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)

No significant differences were found between C57BL/6 and BALB/c mice in the levels of Thy 1.2 antigen (a T-cell marker) or the activities of the T-cell maturation-related enzymes adenosine deaminase (ADA, EC 3.5.4.4), serine-esterase (SE, EC 3.4.21), N-acetyl-beta-D-glucosaminidase (NABG, EC 3.2.1.30) and beta-glucuronidase (BG, EC 3.1.1.1), in either unfractionated lymphoid cells or T-lymphocyte-enriched fractions. ADA, SE, NABG and BG activities were much higher (P < 0.01) in the calf than in the corresponding populations in mice. However, the distributions of these activities among thymocyte subpopulations were very similar in mice and the calf. These results provide indirect evidence to suggest that the course of T-cell maturation is similar in mice and the calf.
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PMID:Markers of T-cell differentiation and maturation in C57BL/6 and BALB/c mice and in the calf: a comparative study. 771 43

In this work we studied the effect of Prothymosin alpha (ProT alpha) and other thymic factors on the expression of Thy 1.2 antigen (a T-cell marker) and the activities of adenosine deaminase (ADA, E.C. 3.5.4.4), N-acetyl-beta-D-glucosaminidase (NABG, E.C. 3.2.1.30), beta-glucuronidase (BG, E.C. 3.1.1.1) and serine-esterase (SE, E.C. 3.4.21)., the levels of which change during the T-cell differentiation process among small thymocytes obtained from C57BL/6 mice. Incubation of small thymocytes in the presence of ProT alpha, Thymus Extracts (TE) or supernatants prepared from thymic stromal cells (TSCS) or thymocytes (TS) reduced the proportion of cells killed by anti-Thy 1.2 monoclonal antibodies but did not affect the enzymatic activities studied. This is the first evidence that ProT alpha affects Thy 1.2 expression in vitro.
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PMID:Prothymosin alpha and factors from calf thymic cells decrease expression of Thy 1.2 antigen among small thymocytes from C57BL/6 mice. 779 93

The health of the respiratory tracts of 19 horses was studied for 11 months. The horses were placed into 3 groups (healthy, periodically diseased and continuously diseased) based on the measurements of blood gases, intrapleural pressure and on neutrophil content of tracheal mucus. Lysosomal enzymes (N-acetyl-beta-D-glucosaminidase and beta-glucuronidase) and reflectors of the proteolytic system (plasmin, plasminogen, trypsin inhibitor capacity) were determined. beta-glucuronidase appeared to be a good indicator of the presence of disease of the respiratory system. High beta-glucuronidase values were seen in horses with elevated numbers of neutrophils, elevated arterial alveolar and intrapleural differences as well as in diseased horses during the stabling period. Trypsin inhibitor capacity seemed to be lower in the diseased respiratory system, probably due to the increased consumption of trypsin inhibitors.
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PMID:Beta-glucuronidase and trypsin inhibitor capacity of tracheal lavage fluid as indicators of seasonal airway irritation in the horse. 798 42

Alterations in the metabolic functions of trabecular meshwork (TM) cells are thought to be involved in the pathogenesis of primary open-angle glaucoma (POAG). In an investigation of this possibility, 30 trabeculectomy specimens from patients with POAG were examined histochemically for 11 lysosomal and membrane-bound enzymes. The patients ranged from 48 to 87 years in age. The degree of enzyme staining was compared with that of 15 age-matched controls obtained from an eye bank at less than 24 h after death. There was no history of eye disease in the controls. The enzymes examined were: dipeptidylpeptidases II and IV (DPPII and IV); beta-glucuronidase (beta-GLUC); acid-beta-galactosidase (s beta-GAL); N-acetyl-beta-D-glucosaminidase (NAG); nonspecific esterase (UE); acid phosphatase (SP); alkaline phosphatase (ALP); gamma-glutamyltransferase (GGT); and aminopeptidase A and M (APA and APM). Evaluation of the specimens was performed by two observers and by computer-aided optic densitometry. Results showed increased staining of SP, UE, GGT and APM in the pathological specimens as compared with the controls. SP and UE indicate phagocytic activity, APM is involved in collagen turnover and GGT participates in both drug detoxification and the breakdown of glutathione in the gamma-glutamyl cycle. Our observations show different hydrolase activities in the TM cells of human glaucomatous eyes as compared with normal values, suggesting that such metabolic differences may be related to the pathogenesis of POAG.
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PMID:Increased hydrolase activities in the human trabecular meshwork of glaucomatous eyes. 809 35

The distributions of the hydrolases acid and alkaline phosphatase (AP and ALP), N-acetyl-beta-D-glucosaminidase (NAG), beta-glucuronidase (beta-Gluc), beta-galactosidase (beta-Gal), non-specific esterase (UE), dipeptidylpeptidases II and IV (DPPII and DPPIV), aminopeptidases M and A (APM and APA), and gamma-glutamyltransferase (GGT) were investigated in the human, pig and Lewis rat normal anterior segment by histochemical methods. The distribution of the above hydrolases, particularly that of proteases, varied between ocular tissues and between the three species. Lysosomal hydrolases together with GGT and ALP were consistently active in the corneal epithelium, stroma and endothelium in all three species; the corneal distribution and activity of beta-Gal, APM, APA and DPPIV, however, displayed interspecies variation. The angular tissues showed similarities for most hydrolases with the exceptions of beta-Gal, UE, APM, APA and DPPIV. In all eyes examined strong ciliary epithelial activity for AP, beta-Gal, UE, GGT and ALP was observed in the pars plicata; only the pig eye also displayed strong DPPIV activity in this area. Regional differences in hydrolase distribution in the iris were observed in all species. A post-mortem freezing delay of longer than 24 h resulted in a decrease in hydrolase activity.
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PMID:Hydrolases of anterior segment tissues in the normal human, pig and rat eye: a comparative study. 818 69

The present investigation evaluated the changes in bronchoalveolar lavage fluid (BALF) biochemical constituents and indices of bronchoalveolar lavage cell functions to detect early lung injury in rats following intraperitoneal administration of cyclophosphamide (CP). Rats were exposed to a single intraperitoneal injection of CP (200 or 300 mg/kg body weight). Experimental and control rats were sacrificed at various time intervals (2, 3, 5, 7, 11, 21, and 42 days after cessation of exposure), and lung lavage was performed to examine several markers of lung injury. Biochemical analyses revealed dose-related increases in BALF angiotensin converting enzyme activity, total protein, lactate, lactate dehydrogenase, and N-acetyl-beta-D-glucosaminidase (NAG) levels on days 2, 3, 5, 7, and dose-related increases in albumin, alkaline phosphatase, acid phosphatase, and lipid peroxidation on days 2, 3, 5, 7, and 11 after CP treatment. In contrast, reduced levels of ascorbic acid and glutathione (GSH) content were observed in lung lavage fluid. We also examined bronchoalveolar lavage cells for acid hydrolases (acid phosphatase, beta-glucuronidase, NAG) and GSH content. Activity of acid hydrolases was slightly elevated on day 2 and peaked on days 3, 5, and 7. However, lavage cell GSH content was decreased. Thus, measurements of pulmonary changes by analyzing lavage fluid and lavage cell functions seems to be a useful marker for assessing the early onset and development of CP-induced lung injury.
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PMID:Cyclophosphamide induced early biochemical changes in lung lavage fluid and alterations in lavage cell function. 820 29

The distributions of the lysosomal enzymes [acid phosphatase (AP), N-acetyl-beta-D-glucosaminidase (NAG), beta-glucuronidase (beta-Gluc), beta-galactosidase (beta-Gal), dipeptidylpeptidase II (DPP II)] and of the membrane-bound proteases [aminopeptidase M (APM), aminopeptidase A (APA), gamma-glutamyltransferase (GGT), dipeptidylpeptidase IV (DPP IV)] were investigated in the normal human adult and foetal anterior segment by histochemical methods. The distribution of these hydrolases varied between ocular tissues. The most active enzymes in the adult corneal epithelium and endothelium were AP, beta-Gluc, NAG, beta-Gal and GGT; in the keratocytes, APM, APA, beta-Gluc and GGT predominated. The adult trabecular meshwork cells were stained by AP, beta-Gluc, NAG, APM, GGT, DPP II and DPP IV. The enzymes AP, beta-Gluc, APM and APA, however, displayed greater activity in the endothelium of Schlemm's canal. The adult ciliary epithelium stained strongly for all lysosomal hydrolases; GGT was the most active protease here. Differences in enzyme activity were noted in some tissues when foetal and adult anterior segments were compared. There appeared to be a decrease in the activity of some enzymes with age and post-mortem delay greater than 24 h. The function(s) of each enzyme and their possible roles in the respective tissues are discussed.
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PMID:Histochemical survey of the anterior segment of the normal human foetal and adult eye. 822 58

To explain the mechanism of renal injury caused by liver ischemia-reperfusion, we investigated biochemical and morphological changes in the liver and kidney in rats. After reperfusion following 60 min of liver ischemia, numerous changes were found. The level of serum transaminases and lipid peroxide formation in the liver tissue increased significantly. Electron microscopic studies revealed that most of the hepatocytes had swollen mitochondria and clumping of the nuclear chromatin. The sinusoidal endothelium was disrupted and the sinusoidal lumen was filled with numerous erythrocytes. Blood endotoxin concentration, plasma lipid peroxide levels, and serum beta-glucuronidase activities were significantly higher than in the control group. Biochemical and morphological renal injury was also observed. Tissue lipid peroxide levels increased in both the kidney and the liver. Microscopic examination revealed damage to the renal tubules, including interstitial edema, dilatation of the lumen, and granular casts derived from necrotic cells in the proximal convoluted tubule. The levels of urinary N-acetyl-beta-D-glucosaminidase (NAG) in the liver ischemia-reperfusion group were also higher than in the control group. These results suggest that the renal injury was caused by an increase in endotoxin, lipid peroxide, and lysosomal enzymes in the blood following the liver injury induced by the ischemia-reperfusion.
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PMID:Investigation of the renal injury caused by liver ischemia-reperfusion in rats. 824

Fourteen mature New Zealand white female rabbits had a right, cemented, tibial hemiarthroplasty using a stemmed, fluted, titanium alloy, condylar-type prosthesis. In one group (seven rabbits), polymethyl methacrylate (PMMA) was used to cement the prosthesis firmly. In a second group (seven rabbits), the prosthesis was treated with cement ex vivo; the prosthesis and cured cement were then implanted, and rotated once within the bone to ensure that the prosthesis was loose fitting. Roentgenograms performed postoperatively and at 3 months were graded for new (i.e., not present on the immediate postoperative radiograph) radiolucent lines. At 3 months, the tissue adjacent to the implant was harvested sterilely and cultured over a 3-day period; the tissues and culture supernatants were then assayed for total protein, DNA content, and lysosomal enzyme activity (N-acetyl-beta-D-glucosaminidase and beta-glucuronidase). The mean cumulative grading of new lucent lines was 0.4 +/- 0.3 (mean +/- standard error) for the well-fixed prosthetic group and 2.0 +/- 0.6 for the loose prosthetic group. The tissue surrounding loose prostheses contained more DNA and total protein, and produced greater amounts of lysosomal enzymes compared to well-fixed prostheses. The control left sides were not statistically different for any parameter analyzed. The increased DNA content demonstrates an increase in cellularity of the tissue surrounding loose prostheses. Normalization of the relative amount of enzyme released as a function of cellularity (DNA) suggests that the influx of cells into the area surrounding loose prostheses may be more important to the overall increase in lysosomal enzyme release than increased production of lysosomal enzymes by individual cells.
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PMID:Lysosomal enzyme production at the interface surrounding loose and well-fixed cemented tibial hemiarthroplasties in the rabbit knee. 829 69

The possibility of minimizing organ damage following cardiopulmonary bypass (CPB) was examined. In the control group, n = 21, upon completion of CPB, elevation of the lysosomal enzyme beta-glucuronidase, which is a sensitive indicator of cellular damage, was affected by the concentration of granulocyte elastase (r = 0.59) or the endothelial-derived constricting factor, endothelin, (r = 0.8). Renal damage, which was detected by an increase in renal tubular enzymes (N-acetyl-beta-D-glucosaminidase and gamma-glutamyltranspeptidase) in urine, was also affected by endothelin (r = 0.79, r = 0.56), elastase (r = 0.6, r = 0.71), and by free hemoglobin levels (r = 0.76, r = 0.82). Next, the efficacy of pharmacological intervention for the prevention of renal damage was evaluated. During CPB, the administration of an elastase inhibitor (ulinastatin, 3 x 10(5) IU), n = 8, or a calcium antagonist (nicaldipine HCl, elastase release inhibitor; 5 gamma/kg per min), n = 8, significantly reduced the elevation of beta-glucuronidase and renal tubular enzymes (p < 0.05). Although the ulinastatin and nicardipine groups demonstrated low values of elastase in the Intensive Care Unit (ICU), only the values of the nicardipine group reached statistical significance (p < 0.05). A reduction in endothelin levels compared to the control group was observed in the nicardipine group. However, preventive and counteractive effects of nicardipine against vasoconstriction caused by endothelin were also considered to play an important role in the prevention of renal damage. The addition of haptoglobin (4,000 IU) to the priming solution of the CPB also reduced levels of renal tubular enzymes (p < 0.05).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Pharmacological intervention for renal protection during cardiopulmonary bypass. 830


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