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)

In addition to the already known acid phosphatase and beta-glucuronidase, 2 other lysosomal enzymes: aryl sulphatase and N-acetyl-beta-glucosaminidase were localized by histochemical methods in the renin-containing granules of the mouse juxtaglomerular cells.
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PMID:Lysosomal enzymes in the juxtaglomerular cell granules. 43 49

Androgen controls the expression of beta-glucuronidase and several other proteins in the kidney of the standard laboratory mouse, Mus musculus. Other species within the genus Mus exhibit a variety of response patterns for kidney beta-glucuronidase and other markers of androgen action. We have investigated the mechanism of androgen action in M. caroli, a Mus species that does not produce beta-glucuronidase in response to testosterone. The failure of testosterone to induce beta-glucuronidase in M. caroli females cannot be overcome by treatment with dihydrotestosterone, with pharmacological doses of testosterone propionate or dihydrotestosterone propionate, or with a variety of potent androgen analogues. All of these compounds induce kidney beta-glucuronidase in M. musculus females and kidney ornithine decarboxylase, submandibular gland renin, and submandibular gland epidermal growth factor in both M. caroli and M. musculus females. Furthermore, kidney androgen receptor proteins from M. caroli and M. musculus animals have the same sedimentation characteristics on sucrose density gradients. These data indicate that androgen resistance in M. caroli is not due to deficient 5 alpha-reductase or aberrant hormone metabolism producing suboptimal levels of functional androgen and is not caused by a defective androgen receptor. They suggest that the resistance of beta-glucuronidase in M. caroli kidney to induction by androgen occurs at the level of the beta-glucuronidase gene.
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PMID:Specificity of androgen resistance in Mus caroli kidney. 307 98

The crude renin granules isolated from rat kidney cortex were purified using iso-osmotic metrizamide-sucrose gradients having osmolalities ranging from 300 mOsm/kg (= isotonic) to 1700 mOsm/kg. The density gradients were centrifuged at 116,000 g (maximum) for 60 min. 1. Working at 22 degrees-25 degrees C gave similar results as working at 0 degrees-4 degrees C. Hence further experiments were performed at room temperature. 2. The density of renin granules, mitochondria and lysosomes was a linear positive function of the log of osmolality. 3. It was not possible to separate renin granules from mitochondria at 300 mOsm/kg since both the organelles equilibrated at 1.154 kg/l. A reproducible separation was achieved at 850 mOsm/kg or higher but then the major fraction of lysosomes was superimposed on renin granules. Microsomes were always lighter than renin granules. 4. As compared with the total homogenates, renin/protein ratio was increased six-fold renin/malic acid dehydrogenase ratio 21-fold and renin/beta-glucuronidase ratio 3.5-fold. 5. Finally it was demonstrated that renin granules purified at high osmolalities tend to lyse when transferred into an isotonic medium.
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PMID:Isolation of renin granules from rat kidney cortex by isotonic or hyperosmotic metrizamide-sucrose gradients. 699 57

The furosemide-induced increase in protein excretion, and its relations to 1) the size of protein molecules as reflected by three enzymes, and 2) glomerular filtration rate (GFR), plasma renin activity (PRA) and prostaglandin (PG) E2 and F2 alpha excretions were studied in 14 outpatients with normal renal function and 13 healthy males. Furosemide (120 mg) was given intravenously, and thereafter the protein excretion and the above parameters were monitored for 1--2 hours. In both groups, furosemide caused a transient increase in protein excretion. The excretion of the largest molecule, beta-glucuronidase, rose to 6.3-fold, while those of N-acetyl-beta-D-glucosaminidase and of the smallest molecule, alpha-amylase, increased by 91 and 37%, respectively. GFR increased, too, but markedly less than the protein excretion. PGE2 and PGF2 alpha excretions increased more than GFR and changed simultaneously with the excretion of proteins. Furosemide also caused a marked increase in PRA. This lasted, however, much longer than the rise in PG and protein excretion or GFR. The results suggest that the furosemide-induced increase in protein excretion is 1) related to the molecular size of proteins, 2) partly due to the rise in GFR, 3) simultaneous with the change in PG excretion. Our findings also agree with the view that furosemide causes changes in glomerular permeability.
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PMID:Increased urinary protein excretion after intravenous injection of furosemide in man. 700 92

As4.1, a renin-expressing cell line isolated from a mouse renal tumor, was characterized for synthesis, processing, storage and secretion of renin polypeptides. Metabolic labeling, immunoprecipitation and SDS/PAGE analysis revealed that renin was secreted into the culture supernatant predominantly in the form of prorenin which migrated as products of 42-47 kDa. The predominant intracellular renin was processed into two chains, of 33-34 and 5 kDa. N-glycanase treatment removed N-linked oligosaccharides and yielded products of 41 kDa for prorenin and 31-32 kDa for the heavier chain of two-chain renin. The N-terminus of the constitutively secreted prorenin was determined by automated Edman degradation to be Leu22 while the N-terminus of the heavy chain was Ser72. Renin polypeptides constituted 3.1 +/- 1.4% (mean percentage of total precipitable radioactivity +/- SD) of de-novo-synthesized protein secreted into the medium and 0.2 +/- 0.17% retained intracellularly. Extrapolation of renin activity assays suggest that a single cell stores approximately 680 fg of active renin. A slow incremental release into the medium of processed renin heavy chain was detected by immunoprecipitation and SDS/PAGE. Renin activity assays confirmed the release of approximately 4 fg prorenin and 0.32 fg active renin cell(-1) h(-1). Indirect immunofluorescence demonstrated intracellular renin to be distributed in a punctate pattern. Renin was found to be colocalized with the lysosomal marker, beta-glucuronidase, by double-fluorescent labeling. These cells have enabled characterization of glycosylated mouse renin-1 and may prove a valuable tool for studying intracellular trafficing of renin and associated processing enzymes.
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PMID:Biosynthesis of renin in mouse kidney tumor As4.1 cells. 903 Jul 38