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)

Enzymes considered to be markers for neurons (angiotensin converting enzyme, thermolysin-like metalloendopeptidase, alanine aminopeptidase, and glutamate-oxaloacetate transaminase), glia (glutamine synthetase, pyruvate carboxylase, and beta-glucuronidase), and endothelial cells (alkaline phosphatase and plasminogen activator) were measured in caudate nucleus from 10 sudden death controls, eight agonal state controls, and 16 Huntington's disease patients. Glutamate-oxaloacetate transaminase was slightly reduced by agonal state. The four enzymes with a neuronal distribution were all correlatively reduced in Huntington's disease caudate nucleus. Glutamine synthetase activity was reduced and beta-glucuronidase mean activity increased over twofold in Huntington's disease caudate nucleus, with the two enzyme activities being inversely related. Pyruvate carboxylase was markedly affected by agonal state and was very variable in Huntington's disease caudate nucleus. The two endothelial enzymes were unaltered in Huntington's disease caudate nucleus. The findings are indicative of neuronal loss, an increased proportion of altered glia, and also of maintained vasculature in Huntington's disease caudate nucleus. Measurement of enzyme activities can help to delineate the types of cell altered in Huntington's disease.
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PMID:Changes in nine enzyme markers for neurons, glia, and endothelial cells in agonal state and Huntington's disease caudate nucleus. 287 90

Amino acid analysis of oxidized or reduced and carboxymethylated beta-glucuronidase have shown the presence of 24 cysteic acid or S-carboxymethylcysteine residues respectively per mole of the tetrameric enzyme. Titration of sulfhydryl groups gave eight cysteine residues, and by difference 16 half-cystine residues per mole. Six peptides containing radiolabelled cysteine residues were isolated from pepsin and chymotrypsin digest of reduced and S-carboxymethylated beta-glucuronidase by ion-exchange chromatography or gel filtration, followed by paper ionophoresis and paper chromatography. The peptides were analysed for amino acids and sequenced by the dansyl-Edman procedure. Peptides containing cysteic acid were selectively recovered from thermolysin digests of performic acid-oxidized glucuronidase. The amino acid sequences confirmed that there were only six different peptide sequences containing either cysteine or half-cystine residues in the tetrameric enzyme, supporting the presence of four identical subunits. These sequences wer: (A)-Val-Asx-Val-Ile-Cys-Val-Asx-Ser-Tyr- (B)-Gly-Asx-Leu-Cys-Ser-Gly- (C)-Phe-Val-Val-Ile-Asx-Glx-Cys-Pro-Gly-Val-Gly- (D)-Val-Val-Cys-Leu- (E)-Gln-Ser-Gly-Cys-Leu-Val-Lys-Gly-Tyr- (F)-Cys-Asp-Arg-Tyr-Gly-Ile-Val-Val-.
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PMID:Amino acid sequences containing cysteine or half-cystine residues in beta-glucuronidase. 721 58

The expression of procyclins is the earliest known marker of differentiation of bloodstream forms of Trypanosoma brucei to procyclic forms. We have generated transgenic bloodstream and procyclic forms in which the coding region of one procyclin gene was replaced by E. coli beta-glucuronidase (GUS). GUS activity can be monitored in a simple one-step colour reaction in microtitre plates; this assay is potentially suitable for large-scale screening for compounds that influence differentiation. GUS was stage-specifically expressed in procyclic forms and its synthesis occurred in parallel with that of procyclin when bloodstream forms were triggered to differentiate by the addition of cis-aconitate. GUS could also be induced by brief treatment with the proteases trypsin, pronase or thermolysin, but not with pepsin or thrombin. Interestingly, a combination of one of the active proteases with cis-aconitate resulted in increased GUS activity relative to either trigger alone. In contrast to cis-aconitate, protease treatment resulted in considerable cell death. Experiments with the pleomorphic strain AnTat 1.1 showed that long slender bloodstream forms were rapidly killed by proteases, whereas stumpy forms were largely resistant. Stumpy forms treated with trypsin differentiated synchronously and expressed procyclin with faster kinetics than when they were triggered by cis-aconitate. As predicted by the GUS assay, differentiation was even more rapid when both inducers were used simultaneously, with all cells expressing maximal levels of procyclin within 3 h.
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PMID:The use of transgenic Trypanosoma brucei to identify compounds inducing the differentiation of bloodstream forms to procyclic forms. 1059 84