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)

beta-Glucuronidase (GUS) has become an important enzyme model for the genetic study of molecular disease, enzyme realization, and therapy, and for the biogenesis and function of the lysosome and lysosomal enzymes. The genetics of human beta-glucuronidase was investigated utilizing 188 primary man-mouse and man-chinese hamster somatic cell hybrids segregating human chromosomes. Cell hybrids were derived from 16 different fusion experiments involving cells from ten different and unrelated individuals and six different rodent cell lines. The genetic relationship of GUS to 28 enzyme markers representing 19 linkage groups was determined, and chromosome studies on selected cell hybrids were performed. The evidence indicates that the beta-glucuronidase gene is assigned to chromosome 7 in man. Comparative linkage data in man and mouse indicate that the structural gene GUS is located in a region on chromosome 7 that has remained conserved during evolution. Involvement of other chromosomes whose genes may be important in the final expression of GUS was not observed. A tetrameric structure of human beta-glucuronidase was demonstrated by the formation of three heteropolymers migrating between the human and mouse molecular forms in chromosome 7 positive cell hybrids. Linkage of GUS to other lysosomal enzyme genes was investigated. beta-Hexosaminidase (HEXB) was assigned to chromosome 5; acid phosphatase2 (ACP2) and esterase A4 (ES-A4) were assigned to chromosome 11; HEXA was not linked to GUS; and alpha-galactosidase (alpha-GAL) was localized on the X chromosome. These assignments are consistent with previous reports. Evidence was not obtained for a cluster of lysosomal enzyme structural genes. In demonstrating that GUS was not assigned to chromosome 9 utilizing an X/9 translocation segregating in cell hybrids, the gene coding for human adenylate kinase1 was confirmed to be located on chromosome 9.
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PMID:Human beta-glucuronidase: assignment of the structural gene to chromosome 7 using somatic cell hybrids. 55 90

The pH optima and apparent Km and Vmax values were determined for nine glycosidases of the retinal pigment epithelium (RPE) of the calf. In terms of micromoles of substrate cleaved per milligram protein per hour, the following relative order of enzymatic activities was observed: beta-N-acetylglucosaminidase greater than alpha-glucosidase = beta-N-acetylgalactosaminidase greater than alpha-mannosidase greater than beta-galactosidase greater than beta-glucosidase greater than alpha-fucosidase greater than alpha-galactosidase greater than beta-glucuronidase. The pH optimum of each of these enzymes was in the acidic range (below pH 6). All these findings refer to enzymatic activities of bovine RPE preparations obtained by the brushing procedure of Glocklin and Potts and washing as described by Berman and Feeney. Thus they may relate to those activities associated with particulate components of the RPE cell and not to the more soluble glycosidases. The distribution of the glycosidases between the washes of the cells and the final pellet of bovine RPE cells was examined. The activities of 10 glycosidases in the RPE of the embryonic chick were also examined. Neither beta-mannosidase nor beta-fucosidase activities could be detected in washed bovine RPE cells, although beta-mannosidase was detected in RPE of the embryonic chick. The presence of isoenzymes of beta-glucuronidase in bovine RPE was indicated. Specificity by beta-glucuronidase of bovine RPE for synthetic substrates was observed.
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PMID:Glycosidases of the retinal pigment epithelium. 70 Sep 67

The activities of four lysosomal enzymes and creatinine levels were measured in the plasma and urine of 17 healthy elderly and 7 young adults. Fractional enzyme excretion (FE ENZ) values for beta-hexosaminidase (N-acetylglucosaminidase), alpha-galactosidase, beta-galactosidase and beta-glucuronidase were calculated and compared between the two groups of subjects. FE ENZ was calculated as the ratio of enzyme clearance to creatinine clearance. The FE ENZ values for alpha-galactosidase, beta-galactosidase and beta-glucuronidase between the elderly and young populations were not statistically different; however, relative to the young control group, the FE ENZ value for beta-hexosaminidase was elevated approximately 2-fold in the elderly population (P = 0.06). The mean urinary alpha-galactosidase activity for the elderly population, when expressed on the basis of creatinine, was 50% lower than that of the control group (P = 0.03), whereas the mean urinary beta-hexosaminidase activity for the elderly was significantly higher compared to the control group (P = 0.008). When data for all subjects was analyzed, no correlation was observed between the urinary excretion of beta-hexosaminidase or alpha-galactosidase and glomerular filtration rate. These data indicate that with advancing age there are changes in the tubular secretion or reabsorption of selective lysosomal enzymes, particularly beta-hexosaminidase and alpha-galactosidase. These biochemical changes may provide a means of assessing subtle progressive deterioration of renal function.
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PMID:Comparison of urinary excretion of four lysosomal hydrolases in healthy elderly and young adults. 133 Mar 76

Several lysosomal enzymes present in human plasma (N-acetyl-beta-glucosaminidase, beta-glucuronidase, beta-galactosidase, alpha-galactosidase, alpha-L-fucosidase, alpha-mannosidase, beta-glucosidase) were maintained in a fully active state for at least 8 months by the addition of ethylene glycol (300 milligrams final concentration) to freshly prepared plasma and storage at -20 degrees C. Pools of human plasma from healthy humans, stabilized and stored as above, and containing a low, medium or high content of the above enzymes, were used to establish the analytical imprecision (within-run, day-to-day and total imprecision) of the fluorimetric assay. Ten replicates in ten different analytical series, covering a period of two months, were performed. The total imprecision (expressed as coefficient of variation) was in general lower than 10%; in a few cases, particularly plasma samples with a low enzyme content, the total imprecision was 18%. The isozymes A, B, I1, and I2 of N-acetyl-beta-glucosaminidase displayed the same stability upon storage as the unfractionated enzyme. It is concluded that pools of human plasma containing known amounts of lysosomal enzymes, stabilized by the addition of 300 micrograms ethylene glycol and stored at -20 degrees C, are suitable liquid materials for calibration and quality control for the assay of the same enzymes.
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PMID:Preparation of a stable liquid material for calibration and quality control for lysosomal enzymes in plasma. Assay of enzymes of lysosomal origin in plasma, I. 133 72

The changes in the activities of certain lysosomal hydrolases, viz., beta-glucuronidase, beta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, alpha-mannosidase, cathepsin B, cathepsin D, and collagenolytic cathepsin, in serum and heart of rats subject to myocardial infarction with isoproterenol, were studied during the periods of peak infarction and recovery. The activities of all the enzymes assayed exhibited a significant increase both in serum and in heart at peak infarction stage and these levels returned to normal during the stage of recovery and repair. The infiltration of inflammatory cells at the infarct regions and the altered lysosomal fragility are probably responsible for the increased activity of the enzymes studied. This may also bring about the catabolism of connective tissue constituents as reported in literature.
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PMID:Influence of isoproterenol-induced myocardial infarction on certain glycohydrolases and cathepsins in rats. 201 10

Three fluorescein-labeled lectins were shown to bind differentially to cell surfaces in different epithelial layers of rat oral mucosa regardless of the age or the site of origin of the tissue. Griffonia simplicifolia (GS-1-B4), specific for alpha-D-galactosyl end groups, labeled basal cells only; Ulex europeus (Ulex 1) specific for alpha-L-fucosyl groups labeled spinous cells; and Bandeiraea simplicifolia (BSII), specific for N-acetyl-D-glucosamine, labeled cornified cells. Pretreatment of sections with alpha-galactosidase completely abolished the staining of basal cells by GS-1-B4, but had no effect on the staining of spinous cells by Ulex 1. In contrast, alpha-fucosidase abolished the staining of spinous cells by Ulex 1 and caused staining of both basal and spinous cells by GS-1-B4. Neuraminidase and chondroitinase ABC produced results similar to one another, with staining of basal cells by GS-1-B4 and labeling of both basal and spinous cells with Ulex 1. beta-galactosidase, beta-glucuronidase, and testicular hyaluronidase did not affect the staining pattern of GS-1-B4 or Ulex 1, whereas chymotrypsin completely abolished any staining with either lectin. The results demonstrate a complex arrangement of cell surface carbohydrates in the epithelium of rat oral mucosa. The findings indicate a possible simplification in the spatial arrangements of cell surface carbohydrates during the differentiation of basal to spinous cells.
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PMID:Preferential lectin binding to specific layers of rat oral epithelium and modification by enzyme pretreatment. 299 51

The activities of several glycosidases in the lysosomal fraction of the uterine endometrium of rabbit were measured using 4-MU-glycosides as substrates. The specific activity of beta-N-acetylglucosaminidase was the highest, which was followed by beta-galactosidase, beta-glucuronidase, and alpha-galactosidase in this order. beta-Glucosidase had the lowest activity among the glycosidases examined. In order to examine the hormonal effects on these glycosidases, the lysosomal fractions were prepared from the uterine endometrium of the control, estrogen-treated, and progesterone-treated rabbits. In all glycosidases examined, except for beta-glucosidase, the specific activity was highest in the lysosome obtained from estrogen-treated rabbit. The specific activity in the lysosome from the progesterone-treated rabbit was between that from the estrogen-treated rabbit and that from control. Hormonal treatments, however, affected neither pH optimum curves nor isozyme patterns of these glycosidases.
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PMID:Hormonal effects on the activities of glycosidases in the endometrium of rabbit uterus. 301 Oct 36

Activities of 10 lysosomal hydrolase enzymes (beta-hexosaminidase, beta-galactosidase, alpha-galactosidase, alpha-mannosidase, beta-mannosidase, alpha-L-fucosidase, beta-glucuronidase, alpha-glucosidase, alpha-N-acetylgalactosaminidase, and acid phosphatase) were determined in eight organs (brain, liver, kidney, spleen, heart, skeletal muscle, lung, and testis) in males and females of six inbred mouse strains (C57BL/6J, C3H/HeJ, DBA/2J, BALB/cJ, P/J, and 129/J). Examples of enzyme-specific variation, organ-specific variation, and enzyme- and organ-specific variation were found. New enzyme-specific variants with the features of systemic regulators for alpha-L-fucosidase and beta-mannosidase were found. Known variants were detected. Organ-specific variants had some of the properties expected for a new class of genes affecting multiple enzymes: organ-specific regulators.
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PMID:Variation in ten lysosomal hydrolase enzyme activities in inbred mouse strains. 302 5

Evidence indicates that lysosomal enzymes can carry out corneal autolysis during corneal storage and that they are damaging to the corneal endothelium. The authors investigated the release of lysosomal enzymes into two corneal storage media (K-Sol and McCarey-Kaufman [M-K]) by paired human donor corneas during 4 degrees C storage. The authors also studied the interaction of these media with lysosomal enzymes from human cornea. K-Sol and M-K stimulated (P less than 0.01) both beta-glucuronidase and alpha-galactosidase about equally. beta-N-Acetyl-glucosaminidase, a major catabolic enzyme of the cornea, was inhibited by the chondroitin sulfate in K-Sol by over 90% (P less than 0.01). Corneas stored in M-K released more lysosomal enzymes than corneas stored in K-Sol. At 4 days, the values approached significance (P less than 0.06) and by day 10 significantly higher values were found in the M-K media (P less than 0.01). Both storage methods showed a linear release. Individual corneas were found to vary in their release rates. Whether corneas that release more enzyme will show higher endothelial cell loss or produce less successful penetrating keratoplasty grafts deserves further study.
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PMID:Lysosomal enzyme levels in corneal storage media. K-Sol versus McCarey-Kaufman. 314 77

Electron inactivation analysis with 16 MeV electrons was used to determine the functional target size of a number of commonly studied lysosomal hydrolases. Observed values ranged from a low of 62 000 +/- 4000 Da for beta-galactosidase to a high of 200 000 +/- 17 500 Da (mouse beta-glucuronidase). One group of lysosomal hydrolases (N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, alpha-galactosidase, beta-mannosidase, beta-glucosidase, arylsulphatase A and sphingomyelinase) had target sizes in the range 100 000-120 000 Da, whereas alpha-glucosidase and alpha-fucosidase exist as complex multimers in the 150 000-160 000 Da range. Analysis of freeze-dried cell material showed little evidence of species (mouse versus human) variation in the functional size of most lysosomal hydrolases with the exception of beta-glucuronidase. Our findings suggest the potential usefulness of lysosomal hydrolases as endogenous marker enzymes in studies where the target size of proteins of unknown molecular mass is to be determined.
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PMID:Functional lysosomal hydrolase size as determined by radiation inactivation analysis. 315 87


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