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

---

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

Leupeptin, a nontoxic thiol protease inhibitor, has been proposed to have therapeutic use in hereditary muscular dystrophies. The purpose of this study was to characterize the in vivo changes in proteolytic activity of skeletal muscles induced by the repeated administration of leupeptin. Further, whether the modulation of proteolytic capacity by leupeptin affects the repair process of muscle injuries caused by heavy exercise was studied. Leupeptin was administered in mice intraperitoneally at a dose level of 15.5 mg/kg twice a day for 9 days. Leupeptin, known to be an inhibitor of cathepsin B both in vitro and after a single injection in vivo, paradoxically induced an increase of cathepsin B activity in mouse skeletal muscles after repeated administration. In addition, leupeptin administration for 9 days increased the activities of cathepsins C and D, as well as the rate of acid autolysis. The activity of beta-glucuronidase also increased, while those of arylsulfatase, ribonuclease, and alkaline protease were unaffected. No histopathologic changes were observed. At the low dosage used, leupeptin had no effect on the repair process of skeletal muscle after exercise injuries, although several proteolytic processes occur during the regeneration. It is suggested that the increase of acid protease activities in skeletal muscles is an adaptive response to the administration of the proteolytic inhibitor leupeptin and that leupeptin can be administered without prevention or delay of regenerative processes after the onset of myopathic changes.
...
PMID:Effects of the protease inhibitor leupeptin on proteolytic activities and regeneration of mouse skeletal muscles after exercise injuries. 638 26

Administration of zinc (Zn) simultaneously with lead (Pb) into the chick egg yolk sac reduced the accumulation of Pb and Pb-induced alterations in the activities of acid phosphatase, beta-glucuronidase and ribonuclease in the brain of the embryo. The results suggest protection against toxic effects of Pb by Zn.
...
PMID:Effect of zinc on lead-induced changes in brain lysosomal enzymes in the chick embryo. 669 89

The effects of fenvalerate, a pyrethroid insecticide, were studied on some mouse liver enzymes. Given orally, either in a single dose of 60 mg/kg or in a six daily doses of 20 mg/kg, fenvalerate reduced the activity of the B6-dependent kynurenine hydrolase (KH), but increased that of kynurenine aminotransferase (KATE) and beta-glucuronidase (beta-Glase). While the single dose treatment with fenvalerate had no effect on acid ribonuclease (RNase), the repeated treatments increased the activity of this enzyme. This study demonstrates that fenvalerate can alter the kynurenine metabolizing enzymes and acid ribonuclease of mouse liver.
...
PMID:Effect of fenvalerate on kynurenine metabolizing enzymes and acid ribonuclease of mouse liver. 717 2

Acid hydrolase activities in skeletal and cardiac muscle were studied 5, 10 and 20 days after exhaustive intermittent running by untrained and endurance-trained mice. Exhaustion increased the activities of cathepsin D, beta-glucuronidase and ribonuclease, but not that of p-nitrophenylphosphatase in skeletal muscle of untrained mice. Activities were highest on the fifth day after exhaustion and decreased during the following two weeks. More intensive loading produced no changes in acid hydrolytic capacity in skeletal muscle of endurance-trained mice. Acid hydrolase activities in cardiac muscle of both untrained and trained mice were unaffected by exhaustive running. It is suggested that exhaustive running causes both lethal and sublethal hypoxic fiber injuries in the skeletal muscle of untrained mice but not in that of endurance-trained mice or in the cardiac muscle of animals of either group. These injuries manifest themselves as fiber necrosis (lethal) and as increased acid hydrolytic capacity in surviving fibers (sublethal).
...
PMID:Acid hydrolase activities in mouse cardiac and skeletal muscle following exhaustive exercise. 719 24

An approximately 50-fold increase in serum beta-glucuronidase activity appeared 2 hours after the administration of such organophosphate insecticides as dichlorvs, diazinon and disulfoton and of a carbamate insecticide, carbaryl. The activities of other acid hydrolases in the serum such as ribonuclease, acid phosphatase, hyaluronidase and N-acetylglucosaminidase did not change significantly after the insecticide treatment. The response was related to the dose level and was evident after a single intraperitoneal dose of diazinon as low as 1.6 mg/kg. This appearence of an increase in beta-glucuronidase was retarded by pretreatment with SKF 525A, an inhibitor of drug metabolizing enzyme. When beta-glucuronidase was elevated by a large dose of diazinon, full response to a second dose of diazinon did not occur until approximately one month after administration of the first dose.
...
PMID:Increase of beta-glucuronidase activity in the serum of rats administered organophosphate and carbamate insecticides. 726 27

The effect of a low protein (4%) diet on the activity of the hydrolytic enzymes ribonuclease, deoxyribonuclease, acid and alkaline phosphatases, beta-glucuronidase and lysozyme has been studied in the spleen and thymus of weanling Wistar rats. Experimentation was carried out over 20 and 30 days, and comparisons were made with well-nourished (12% protein) controls. Body weight decreased during the terminal period in protein-deficient animals (P less than 0.001). Spleen and thymus absolute net weights also dropped significantly (P less than 0.001). In terms of organ weight relative to body weight, there was a clear decrease in thymus compared with controls (P less than 0.001). Enzyme activities expressed per total organ fell significantly. Thus, in spleen at 20 days the decrease was maximum in ribonuclease activity (91.15%) and minimum in acid phosphatase activity (44.09%). Thymus decreases ranged from 83.60% activity in beta-glucuronidase and 93.56% in ribonuclease. At 30 days decreases were accentuated; the maximum value in spleen was 92.34% lysozyme and, in thymus, 97.09% acid phosphatase. A large increase in hydrolytic activity expressed per milligram of protein was registered, especially at 30 days. This increase reached a maximum of 78.08% beta-glucuronidase in thymus and a minimum of 56.1% alkaline phosphatase; acid phosphatase and ribonuclease activities were not modified. In spleen, however, acid phosphatase (34.00%), alkaline phosphatase (62.50%), deoxyribonuclease (39.25%), and beta-glucuronidase (36.01%) increased, but lysozyme and ribonuclease enzymes decreased. We concluded that a low protein diet increases catabolism in spleen and thymus through an enhancement of lysosomal hydrolase activities.
...
PMID:Effect of protein deficiency on the lysosomal enzyme activities of the spleen and thymus of weanling rats. 731 May 38

To determine the ability of isolated S-locus promoter sequences to direct organ-specific gene expression, we used microprojectile bombardment to introduce chimeric S-allele/beta-glucuronidase genes into different tissues of Petunia hybrida for transient expression. Histochemical staining showed that S-locus/beta-glucuronidase fusions were expressed in pistil, ovary, and petal tissue. No expression of the chimeric genes was detected in leaves or in mature pollen, either by histochemical staining or by fluorescence assays. RNA blot hybridization confirmed that low levels of S-locus mRNA accumulate in petals and ovaries in vivo. Analysis of the expression pattern of S-locus promoter deletions showed that sequences in the immediate vicinity of the TATA box were sufficient to confer qualitatively correct organ-specific expression of beta-glucuronidase. To further investigate the potential for S-ribonuclease expression in pollen, we used the polymerase chain reaction to amplify RNA accumulated in developing anthers. These assays demonstrated that mRNA for the S-ribonuclease accumulates to low levels in developing anthers several days prior to corolla opening and pollen anthesis. We discuss these results in light of current models of self-incompatibility.
...
PMID:The S-ribonuclease gene of Petunia hybrida is expressed in nonstylar tissue, including immature anthers. 797 17

The intracellular pathogenesis-related (PR) proteins of common bean (Phaseolus vulgaris L.) are encoded by a highly polymorphic family of at least 20 genes. One member, the Ypr10*c gene, has been isolated and characterised. The deduced amino acid sequence of the encoded protein, PR-10, exhibits similarities to tree-pollen allergens, to food allergens from celery and apple and to ginseng ribonuclease peptide sequences. We show by RNA blot analysis that the Ypr10 gene family, including Ypr10*c, is strongly expressed in bean roots. In leaves Ypr10 transcript levels are low in young and mature stages but are elevated during senescence and in diseased states. Dark treatment of leaves causes strong induction of Ypr10 transcripts, which is reversible by light, and diurnal rhythms of transcript accumulation during the night are observed. Ypr10 genes are responsive to external stimuli related to pathogen-defence such as glutathione or salicylic acid. Transcriptional activity of a Ypr10*c promoter-beta-glucuronidase fusion gene in transgenic tobacco was observed in roots, in developing xylem and phloem of stems, and in the blade of senescent leaves, with highest levels at the onset of senescence. The most striking characteristic of developmental expression was the specific localisation of beta-glucuronidase activity in the transmitting tract of styles in flowers at anthesis. Feeding of various pathogen-related and stress-related stimuli to young tobacco leaves led to accumulation of GUS activity in leaf blades. We identify considerable spatio-temporal similarities between reported expression patterns of Ypr10 genes and ribonuclease genes, which, together with the significant sequence similarity to the ginseng ribonuclease, support the hypothesis of a ribonuclease function for PR-10 proteins and allow the prediction of possible biological roles.
...
PMID:Bean ribonuclease-like pathogenesis-related protein genes (Ypr10) display complex patterns of developmental, dark-induced and exogenous-stimulus-dependent expression. 870 31

AP19 is the smallest polypeptide component of AP-1, the clathrin associated protein complex found in clathrin-coated vesicles of the Golgi apparatus. Two genomic clones that encode homologues of AP19 were isolated from Arabidopsis thaliana (AAP19-1 and AAP19-2). Analysis of their nucleotide sequences predict proteins of 162 and 163 amino acids with mr of 18,913 and 18,758 respectively. Amino acid sequence comparisons with mammalian, yeast and plant clathrin associated sequences indicates that the Arabidopsis genes encode polypeptides that are more closely related to the AP19 proteins associated with clathrin-coated Golgi vesicles than to AP17, which is part of the AP-2 complex of endocytic clathrin-coated pits. Ribonuclease protection assays showed that both genes are expressed in all Arabidopsis tissues throughout development. Constitutive transcription of AAP19-1 was confirmed in transgenic Arabidopsis seedlings and plants containing an AAP19-1 promoter::beta-glucuronidase (GUS) fusion by ribonuclease protection assays and GUS histochemical staining.
...
PMID:Molecular characterization of the AP19 gene family in Arabidopsis thaliana: components of the Golgi AP-1 clathrin assembly protein complex. 942 6

A major response of eukaryotic cells to the presence of unfolded proteins in the lumen of the endoplasmic reticulum (ER) is to activate genes that encode ER-located molecular chaperones, such as the binding protein. This response, called the unfolded protein response, requires the transduction of a signal from the ER to the nucleus. In yeast (Saccharomyces cerevisiae) and mammalian cells, an ER-located transmembrane receptor protein kinase/ribonuclease called Ire1, with a sensor domain in the lumen of the ER, is the first component of this pathway. Here, we report the cloning and derived amino acid sequences of AtIre1-1 and AtIre1-2, two Arabidopsis homologs of Ire1. The two proteins are located in the perinuclear ER (based on heterologous expression of fusions with green fluorescent protein). The expression patterns of the two genes (using beta-glucuronidase fusions) are nearly nonoverlapping. We also demonstrate functional complementation of the sensor domains of the two proteins in yeast and show that the Ire1-2 protein is capable of autotransphosphorylation. These and other findings are discussed in relation to the involvement of these genes in unfolded protein response signaling in plants.
...
PMID:Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum-located transmembrane protein kinases. 1170 77


<< Previous 1 2 3 Next >>

---