. The increased activity of the LAP and beta-GD found in the infiltration zone of the tumours is considered as an demonstration of a strong proteolytic activity of the tumour cells. The findings are discussed in the aspect of the invasive tumour growth.
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PMID:[Histochemical and ultrastructural investigations on invasive growth of tumour. I. Enzyme-histochemical investigations (author's transl)]. 40 21

Histochemical and ultrastructural investigation of the prostate in baboons treated parenterally with saline revealed that the epithelial cells in the caudal prostatic lobe possess very high acid phosphatase activity, moderate nonspecific esterase activity and alkaline phosphatase activity, and little or no amino-peptidase or beta-glucuronidase activity. Only a few lipofuscin granules were found. Ultrastructurally, the epithelial cells had a characteristic polar appearance with a supranuclear zone dominated by large secretory vacuoles. Secretory granules were abundant in the apical zone. No clear difference was found between the cranial and the caudal prostate except that the acid phosphatase activity of the epithelial cells was much lower in the former. In baboons treated with estraumustine phosphate, diethylstilbestrol diphosphate, or with flutamide, i.e., drugs used in the treatment of advanced prostatic carcinoma, the epithelial cells in the caudal prostatic lobe showed a varying degree of atrophy, which was least in the flutamide-treated animals. The histologic changes were accompanied by only minor changes in the enzyme activities, but the number of histochemically demonstrable lipofuscin granules were substantially increased, a finding confirmed by electron microscopy. The drugs did not notably affect the cranial prostate. The findings showed that the caudal, but not the cranial, lobe of the prostate of the baboon resembles the human prostate and can be affected by drugs known to have a desirable effect on the carcinomatous human prostate.
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PMID:Histochemical and ultrastructural study of prostatic tissue from baboons treated with antiprostatic drugs. 82 25

Unicameral bone cyst fluid possesses N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, PZ-peptidase, cathepsin D, acid phosphatase, N-acetyl-beta-D galactosaminidase, and beta-galactosidase activities. The activities of lysosomal enzymes in the cyst fluid are, as a rule, higher than in the serum, whereas the total protein content is lower. The content of collagen degradation products in the cyst fluid is higher compared to the serum. In bone cavity wall tissues, the collagen content is decreased. Adenosine 3':5'-cyclic phosphate and cyclic guanosine 3,5'-monophosphate accumulate in the cyst cavity. However, in some cases, there is no correlation among the activities of lysosomal enzymes in the cyst fluid, blood serum, and cyst wall tissues. The ratios of lysosomal enzyme activities in the cyst fluid differ from those in the cyst wall tissues, cultured skin fibroblasts, and blood polymorphonuclear leucocytes. The lack of coincidence of enzymatic spectra of the cyst fluid, wall tissues, and serum is suggestive of the diversity of ways of lysosomal enzyme enter the cyst cavity, i.e., blood, cyst fluid cells, and cyst cavity walls. The cysts with different locations (i.e., active and latent cysts) have similar lysosomal lytic potentials. The presence in the cyst cavity of extracellular lysosomal enzymes and collagen degradation products testifies to the permanent corrosion of the cyst cavity walls from the inside as well as to the increase in the osmotic pressure of the cyst fluid. Lysosome destruction should be regarded as an important pathogenetic factor that requires surgical or pharmacologic correction or both in the course of bone cyst management.
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PMID:The role of lysosomes in the pathogenesis of unicameral bone cysts. 185 Mar 36

Endothelial injury has been proposed as a feature of a wide variety of vascular diseases, and release of endothelial lysosomal hydrolases could contribute to the pathological changes seen. We have determined the relative activities of 14 glycosidases, two esterases and four peptide hydrolases in human umbilical vein endothelial cells and investigated whether known agonists of endothelial function, or materials known to modulate hydrolase secretion in other phagocytic cells, influenced the activity or secretion of these enzymes by human umbilical vein endothelial cells. Hexosaminidase, beta-galactosidase, beta-glucuronidase and alpha-iduronidase accounted for most of the measured glycosidase activity. Acid phosphatase activity greatly exceeded arylsulphatase activity, and most of the measured peptidase activity was due to acid peptidases. Optimum pH and apparent Km values were determined for the most abundant hydrolases. Exposure of human umbilical vein endothelial cells to bradykinin, thrombin or interleukin-1 resulted in negligible release of either hexosaminidase or lactate dehydrogenase (LDH), in contrast to phorbol myristate acetate, which caused a parallel, dose-dependent release of both enzymes. Treatment of these cells with calcium ionophore A23187, trypsin or platelet-activating factor, caused less than 10% release of either hexosaminidase or LDH. Agents known to modulate lysosomal enzyme secretion by other phagocytic cells failed to induce selective secretion of lysosomal enzymes by human umbilical vein endothelial cells.
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PMID:Lysosomal hydrolases of human vascular cells: response to agonists of endothelial function. 264 39

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

Circulating non-T lymphocytes had higher activities of 5'nucleotidase (plasma membrane), neutral alpha-glucosidase (endoplasmic reticulum) and basal leucine amino-peptidase than did T lymphocytes. Activities of catalase (peroxisomes), malate dehydrogenase (mitochondria), lactate dehydrogenase (cytosol) and N-acetyl-beta-glucosaminidase, beta-glucuronidase and acid phosphatase (lysosomes), were similar in the lymphocyte subfractions. Lymphocyte 5'nucleotidase (plasma membrane) in patients with common variable hypogammaglobulinaemia is much lower than normal. However, the decrease is less marked in X-linked hypogammaglobulinaemia, chronic lymphatic leukaemia or protein loosing enteropathy or in lymphocytes isolated from cord blood. Cells from patients with nephrotic syndrome had normal levels of 5'nucleotidase. Other plasma membrane marker enzymes (gamma-glutamyl transferase, leucine amino-peptidase) were normal in lymphocytes from patients with common variable hypogammaglobulinaemia. There is a selective reduction of mitochondrial (malate dehydrogenase) and cytosolic (lactate dehydrogenase) enzymes, with normal activities of lysosomal, peroxisomal and endoplasmic reticulum enzymes, in patients with common variable hypogammaglobulinaemia. The lymphocyte subcellular organelles in normal subjects and patients with common variable hypogammaglobulinaemia have similar properties on sucrose density gradient centrifugation. It is suggested that lymphocytes from patients with common variable hypogammaglobulinaemia show a specific enzymopathy and that this is not simply a reflection of cellular immaturity.
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PMID:Lymphocyte enzyme activities in immunodeficiency syndromes with particular reference to common variable hypogammaglobulinaemia. 630 45

Human synovial fluid often contains small cartilaginous "wear particles." Previous in vitro experiments have indicated the potential involvement of these particles in the pathophysiology of arthritis. To determine whether this potential is realized under the conditions existing within joints, standard suspensions of lapine articular cartilage were injected intraarticularly into the knee joints of rabbits. Thrice-weekly injections of 1 mg allogenic cartilage produced an inflammatory arthritis, accompanied by a marked cellular effusion, in all rabbits within 5 months. The synovium became hyperplastic, discolored, and infiltrated with mononuclear inflammatory cells. Embedded particles of the injected material were seen in histologic preparations of these synovia. Organ cultures of such synovia produced 4 to 5 times more collagenase, plasminogen activator, "Pz-peptidase," neutral and acid azocaseinase, and beta-glucuronidase than did cultures of synovia from control knees injected with saline. Furthermore, the articular cartilage of knees injected with cartilaginous particles showed elevated intrinsic collagenolytic activity. Histologic examination of the articular cartilage revealed an attendant loss of metachromasy, resulting in friability, pitting, and discoloring of the cartilage. Preliminary immunoassays failed to demonstrate a systemic immune response to the injected material.
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PMID:Experimental arthritis induced by intraarticular injection of allogenic cartilaginous particles into rabbit knees. 632 Aug 35

1. Activities of dipeptidyl aminopeptidases (DAP), leucine arylamidase and beta-glucuronidase were assayed in red and white parts of mouse quandriceps femoris muscle 3 and 7 days after a single bout of prolonged running. 2. The activities of lysosomal acid hydrolases (DAP I, DAP II and beta-glucuronidase) were highly increased on the 3rd day after the exertion and then decreased by the 7th day. The response was more prominent in red than in white skeletal muscle. 3. The activities of two microsomal hydrolases, DAP IV and leucine arylamidase, increased much less than those of the lysosomal acid hydrolases. The highest activities were recorded on the 7th day after exertion. 4. The activity of DAP III, a cytoplasmic peptidase, was unaffected in red muscle but slightly increased in white muscle. 5. The protein content of red skeletal muscle, but not that of white muscle, decreased transiently after the running. 6. It seems that strenuous exercise selectively stimulates the lysosomal proteolytic system in skeletal muscle, while the others are less affected.
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PMID:Changes of dipeptidyl aminopeptidase activities in mouse skeletal muscle following prolonged running. 703 82

XCP1 is a xylem-specific papain-like cysteine peptidase in Arabidopsis. To determine whether XCP1 could be involved in tracheary element autolysis, promoter activity and localization of XCP1 were investigated using XCP1 promoter-beta-glucuronidase fusions and immunofluorescence confocal microscopy. A tracheary element expression pattern was detected for XCP1. Results from confocal microscopy and biochemical subcellular fractionation indicated that XCP1 was localized in the vacuole. Ectopic expression of XCP1 resulted in a reduction in plant size in some lines and early leaf senescence, as indicated by early loss of leaf chlorophyll. Reduced plant size was correlated with higher levels of XCP1, as shown by immunoblot and peptidase activity gel analyses. The XCP1 prodomain exhibits exceptionally high similarity (greater than 80%) to the prodomains of papain and other papain-like enzymes isolated from papaya (Carica papaya) laticifers when compared with all other reported papain-like enzymes. The potential for XCP1 and papain to perform common functions as catalysts of autolytic processing following cell death due to programmed suicide or to wounding is discussed.
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PMID:The Arabidopsis xylem peptidase XCP1 is a tracheary element vacuolar protein that may be a papain ortholog. 1178 55


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