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 activity of the lysosomal enzymes acid phosphatase, beta-glucuronidase, alpha-mannosidase and hexosaminidase were determined in CSF obtained from patients with proven bacterial meningitis and from patients with various other diagnoses. The mean value for CSF beta-glucuronidase from bacterial meningitis was elevated 73-fold when compared to the aggregate mean of all control groups. Acid phosphatase and alpha-mannosidase means were 26-fold and 33-fold elevated respectively while hexosaminidase was threefold elevated. Measurement of CSF acid phosphatase and beta-glucuronidase should prove a rapid useful test in establishing the diagnosis of bacterial meningitis. Chromatography of CSF samples on DEAE Sephadex allowed the resolution of hexosaminidase and beta-glucuronidase into individual isozymes. The ratio of hexosaminidase A to hexosaminidase B was generally higher in CSF from patients with bacterial meningitis but was very variable. The isozyme distribution for beta-glucuronidase was identical to that found in serum and no differences in pattern were found between patients and control subjects.
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PMID:CSF lysosomal hydrolase activity as an aid in the diagnosis of bacterial meningitis. 721 93

beta-Hexosaminidase isoenzymes were separated by DEAE-cellulose chromatography in the serum of 23 patients infected with human immunodeficiency virus at different stage of the disease. Forms corresponding to hexosaminidase B, I and A were present in pathological sera. There is an increase in the percentage of hexosaminidase I in pathological sera, that could be used as an additional marker to monitor the clinical stage of the disease. Furthermore, total activities of some lysosomal enzymes were determined in these sera. Activities of beta-hexosaminidase, determined with 4-methylumbelliferyl-beta-N-acetylglucopyranoside substrate, alpha-mannosidase and beta-mannosidase were significantly higher in the serum of patients at the C3 stage of disease than in controls. No significant differences were observed in the activity of beta-hexosaminidase, determined with 4-methylumbelliferyl-beta-N-acetylglucopyranoside-6-sulphate substrate, beta-glucuronidase and beta-galactosidase.
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PMID:Lysosomal hydrolases in serum from human immunodeficiency virus-infected patients. 893 Apr 13

Because inflammation could affect lysosomal enzyme trafficking, resulting in increased enzyme release from the cells, tissue necrosis, or altered blood- and the brain-cerebrospinal fluid (CSF) barrier, the activity of four lysosomal enzymes in the cell-free CSF of 34 patients with bacterial meningitis, 20 with aseptic meningitis, and 39 control subjects was measured. Activities are expressed in nanomoles of 4-methylumbelliferone mL/h. The median beta-hexosaminidase A activity in bacterial meningitis was 313, in aseptic meningitis it was 173, and in the control subjects it was 175, the median beta-hexosaminidase B activity was 417, 165, and 120; the median alpha-mannosidase activity was 171, 124, and 113; and the median beta-glucuronidase activity was 133.7, 14.3, and 10.0, respectively. The difference of the activities of the four enzymes measured between the bacteria meningitis and the controls is significant (p < 0.000). Also significant is the difference between bacterial and aseptic meningitis (p = 0.005 to < 0.000), but it is not significant between aseptic and control subjects. Both the sensitivity and specificity of the beta-glucuronidase activity between bacterial meningitis and control subjects were 100%, whereas the corresponding values between bacterial and aseptic meningitis were 100% and 90%, respectively. No significant correlation was observed between the activities of the enzymes measured and the number of the polymorphonuclear leukocytes or other laboratory characteristics of the CSF. The increased lysosomal enzyme activities in the CSF of patients with meningitis may result from diffusion across the blood-CSF or the brain-CSF barrier or from enzyme leakage through the cell membranes.
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PMID:Increased activity of lysosomal acid hydrolases in the cell-free cerebrospinal fluid of bacterial meningitis. 902 45