Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The anti-cancer drug cyclophosphamide (CYP) is nephrotoxic besides being urotoxic thereby limiting its clinical utility. Since the nephrotoxicity of CYP is less common compared to its urotoxicity, not much importance has been given for the study of mechanism of CYP-induced nephrotoxicity. The aim of the present study is to investigate the possible role of lysosomal enzymes in CYP-induced renal damage. Adult female Wistar rats weighing 200-250 g were used for the study. The rats were administered single-intraperitoneal injection of CYP at the dose of 150 mg/kg body wt and sacrificed at various time intervals 6, 16 or 24 h after the dose of CYP. The control rats were administered saline alone. Nephrotoxicity was assessed by measuring plasma creatinine and urea and histopathology of the kidney. The kidney was weighed and used for the assay of lysosomal enzymes namely acid phosphatase, beta-glucuronidase and N-acetylglucosaminidase and total protein content. Histologically, the CYP-treated rat kidneys showed progressive renal damage with increase in time after treatment. Glomerular nephritis, cortical tubular vacuolization and interstitial edema were observed in the CYP-treated rats. Surprisingly, a significant drastic decrease (instead of an increase) in the activities of lysosomal enzymes was observed in the kidneys of CYP-treated rats at 16 and 24 h as compared with the control. A highly significant increase (270%) in protein content was observed in the kidneys of the CYP-treated rats as compared with the control. Decrease in the activities of lysosomal protein digestive enzymes may contribute to CYP-induced renal damage. The accumulation of abnormal amounts of the protein in the kidney may be due at least in part to defect in lysosomal enzyme activity and contribute to renal damage.
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PMID:Effect of cyclophosphamide treatment on selected lysosomal enzymes in the kidney of rats. 1768 19

Posttranscriptional processes are important for regulation of gene expression in plant mitochondria. DEAD-box proteins, which form a huge protein family with members from all kingdoms, are fundamental components in virtually all types of processes in RNA metabolism. Two members of this protein family, designated PMH1 and PMH2 (for PUTATIVE MITOCHONDRIAL RNA HELICASE), were analyzed and characterized in mitochondria of Arabidopsis (Arabidopsis thaliana). Green fluorescent protein tagging with N-terminal PMH1 and PMH2 sequences supports the mitochondrial localization of these proteins. Northern experiments, as well as histochemical beta-glucuronidase staining of transgenic plants carrying respective promoter:beta-glucuronidase fusion constructs, revealed differing transcription patterns for the two genes. In response to cold, however, transcript levels of both genes increased. Immunodetection analyses of mitochondrial protein complexes after two-dimensional blue native/urea SDS-PAGE and after fractionation on sucrose gradients strongly suggest that one or both proteins are part of RNA-dependent complexes. Cold treatment of cell cultures or solubilization of mitochondria in the presence of MgCl(2) favored the detection of high-molecular-mass complexes. This study paves the way for detailed analysis of high-molecular-mass complexes in mitochondria of higher plants.
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PMID:Two DEAD-box proteins may be part of RNA-dependent high-molecular-mass protein complexes in Arabidopsis mitochondria. 1795 54

Four ruminally fistulated multiparous Holstein cows were assigned to a 4x4 Latin square design with a 2x2 factorial arrangement of treatments to study the effects of dietary supplementation of monensin and flaxseed hulls on ruminal and milk concentration of the mammalian lignan enterolactone (EL) and ruminal and faecal activity of beta-glucuronidase. The hypothesis was that monensin supplementation has no effect on the incorporation of EL into milk when cows are fed flaxseed hulls. Treatments were: 1) control, neither flaxseed hulls nor monensin (CO); 2) diet containing (dry matter basis) 20% flaxseed hulls (FH); 3) diet with monensin (16 mg/kg of dry matter; MO); 4) diet containing 20% (dry matter basis) flaxseed hulls and 16 mg/kg monensin (HM). Intake of dry matter was higher for CO and MO than for FH and HM and monensin had no effect. Milk production decreased in cows fed flaxseed hulls while monensin had no effect. Production of 4% fat-corrected milk and concentrations of milk fat, lactose, urea N, and total solids were similar among treatments. Although there was a decrease in ruminal activity of beta-glucuronidase when feeding flaxseed hulls, the metabolism of plant into mammalian lignans may be increased as shown by enhanced concentration of EL in the rumen and milk. Supplementation with flaxseed hulls then may contribute to favourably change milk composition for better human health by enhancing mammalian lignan EL concentration.
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PMID:The interaction of monensin and flaxseed hulls on ruminal and milk concentration of the mammalian lignan enterolactone in late-lactating dairy cows. 1982 14


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