Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To evaluate the effects of acute pancreatitis on hepatic function and hepatic cellular and subcellular organellar fragility, we studied 1) the hepatic secretion of lysosomal enzymes (beta-glucuronidase, beta-galactosidase, and N-acetyl-beta-glucosaminidase) into bile in the isolated perfused rat liver model; 2) the aspartate aminotransferase (ASAT), alanine aminotransferase (ALAT), and lysosomal enzyme levels in the effluent in an isolated liver model; 3) hepatic lysosomal fragility in an in vitro incubation study; and 4) protective effects of a new low molecular weight synthetic protease inhibitor, ONO 3307, against hepatic injury in doses of 2 and 5 mg/kg.h in acute pancreatitis induced by a supramaximal dose of cerulein in rats. Decreased hepatic secretion of lysosomal enzymes into bile and accelerated hepatic lysosomal fragility were observed in acute pancreatitis induced by cerulein. ONO 3307 showed a significant protective effect against this hepatic injury in acute pancreatitis, the dose of 5 mg/kg.h showing a more potent effect than the dose of 2 mg/kg.h. These results suggest that the impaired hepatic function, including depressed hepatic secretion of lysosomal enzymes, seems to be closely related to accelerated hepatic fragility and that some unknown protease, which is present in pancreatitis and is susceptible to inhibition by ONO 3307, plays a crucial pathologic role in the development of this liver injury during acute pancreatitis.
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PMID:Effects of acute pancreatitis on hepatic secretion of lysosomal enzymes into bile and hepatic lysosomal fragility: protective effects of a new synthetic protease inhibitor, ONO 3307. 150 86

The effect of two exoglycosidases, beta-galactosidase and N-acetyl-beta-glucosaminidase (GlcNAc-ase) on chondrogenic expression of stage 19 mouse limb bud micromass cultures was investigated. Chondrogenic expression was monitored by Alcian blue staining and immunofluorescent localization of cartilage-specific proteoglycan and type II collagen. Chondrogenesis was inhibited by exposure to 0.1 U/ml beta-galactosidase or 0.025 U/ml GlcNAc-ase for 24 h or longer in culture. The effect of both enzymes was concentration and time dependent. Exoglycosidic hydrolysis of galactose or N-acetylglucosamine was substantiated by treatment with HRP-conjugated peanut agglutinin and succinylated wheat germ agglutinin, respectively. Cells treated with beta-galactosidase appeared to be flattened with a stellate morphology, whereas GlcNAc-ase-treated cells were bipolar forming ridge-like mounds that had a directional orientation. The antichondrogenic effect was not alleviated when the cells were induced to assume a spherical shape upon treatment with cytochalasin D. DNA measurements indicated that the lack of chondrogenic expression was not related to cell attachment or cell proliferation. These data support the hypothesis that the expression of specific terminal sugars on cell surface glycoconjugates of limb bud cells represents an important component of the chondrogenic process.
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PMID:Lack of chondrogenic expression in mouse limb bud micromass cultures exposed to exogenous beta galactosidase or N-acetyl-beta-glucosaminidase. 190 37

Four renal tubular enzymes, N-acetyl-beta-glucosaminidase, beta-galactosidase, angiotensin-converting enzyme and gamma-glutamyltransferase, were measured in the urine before, and 24 hours and 1 week after extracorporeal shock wave lithotripsy in 20 consecutive patients. Extracorporeal shock wave lithotripsy was performed on the Sonolith 2000 device with the patient under intravenous narcotic sedation with fentanyl. Enzymatic activity per gram of urinary creatinine was consistently but not significantly higher before extracorporeal shock wave lithotripsy than in control subjects. All 4 enzymes were elevated 24 hours after extracorporeal shock wave lithotripsy, with the increases in beta-galactosidase and angiotensin-converting enzyme being statistically significant. However, by 7 days after the procedure the enzymes had decreased to pre-procedure concentrations or below. These data suggest that any renal tubular damage induced by extracorporeal shock wave lithotripsy is of limited magnitude and brief duration.
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PMID:Absence of persisting parenchymal damage after extracorporeal shock wave lithotripsy as judged by excretion of renal tubular enzymes. 197 64

1. Tests for glycosidases were performed in homogenates of Brachionus plicatilis. 2. Hydrolytic activity was detected with the following substrates: (a) with synthetic substrates (NP = 4-nitrophenyl): NP-alpha- and NP-beta-D-glucopyranoside, NP-alpha- and NP-beta-D-galactopyranoside, NP-N-acetyl-beta-D-glucosaminide, NP-N-acetyl-beta-D-galactosaminide, NP-alpha- and NP-beta-D-mannopyranoside and NP-alpha-L-fucopyranoside; (b) with disaccharides: sucrose, maltose, trehalose, isomaltose, cellobiose, gentiobiose and lactose; (c) with polysaccharides: laminarine, carboxymethyl-cellulose, avicel, Micrococcus luteus (for lysozyme) and 4-nitrophenyl-alpha-D-maltoheptaoside (for amylase). 3. The pH dependence of the glycosidase activities was determined. 4. The distribution of enzyme activities within fractions from the homogenate was studied in order to localize them within the cell. 5. Proteins from Brachionus homogenate were separated by SDS-gel electrophoresis and the positions of the following glycosidase activities were detected by assays performed on the gels (estimated molecular weights in parentheses): alpha-glucosidase (250,000); beta-glucosidase (200,000); beta-galactosidase (70,000); N-acetyl-beta-glucosaminidase (60,000).
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PMID:Glycosidases in Brachionus plicatilis (Rotifera). 232 73

The acute effect of a physiological concentration (1 mU/l) of thyrotropin (TSH) on the activity of four lysosomal enzymes in the thyroid follicular lining cell has been studied by quantitative cytochemical techniques. N-acetyl-beta-glucosaminidase (NAG) activity was increased by 14% after 10 min TSH stimulation and NAG and beta-galactosidase activities were increased by 24% and 25% respectively (P less than 0.05) after 20 min stimulation and by 40% and 45% (P less than 0.05) respectively after 30 min stimulation with TSH, indicating an early processing of these carbohydrate residues in thyroglobulin. Acid phosphatase activity, an acid hydrolase unrelated to the hydrolysis of thyroglobulin, was unchanged 30 min after TSH stimulation. Leucyl-beta-naphthylaminidase (LNA) activity changed biphasically with peak activities of 7 and 25 min possibly representing an early fusion of endocytotic vesicles and lysosomes and later the release process of the thyroid hormones. The changes in LNA activity and thus membrane permeability were not reflected in the other enzyme activities studied. This may indicate that the TSH regulation of lysosomal enzyme activities could be independent to the endocytotic process, which is known to involve fusion of lysosomes and endocytotic vesicles. In conclusion we have demonstrated for the first time with physiological concentrations of TSH a specific acute regulation of some lysosomal enzyme activities which may be involved in thyroglobulin processing. Further, these effects may be independent of the changes in lysosomal membrane permeability due to formation of secondary lysosomes.
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PMID:Acute in vitro thyrotropin regulation of lysosomal enzyme activity in the thyroid follicular cell. 250 89

Urinary enzyme testing has been used by many investigators to diagnose and monitor various types of renal injury. Three urinary enzymes, N-acetyl-beta-glucosaminidase, beta-galactosidase and gamma-glutamyl transferase were monitored in 17 patients before and after a single, unilateral extracorporeal shock wave lithotripsy treatment. Stones were in the renal pelvis or calices except for 1 treated in situ in the proximal ureter. Urine specimens were collected before extracorporeal shock wave lithotripsy and at 1, 3, 5, 7, 10, 14, 21 and 28 days after treatment. N-acetyl-beta-glucosaminidase and beta-galactosidase levels increased significantly after treatment (p less than 0.05). Gamma-glutamyl transferase levels increased after treatment but this was not statistically significant. All enzyme levels were highest on days 1 and 3 after lithotripsy and returned to baseline by day 28. Factors associated with post-treatment enzyme elevation included female sex, a lower pre-treatment creatinine clearance and stone size greater than 1 cm. These findings indicate that there is a transient selective increase in urinary enzyme excretion after extracorporeal shock wave lithotripsy.
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PMID:Selective elevation of urinary enzyme levels after extracorporeal shock wave lithotripsy. 257 Jan 65

Male Sprague-Dawley rats were challenged with various hyperoxaluric agents including ammonium oxalate, hydroxy-L-proline, and ethylene glycol. All treatments resulted in increased urinary oxalate. Associated with hyperoxaluria was an increase in urinary levels of renal enzymes, gamma-glutamyl transpeptidase, N-acetyl-beta-glucosaminidase, and alkaline phosphatase. Most of the rats did not demonstrate any significant change in urinary levels of beta-galactosidase. There was a highly significant positive correlation between urinary oxalate and N-acetyl-beta-glucosaminidase.
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PMID:Urinary enzymes and calcium oxalate urolithiasis. 257 Jan 67

Adler and Martin (1983, Curr. Eye Res. 2, 359-66) found cathepsin D to be present in crude preparations of bovine interphotoreceptor matrix (IPM). The purpose of the present study was to determine, by investigating several acid hydrolases in purer IPM samples, whether hydrolytic enzymes abundant in RPE lysosomes were present also as normal components of the IPM. IPM was prepared from bovine eyes by the introduction of a small bleb of buffer between the neural retina and the RPE. These IPM samples were free from significant contamination by surrounding tissues; they contained IRBP as their only major protein, and had negligible amounts of lactate dehydrogenase and ROS-specific proteins. Most acid hydrolases were assayed fluorometrically by measuring the 4-methylumbelliferone released upon hydrolysis of appropriate derivatives; the substrate for cathepsin was hemoglobin. The amounts of the enzymes found in the IPM were far from uniform and could not be correlated with enzyme activities in either RPE or retina homogenates. The hydrolases in the IPM varied in amount from beta-galactosidase (28% of the RPE level), through N-acetyl-beta-glucosaminidase (20%), alpha-fucosidase (15%), beta-glucuronidase (12%), alpha-glucosidase (8%), cathepsin D (7%), alpha-mannosidase (7%), down to beta-glucosidase, acid phosphatase, and acid lipase (trace amounts, less than 1%). These results agree with the relative amounts of enzymes found by Wilcox (1987) to be secreted into the medium by cultured human RPE cells. Furthermore, the rank order of hydrolases in the IPM is the same as that for hydrolases secreted (but not recaptured) by human fibroblasts in I-cell disease. The conclusion from these correlations is that lysosomal enzymes are probably secreted, as a normal process, by the RPE into the IPM, where they may have a role in digesting shed outer segments and in catabolizing IPM components.
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PMID:Selective presence of acid hydrolases in the interphotoreceptor matrix. 261 85

Human intestinal bacteria were grown in a 3-stage continuous culture system on a medium containing complex polysaccharides and proteins as carbon and nitrogen sources. Selected bacterial populations were enumerated and glycosidase, protease and arylamidase activities measured. Comparison of arylamidase and glycosidase activities in the multichamber system (MCS) and faeces showed that the predominant faecal enzymes were also produced by bacteria growing in the MCS. After 48 d operation, porcine gastric mucin (5.8 g/d) was independently fed to vessel 1. Elevated levels of volatile fatty acid (VFA) formation showed that the glycoprotein was actively fermented. The increase in carbohydrate availability as a result of breakdown of the mucin oligosaccharides stimulated bacterial growth and activities. The enzymological measurements showed that mucin increased production of both cell-bound and extracellular glycosidases, such as beta-galactosidase, alpha-glucosidase and N-acetyl-beta-glucosaminidase. Protease activities were profoundly influenced by mucin. These were largely cell-bound in non-mucin cultures but were predominantly extracellular and collagenolytic when mucin was present. Experiments with protease inhibitors showed that cysteine proteases were the major cell-bound and extracellular enzymes in both mucin and non-mucin cultures, but that serine and metalloproteases were also present. The effect of mucin on arylamidase formation was less marked, although there was increased production of these enzymes in vessels 1 and 2 of the MCS. These results suggest that host-produced substances such as mucin glycoprotein may play a role in modulating the growth and activity of bacteria growing in the human large intestine.
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PMID:Influence of mucin on glycosidase, protease and arylamidase activities of human gut bacteria grown in a 3-stage continuous culture system. 266 79

Normal arterial foci which take up Evans blue dye (EBD) in vivo are believed to represent atherosclerosis-prone, hemodynamically stressed foci compared to areas which exclude dye. We have used the rabbit EBD model to examine focal aortic hydrolases of blue areas versus white areas, and we report herein significant focal variations of hydrolase activities. Enzymes measured included neutral alpha-glucosidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, acid alpha-glucosidase, beta-galactosidase, beta-glucuronidase, cathepsin C, and acid cholesteryl esterase (ACE); specific activities were expressed on the basis of tissue DNA. In correlative areas of EBD uptake in normal rabbit aortic arch, ACE activity averaged 17% higher and cathepsin C activity averaged 37% lower than activities of areas free of EBD in the descending thoracic aorta (P less than 0.02). None of the glycosidases studied differed significantly between blue and white aortic areas. These findings indicate that discrete, intrinsic differences of hydrolytic enzyme activities exist in the normal rabbit aorta in areas delineated by in vivo EBD uptake, areas recognized as lesion-prone vs lesion-resistant.
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PMID:Intrinsic focal variations of rabbit aortic hydrolase activities. 276 19


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