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:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We examined specific activities (based on DNA) of six glycosidases and cathepsin C in aorta, kidney, and liver from male rats of 2, 6, 10, and 14 months of age. The premise was that assessing cellular catabolism of arterial and nonvascular tissues over age might more fully clarify the impact of age (and growth) alone upon vascular wall metabolism. All aortic glycosidases increased significantly (P less than 0.05) over the holding period as follows: neutral alpha-glucosidase, up 93%; beta-galactosidase, up 102%; N-acetyl-beta-glucosaminidase, up 119%; alpha-mannosidase, up 77%; beta-glucuronidase, up 65%; acid alpha-glucosidase, up 95%. Cathepsin C specific activity was unchanged as was aortic DNA content; total protein content increased 136%. In the kidney, all glycosidase specific activities declined over age with decreases ranging 39-55%; cathepsin C was unchanged. In the liver, neutral alpha-glucosidase increased 12%, acid alpha-glucosidase was unchanged, and the four remaining glycosidases decreased an average of 5-35% by 14 months of age. Liver cathepsin C decreased 44% over this period. Thus, enhancement of hydrolase baseline activities prevails during growth and aging in rat aortic tissue whereas hydrolases of kidney and liver tissues generally decline.
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PMID:Hydrolase activities increase in the rat aorta with growth and aging but not in liver and kidney. 309 18

Oligosaccharides of a non-oligomannoside type were released from porcine alpha-mannosidase by hydrazinolysis, and were fractionated into at least 15 homogeneous oligosaccharides. Most of them are oligosaccharides with galactose and N-acetylglucosamine residues attached to a common core, alpha Man2 beta Man beta GlcNAc(+/- alpha-L-Fuc)beta GlcNAc. About 50% of the oligosaccharides contain one or two outer chains composed of one beta-linked N-acetylglucosamine and two beta-linked galactose residues attached to the core portions, and the others seem to be metabolic intermediates. Based on the results of studies on the binding of alpha-mannosidase to RCA (Ricinus communis agglutinin) I-agarose and MBP (mannan-binding protein)-Sepharose, which are specific for glycoproteins possessing N-acetyllactosamine-type and oligomannoside-type (including oligomannosides with N-acetylglucosamine at the reducing termini) oligosaccharides, respectively, about 85% of the enzyme molecules were found to have both types of oligosaccharides. Similarly, it was shown that of the several acid hydrolases present in the lysosomes purified from rat liver, only alpha-mannosidase has both types of oligosaccharides, and the greater parts of beta-glucuronidase, acid phosphatase and beta-N-acetylhexosaminidase seem to have only oligomannoside-type oligosaccharides.
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PMID:Structures of galactose-containing oligosaccharides of alpha-mannosidase from porcine kidney. 309 80

The intracellular and extracellular distribution of acid hydrolases in cultured retinal pigmented epithelium (RPE) was studied. Incubation of cultured RPE in medium containing 20 mM mannose-6-phosphate resulted in the extracellular release of approximately 15% of the cell-associated activity of several acid hydrolases. This represents an approximate 120% increase over control levels after 24 hr of culture with 20 mM mannose-6-phosphate. The extracellular release is not due to cell lysis, since no release of the cytoplasmic marker lactate dehydrogenase was seen. n-Acetyl-beta-glucosaminidase, alpha-mannosidase, and beta-glucuronidase were released into the extracellular medium, while acid phosphatase and beta-glucosidase were not. The release was specific for mannose-6-phosphate, and was dose-dependent. Inhibition of protein synthesis by treatment of RPE cells with cycloheximide (100 micrograms/ml) inhibited extracellular acid hydrolase release. RPE cells exhibited n-Acetyl-beta-glucosaminidase bound to the cell surface via a mannose-6-phosphate sensitive receptor. These results demonstrate a specific extracellular release of acid hydrolases by RPE and the presence of at least one acid hydrolase on the RPE cell surface. This may represent a mechanism for control of cell surface and extracellular levels of these enzymes in RPE via the mannose-6-phosphate receptor.
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PMID:Extracellular release of acid hydrolases from cultured retinal pigmented epithelium. 310 Apr 74

Seven glycosidases (beta-N-acetylglucosaminidase, alpha-fucosidase, beta-galactosidase, acid alpha-glucosidase, beta-glucuronidase, acid and neutral alpha-mannosidase) were analysed in seminal plasma from the first and second successive ejaculates in normal Ayrshire bulls. In comparison to our previous data the results indicate that beta-N-acetylglucosaminidase, beta-galactosidase and beta-glucuronidase are derived mainly from epididymal secretions, while alpha-fucosidase and particularly neutral alpha-mannosidase originate additionally from the spermatozoan cytoplasmic droplets. The seminal vesicles appear to contribute particularly to the seminal plasma acid alpha-glucosidase and acid alpha-mannosidase activities. The seminal plasma enzymes derived from the epididymis and cytoplasmic droplets were suppressed in semen samples with low sperm density or with high numbers of abnormal spermatozoa. The epididymal and seminal vesicle enzymes could be utilized in assessment of the secretory/functional capacity of these glands.
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PMID:Comparison of glycosidase levels in bovine seminal plasma. 311 30

The activities of a number of lysosomal hydrolases were determined in sera from 100 patients with cystic fibrosis (CF), age 2-35 yr, and age-matched controls: beta-hexosaminidase activity was significantly elevated (p less than 0.005) in CF patients from all age groups. alpha-Mannosidase activity was increased only in the older CF patients (greater than 13 yr). The following enzyme activities were not altered in CF serum: alpha-fucosidase, beta-glucuronidase and acid phosphatase. The abnormal patterns of serum alpha-mannosidase and beta-hexosaminidase in CF cannot be explained by pancreatic disease or undernutrition, since serum values of these hydrolases in patients with anorexia nervosa or acute pancreatitis were not altered. However, the altered activities of the alpha-mannosidase and beta-hexosaminidase were proportional to the degree of pulmonary insufficiency in the CF group, indicating that these changes are probably a secondary consequence of the primary disease process. Except for beta-hexosaminidase, because differences in the serum hydrolases in CF do not become apparent until the second decade of life, determinations of lysosomal enzyme activities in serum will probably be of little diagnostic value.
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PMID:Serum lysosomal hydrolases in cystic fibrosis. 316 78

The effect of culture conditions on the ultrastructure and enzyme activities of cultured skin fibroblast cells relevant to the diagnosis of lysosomal storage disorders are reported. The parameters examined were: pH of the culture media, type of media, increasing cell passage, and day of harvest. Ultrastructural changes were defined in terms of the number of lysosome-like inclusion bodies per cell according to a method devised in our laboratory and proven reliable in the detection of affected individuals. Our biochemical results included determination of enzyme activities of beta-hexosaminidase, alpha-mannosidase, beta-glucuronidase-lysosomal enzymes, arylsulfatase C, a microsomal marker, and 5' nucleotidase, a plasma membrane marker. Our results indicate that the cellular ultrastructure is more sensitive than enzyme activity to changes in culture conditions. The resulting ultrastructural "artifacts" observed under certain conditions were severe enough to result in a mistaken diagnosis. Due to certain difficulties we had previously encountered in heterozygote cultures (for lysosomal storage disorders) of amniotic cells, we decided to examine heterozygote cultures of skin fibroblasts. From these (preliminary) studies it seems that an elevation in the pH over the physiologic levels in the culture media may help to define between normal individuals and affected heterozygotes. On the basis of our results, we recommend that to minimize false positive ultrastructural results for the diagnosis of lysosomal storage disorders, cultures be grown in minimal essential medium, the pH of the medium carefully monitored to remain below 7.4, examining the cultures not later than cell Passage 8 and no later than Day 10 after subculture.
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PMID:Culture conditions found to minimize false positive diagnosis of lysosomal storage disorders. 320 85

A panel of 42 rodent x cat somatic cell hybrids has been used to assign seven structural genes for lysosomal enzymes to specific chromosomes in the domestic cat. The assignments include alpha-glucosidase (GANAB) to chromosome D1, alpha-galactosidase (GLA) to the X chromosome, beta-galactosidase 1 (GLB1) to chromosome B3, beta-glucuronidase (GUSB) to chromosome E3, alpha-mannosidase A (MANA) to chromosome B3, alpha-L-fucosidase (FUCA) to chromosome C1, and hexosaminidase A (HEXA) to chromosome B3. In all cases, the feline lysosomal enzyme genes were located in linkage groups which were syntenic with their homologous positions in the human gene map. These assignments expand the genetic map of the cat and reaffirm the extensive syntenic homology between the chromosome maps of man and cat.
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PMID:Chromosomal mapping of lysosomal enzyme structural genes in the domestic cat. 322 Apr 74

In Creutzfeldt-Jakob disease (CJD), there are prominent ultrastructural alterations of the plasma membrane, which contains many glycolipids and glycoproteins. Glycosidases can degrade glycolipids and glycoproteins. Gangliosides, a subset of glycolipids, are decreased in amount at the terminal stages of CJD, and CJD infectivity is closely associated with membrane rich fractions. We therefore studied 10 glycosidases, and found a statistically significant increase in beta-xylosidase, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activities in CJD. In contrast, alpha-glucosidase, beta-glucosidase, alpha-galactosidase, alpha-mannosidase, alpha-fucosidase, and beta-galactosidase were not significantly changed. The above results are consistent with degenerative membrane changes observed morphologically, and with increased degradation of sugar residues on lipids and/or proteins. These changes may be effected by the accumulation of the CJD agent in cell membranes. We suggest that the higher activities of these enzymes in CJD may be partially responsible for some of the structural and biochemical alterations in CJD infected brains.
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PMID:Cerebral glycosidases in experimental Creutzfeldt-Jakob disease. 328 70

Systemic release of lysosomal enzymes and local release in the pulmonary microcirculation from sequestrated and activated leucocytes could be an important factor in the development of the lung microvascular injury seen after septicaemia. The maximal activities of 11 lysosomal acid hydrolases (acid phosphatase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, alpha-mannosidase, beta-acetylglucosaminidase, beta-glucuronidase, arylamidase and cathepsins B and C) were measured in serum and lung lymph from seven sheep before and after infusion of live E. coli bacteria. In the early phase of septicaemia (the first hour) the activities of eight enzymes were increased in serum and/or lung lymph (1.1 to 2X pre-infusion values). In the late phase, 3-4 h after sepsis, there were significantly elevated serum activities of beta-glucosidase (5.4X), alpha- and beta-galactosidases (2.7X, 1.5X), beta-acetylglucosaminidase (2.0X) arylamidase (1.2X) and cathespin B (1.7X). In lymph acid phosphatase (1.7X), alpha- and beta-glucosidases (1.6X, 6.4X), alpha- and beta-galactosidases (2.1X, 1.7X). Beta-acetylglucosaminidase (2.6X), and beta-glucuronidase (4.0X pre-infusion) were elevated. The findings of a heterogenicity of changes in serum and lymph activities, as well as the large molecular sizes of some of the enzymes with changed activities indicated to us that permeability changes were not major causes of increased lymph enzyme activities. The results could indicate a local release of enzymes either from sequestrated leucocytes or lung tissue due to local reactions in the lung or lung microvessels. The heterogenous changes in activities for the various lysosomal enzymes as found in the present study indicated that measurement of only one enzyme could be misleading.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lysosomal enzyme pattern in lung lymph and blood during E. coli sepsis in sheep. 329 74

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98


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