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)

Adult mongrel dogs were castrated and treated by intramuscular injections of 5 alpha-androstane-3 alpha,17 beta-diol (androstanediol) alone or in combination with estradiol in order to find convenient enzymatic markers of hormone action in prostate. The activities of 15 hydrolytic enzymes were determined. Arginine esterase, acid sulfatase, and acid phosphatase were found to be the most sensitive markers of testicular hormones since they were decreased 18-, 5- and 5-fold respectively after 1 month of castration. The enzyme activities returned to precastration levels after 2 weeks of injection of androstanediol to castrated animals. The effect of androstanediol on the majority of the remaining enzymes was small. In general, the activities obtained after androstanediol treatment in combination with estradiol were similar to those obtained with androstanediol alone. Finally, beta-glucuronidase and neutral sulfatase were increased after castration, a finding that suggests that these enzymes are constituents of stromal cells. These studies will provide a basis for future studies of hormone action in the dog prostate.
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PMID:Effect of castration and steroid treatments on the activity of some hydrolytic enzymes in dog prostate. 686 53

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

Chemical alteration of the glucocorticoid, methylprednisolone, has led to the introduction of a new class of compounds called the 21-aminosteroids (21-ASs). The purpose of this study was to investigate the effect of the 21-AS, U74389G, on silica-induced acute lung injury. Male Fischer 344 rats were treated intraperitoneally with saline or U74389G in a total dose of 15 mg/kg divided into three injections of 5 mg/kg separated by 4 h. Following the first treatment, animals from the two groups were intratracheally instilled with silica (10 mg/100 g body wt in 0.5 ml of saline) or saline vehicle (0.5 ml). Twenty-four hours after the instillations, bronchoalveolar lavage (BAL) was performed. In the animals not receiving U74389G, marked increases in total protein, beta-glucuronidase, and lactate dehydrogenase (LDH) activities and number of neutrophils (PMNs) were demonstrated in the BAL fluid of the silica-treated animals compared to their controls. Silica also caused dramatic increases in the luminol-dependent chemiluminescence (CL) of lung tissue and BAL cells. The CL reaction was decreased by superoxide dismutase (SOD) and N-nitro-L-arginine methyl ester hydrochloride (L-NAME), a nitric oxide (NO) synthase inhibitor. In animals treated with U74389G, there was attenuation of the silica-induced increases in biochemical, cellular, and chemiluminescent indices of damage. This study demonstrates that U74389G significantly reduces acute lung injury caused by the intratracheal instillation of silica, and this drug may be of potential value for treatment of lung diseases in which damage caused by reactive oxygen species has been implicated.
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PMID:Attenuation of acute inflammatory effects of silica in rat lung by 21-aminosteroid, U74389G. 770 90

The nuclear localization sequences (NLSs) of the Ac transposase (TPase) protein have been characterized by indirect immunofluorescence detection of TPase deletion derivatives and TPase/beta-glucuronidase (GUS) fusion proteins in transiently transfected Petunia cells. The TPase contains three NLSs near its amino-terminal end, NLS(44-62), NLS(159-178) and NLS(174-206), each of which is sufficient to redirect GUS to the nucleus. Deletion of the N-terminal 102 TPase residues including NLS(44-62) results in strongly reduced nuclear import of the truncated TPase. NLS(44-62) and NLS(159-178) are bipartite NLSs, whereas the structure of NLS(174-206) does not allow a classification into one of the three major NLS categories. NLS(174-206) overlaps with the basic DNA-binding domain of TPase. A substitution of two amino acids in this segment (His191-->Arg and Arg193-->His) results in a total loss of DNA-binding activity, but retains reduced NLS activity. Accordingly, the two functions can be separated. In addition, we show that a NLS-deficient 71 kDa TPase derivative is co-imported into the nucleus in the presence of wild-type TPase.
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PMID:One of three nuclear localization signals of maize Activator (Ac) transposase overlaps the DNA-binding domain. 775 16

Four prior mutations have been reported in three patients with beta-glucuronidase deficiency mucopolysaccharidosis (MPS VII), none of whom had the severe, infantile, hydropic form of the disease. We identified two mutations in the first reported case of nonimmune hydropic MPS VII whose cultured fibroblasts had < 1% of residual activity. The first mutation was a C-->T transition at position 1061 of the cDNA in exon 6 that gave rise to an Ala-->Val substitution in codon 354 (A354V). The second was a C-->T transition at position 1831 in exon 12 that produced an Arg-->Trp substitution in codon 611 (R611W). Transient expression in COS-7 cells revealed that both mutant enzymes were synthesized as normal-size precursors in normal quantities, but both exhibited accelerated turnover. The expressed A354V enzyme had a t0.5 (half-life) of 33 hr (wild-type t0.5 > 60 hr) and a specific activity 35% of wild-type enzyme. The R611W enzyme had a t0.5 of 20 hr and no detectable catalytic activity. The t0.5 of enzyme produced on cotransfection with A354V and R611W was nearly identical to that of A354V alone. Mutant enzyme expressed in transfected murine MPS VII cells gave similar residual activities relative to the wild-type enzyme. In COS cells, the A354V monomers formed mixed tetramers with coexpressed rat monomers, but the product of R611W did not. The higher than expected activity, both in COS cells and in murine MPS VII cells expressing A354V, provides further evidence that overexpression can partially correct some beta-glucuronidase mutations, apparently by driving the folding reaction of monomers or the assembly into tetramers by mass action.
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PMID:Mutational studies in a patient with the hydrops fetalis form of mucopolysaccharidosis type VII. 811 13

Nodulin-24 is a nodule-specific protein of the peribacteroid membrane (PBM) in soybean. It has an apparent molecular mass of 33 kDa while its full-length cDNA encodes a polypeptide of only 24 kDa. In vitro transcription of nodulin-24 cDNA followed by translation resulted in a peptide translocated into microsomal membranes with cleavage of a signal sequence. The cleavage site of the signal sequence in nodulin-24 was determined to be between Ala (A25) and Arg (R26) by microsequencing of the [3H]leucine-labeled processed peptide. Fusion of the signal sequence of nodulin-24 with the beta-glucuronidase peptide prevented co-translational cleavage of the signal sequence although the translocation of the fused protein into microsomes occurred co-translationally. Trypsin treatment of membrane-translocated nodulin-24 did not result in any alteration in size suggesting that the newly synthesized peptide is fully protected in the membrane vesicle. Fusion of nodulin-24 with beta-glucuronidase also showed no change in size following trypsin treatment, suggesting that nodulin-24 has no membrane-spanning region. In addition, in vitro synthesized nodulin-24 was present in the supernatant fraction after sonication of microsomal membranes. Mature nodulin-24, on the other hand, is not solubilized from PBM by sodium carbonate (pH 11) or EGTA and is soluble only in detergent. These data suggest that nodulin-24 is synthesized as a lumenal protein in the endoplasmic reticulum and post-translationally attached to the membranes en route to the PBM. This processing results in a significant increase in the apparent molecular mass of nodulin-24 which may be due to the attachment of membrane lipids as this protein shares characteristics with membrane lipoproteins of many pathogenic bacteria.
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PMID:Nodulin-24 follows a novel pathway for integration into the peribacteroid membrane in soybean root nodules. 812 12

Previous genetic and structural evidence indicates that the maize R gene encodes a nuclear transcriptional activating factor. In-frame carboxyl- and amino-terminal fusions of the R gene to the reporter gene encoding beta-glucuronidase (GUS) were sufficient to direct GUS to the nucleus of the transiently transformed onion (Allium cepa) epidermal cells. Further analysis of chimeric constructs containing regions of the R gene fused to the GUS cDNA revealed three specific nuclear localization sequences (NLSs) that were capable of redirecting the GUS protein to the nucleus. Amino-terminal NLS-A (amino acids 100-109, GDRRAAPARP) contained several arginine residues; a similar localization signal is found in only a few viral proteins. The medial NLS-M (amino acids 419-428, MSERKRREKL) is a simian virus 40 large T antigen-type NLS, and the carboxyl-terminal NLS-C (amino acids 598-610, MISESLRKAIGKR) is a mating type alpha 2 type. NLSs M and C are independently sufficient to direct the GUS protein to the nucleus when it is fused at the amino terminus of GUS, whereas NLS-A fused to GUS partitioned between the nucleus and cytoplasm. Similar partitioning was observed when localization signals NLS-A and NLS-C were independently fused to the carboxy-terminal portion of GUS. A sequential deletion of the localization signals indicated that the amino-terminal and carboxyl-terminal fusions of R and GUS were redirected to the nucleus only when both NLS-A and -M, or NLS-C and -M, were present. These results indicate that multiple localization signals are necessary for nuclear targeting of this protein. The conservation of the localization signals within the alleles of R and similar proteins from other organisms is also discussed.
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PMID:Nuclear targeting of the maize R protein requires two nuclear localization sequences. 827 4

Exposure to silica, a cytotoxic and fibrogenic mineral dust, has been demonstrated to cause pulmonary inflammation and damage to the lung tissue. In contrast to the long-term consequences, little information exists on the sequence of inflammatory/damaging events occurring acutely after exposure to silica. The purpose of this study was to determine the minimum time after the administration of silica that the inflammatory/damage response is detectable and the temporal relationship of these processes. Male Fischer 344 rats were dosed intratracheally with silica (2.5 or 10 mg/100 g body weight) or saline vehicle. At 2 and 4 h after instillation, both cellular (total cell count and neutrophil count) and biochemical (total protein, albumin, and beta-glucuronidase and lactate dehydrogenase activities) parameters of inflammation and damage were evaluated in the bronchoalveolar lavage fluid. At 2 h, total protein levels were elevated at both silica doses, but all other parameters were unchanged; however, 4 h after silica exposure all parameters were elevated over those of the saline control. In a further attempt to characterize the inflammatory/damage processes, luminol-dependent chemiluminescence (LDCL) was performed on aliquots of chopped lung. At 2 h after silica instillation, phorbol myristate acetate-stimulated lung tissue from silica-treated rats had no increase in light production when compared to controls, whereas after 4 h there were significant increases in LDCL activity in both dose groups when compared to controls. The addition of superoxide dismutase (SOD) decreased LDCL activity of the 2.5 mg/100 g group by 59% (2 h) and 66% (4 h), and of the 10 mg/100 g group by 49% (2 h) and 73% (4 h). Alternatively, the addition of N-omega-nitro-L-arginine methyl ester (L-NAME), an inhibitor of nitric oxide synthase, decreased the 2.5 mg/100 g group by 52% (2 h) and 60% (4 h). The 10 mg/100 g group was decreased by 67% (2 h), but only exhibited a 12% reduction at 4 h. SOD and L-NAME also inhibited the background LDCL in saline-treated rats. These reductions in LDCL activity indicate that reactive oxygen and nitrogen species play a role in the acute phase pulmonary response from silica. The results of this study indicate that the initial stages of damage begin to appear by 2 h, but damage and inflammation are definitive by 4 h after administration of silica in rats.
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PMID:Characteristics of the acute-phase pulmonary response to silica in rats. 856 14

Malate synthase is a glyoxysome-specific enzyme. The carboxy-terminal tripeptide of the enzyme is Ser-Arg-Leu (SRL), which is known to function as a peroxisomal targeting signal in mammalian cells. To analyze the function of the carboxy-terminal amino acids of pumpkin malate synthase in plant cells, a chimeric gene was constructed that encoded a fusion protein which consisted of beta-glucuronidase and the carboxyl terminus of the enzyme. The fusion protein was expressed and accumulated in transgenic Arabidopsis that had been transformed with the chimeric gene. Immunocytochemical analysis of the transgenic plants revealed that the carboxy-terminal five amino acids of pumpkin malate synthase were sufficient for transport of the fusion protein into glyoxysomes in etiolated cotyledons, into leaf peroxisomes in green cotyledons and in mature leaves, and into unspecialized microbodies in roots, although the fusion protein was no longer transported into microbodies when SRL at the carboxyl terminus was deleted. Transport of proteins into glyoxysomes and leaf peroxisomes was also observed when the carboxy-terminal amino acids of the fusion protein were changed from SRL to SKL, SRM, ARL or PRL. The results suggest that tripeptides with S, A or P at the -3 position, K or R at the -2 position, and L or M at the carboxyl terminal position can function as a targeting signal for three kinds of plant microbody.
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PMID:Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. 877 80

Mucopolysaccharidosis type VII (MPS VII) is an inherited disease resulting from deficient activity of the lysosomal acid hydrolase beta-glucuronidase (GUSB) and has been reported in humans, mice, cats, and dogs. To characterize canine MPS VII, we have isolated and sequenced the canine GUSB cDNA from normal and affected animals. A single nucleotide substitution was detected in the GUSB cDNA derived from MPS VII dogs. This guanosine to adenine base change at nucleotide position 559 in the canine cDNA sequence causes an arginine to histidine substitution at amino acid position 166. Introduction of the G to A substitution at position 559 in a mammalian expression vector containing the normal canine GUSB cDNA nearly eliminated the GUSB enzymatic activity, demonstrating that this mutation is the cause of canine MPS VII. A retroviral vector expressing the full-length canine beta-glucuronidase cDNA corrected the deficiency in MPS VII cells.
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PMID:Cloning of the canine beta-glucuronidase cDNA, mutation identification in canine MPS VII, and retroviral vector-mediated correction of MPS VII cells. 952 79


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