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)

A procedure was developed for the analytical isolation of brush border and basal lateral plasma membranes of intestinal epithelial cells. Brush border fragments were collected by low speed centrifugation, disrupted in hypertonic sorbitol, and subjected to density gradient centrifugation for separation of plasma membranes from nuclei and core material. Sucrase specific activity in the purified brush border plasma membranes was increased fortyfold with respect to the initial homogenate. Basal lateral membrane were harvested from the low speed supernatant and resolved from other subcellular components by equilibrium density gradient centrifugation. Recovery of Na, K-ATPase activity was 94%, and 61% of the recovered activity was present in a single symmetrical peak. The specific activity of Na, K-ATPase was increased twelvefold, and it was purified with respect to sucrase, succinic dehydrogenase, NADPH-cytochrome c reductase, nonspecific esterase, beta-glucuronidase, DNA, and RNA. The observed purification factors are comparable to results reported for other purification procedures, and the yield of Na, K-ATPase is greater by a factor of two than those reported for other procedures which produce no net increase in the Na, K-ATPase activity. Na, K-ATPase rich membranes are shown to originate from the basal lateral plasma membranes by the patterns of labeling that were produced when either isolated cells or everted gut sacs were incubated with the slowly permeating reagent 35S-p-(diazonium)-benzenesulfonic acid. In the former case subsequently purified Na, K-ATPase rich and sucrase rich membranes are labeled to the same extent, while in the latter there is a tenfold excess of label in the sucrase rich membranes. The plasma membrane fractions were in both cases more heavily labeled than intracellular protein. Alkaline phosphatase and calcium-stimulated ATPase were present at comparable levels on the two aspects of the epithelial cell plasma membrane, and 25% of the acid phosphatase activity was present on the basal lateral membrane, while it was absent from the brush border membrane. Less than 6% of the total Na, K-ATPase was present in brush border membranes.
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PMID:Analytical isolation of plasma membranes of intestinal epithelial cells: identification of Na, K-ATPase rich membranes and the distribution of enzyme activities. 13 16

Rats were injected with labeled Kunitz protease inhibitor and killed at various times thereafter. Radioactivity was measured in various fractions of kidney homogenates in order to study the time-dependent fixation to different cell organelles, expecially the transition from the brush border to lysosome fraction. With short survival periods (up to 5 min), the renal protease inhibitor is recovered nearly completely with the brush border fraction. With longer periods, a shift towards particles with higher densities and higher beta-glucuronidase activities takes place. Similar results have been achieved with insulin. Lysosomes were prepared and subfractionated following i. v. administration of the protease inhibitor or insulin. The radioactivity of the peptides was found in the lysosomal range of density. According to our present and previous results, the renal pathway of the protease inhibitor consists of 3 steps: binding to the brush border, reabsorption into micropinocytotic vesicles and phagosomes, and final enrichment in phagolysosomes with subsequent degradation. We suggest this type of transport to be representative for peptides in general.
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PMID:In vivo interaction of the Kunitz protease inhibitor and of insulin with subcellular structures from rat renal cortex. 107 84

Serum gamma-glutamyltransferase is used as a marker of hepatic enzyme induction. The kidney contains high activities of gamma-glutamyltransferase in the brush border membrane of the proximal tubule, from which it is released into urine. This study investigated the effect of phenobarbital and antipyrine, two inducers of hepatic monoxygenases and gamma-glutamyltransferase, on the urinary excretion of renal gamma-glutamyltransferase. Three groups (n = 6) of healthy male volunteers received 100 mg phenobarbital for 7 and 14 days and 1200 mg antipyrine for 7 days, respectively. Antipyrine and phenobarbital increased antipyrine elimination, serum gamma-glutamyltransferase, and the urinary excretion of renal gamma-glutamyltransferase, whereas urinary beta-N-acetylglucosaminidase, beta-glucuronidase, and total protein and glucose excretion were unchanged. No correlation was found between serum and urinary gamma-glutamyltransferase or both enzymes and antipyrine elimination. Increases in antipyrine elimination were positively correlated to increases in serum, but not urinary gamma-glutamyltransferase. The findings suggest that antipyrine and phenobarbital increase urinary gamma-glutamyltransferase excretion. However, the increase in urinary gamma-glutamyltransferase does not reflect the magnitude of hepatic enzyme induction.
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PMID:Effect of antipyrine and phenobarbital on renal gamma-glutamyltransferase excretion in human urine. 197 43

The distribution of enzymes and laminin was examined in ileal tissue from pigs suffering from intestinal adenomatosis to reveal the nature of the lesion. A disruption of the normal and specific pattern of distribution was found. Thus, the normal ileal epithelium was characterised by brush border enzymes: alkaline phosphatase, magnesium-dependent adenosine triphosphatase (Mg-ATPase), fluoride resistant acid phosphatase and 5'-nucleotidase; enzymes of the basolateral border: Mg-ATPase; and cytoplasmic enzymes: beta-glucuronidase, non-specific esterase and acid phosphatase. Subepithelial fibroblasts seemed to be characterised by 5'-nucleotidase. Laminin was present as a continuous band under the surface and crypt epithelium, somewhat thicker in the former. In contrast, the branching proliferating crypts of intestinal adenomatosis largely lacked enzymes characteristic of both villus and crypt cells. Reactions for the subepithelial components, laminin and fibroblasts were also reduced. The deficient differentiation of the epithelial as well as subepithelial components in porcine intestinal adenomatosis distinguish the condition from crypt hyperplasia and indicate an adenoma-like character.
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PMID:Cell differentiation in intestinal adenomatosis of pigs studied by histochemistry of laminin and enzymes of epithelial and subepithelial tissue. 214 4

The urinary secretion of two lysosomal enzymes, N-acetyl-D-glucosaminidase (NAG, EC 3.2.1.30) and beta-glucuronidase (GLR, EC 3.2.1.31), and two brush border enzymes, alanine aminopeptidase (AAP, EC 3.4.11.2) and gamma-glutamyltransferase (GGT, EC 2.3.2.2), was examined in apparently healthy individuals and in patients before and after renovascular surgery for treatment of hypertension. Eight out of nine patients had elevated levels of at least one enzyme before surgery. The ranking in their frequency of elevation was NAG greater than AAP greater than GLR greater than GGT. In comparing the release of any two enzymes in apparently healthy individuals, the release was coordinated except for GGT and GLR. In individual patients following surgery the excretion of the lysosomal enzymes was highly coordinated whereas the release of the brush border enzymes was less coordinated. Comparisons of lysosomal to brush border enzyme activities revealed dissimilar release patterns between these two classes of enzymes. Analysis of variance over the entire hospitalization period showed that NAG/GLR (p = 0.42) and AAP/GGT (p = 0.12) did not vary significantly whereas all comparisons of lysosomal to brush border enzymes varied significantly (p less than or equal to 0.03). These results indicate that enzymes derived from different subcellular organelles, lysosomes or brush borders, have similar release patterns. However, the lack of a significant correlation between lysosomal and brush border enzyme excretion implies that the two processes are not interdependent. These studies further suggest that the transient pathophysiological changes that occur within renal cells following renovascular surgery affect these cellular components in different ways.
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PMID:A lack of coordination in the release of urinary lysosomal and brush border enzymes following renovascular surgery. 257 67

Renal toxicity is the major side effect of cis-dichlorodiammine platinum (CDDP) and it develops renal tubular damage. In the present study, the acute changes of urinary beta-glucuronidase (beta-GL) and alkaline phosphatase (ALP) activities following CDDP administration as indicators of its toxicity were studied in 5 patients with urological malignant tumors. The activities were measured for 11 days continuously from the day before CDDP administration. In all cases, both urinary enzyme activities increased with CDDP administration. Increase patterns of urinary beta-GL activities were similar to those of urinary NAG, but remarkably-high values of beta-GL activities were found in cases of urothelial tumors probably because urinary beta-GL derives from the kidney (lysosomes of tubular cells) and from the epithelial cells of urinary tract. Urinary ALP activities changed corresponding well with urinary gamma-glutamyl transpeptidase (gamma-GTP). This study shows that the determination of urinary beta-GL is not a significant marker of CDDP renal toxicity, especially in cases with urological malignancies, in contrast to results for urinary brush border enzyme activities such as ALP or gamma-GTP.
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PMID:[Study on urinary beta-glucuronidase and alkaline phosphatase activities as indicators of CDDP renal toxicity]. 272 12

The distribution of a number of membrane proteins on plasmalemmal microdomains (microvilli, coated pits) and in endosomes and lysosomes of the proximal tubule epithelial cell was determined in normal rat kidneys by immunofluorescence and immunoelectron microscopy. Two major brush border proteins, 130 and 94 kD, and gamma-glutamyl transpeptidase were detected on the membranes of the microvilli but were not found on membranes of coated pits. Gp330, the Heymann nephritis antigen, and clathrin were localized in coated pits. The lysosomal membrane glycoprotein, lgp120 (Lewis, V., S. A. Green, M. Marsh, P. Vihko, A. Helenius, and I. Mellman, 1985, J. Cell Biol., 100: 1839-1847) was restricted to lysosomes where it co-localized with beta-glucuronidase. Endosomes, identified by preloading with HRP injected 5-15 min before rats were killed, did not contain detectable amounts of any antigen tested. The distribution of the same proteins was also determined in rats given sodium maleate, which is known to slow or reduce protein absorption by the proximal tubule and to cause vacuolation of the endocytic apparatus. After maleate treatment the distribution of microvillar and lysosomal markers was unchanged, but the coated pit markers were redistributed--gp330 was concentrated in newly formed apical vacuoles, and clathrin was diffusely distributed in the apical cytoplasm or on apical coated vesicles. These findings indicate that the membrane composition of microvilli, coated pits, endosomes, and lysosomes is distinctive in the proximal tubule cell; and that gp330, unlike other known coated pit membrane components, is not transferred to endosomes during endocytosis. After maleate treatment, the coated pits lose their clathrin coats, and the corresponding membrane is internalized.
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PMID:The membrane composition of coated pits, microvilli, endosomes, and lysosomes is distinctive in the rat kidney proximal tubule cell. 286

The mucosal enzyme activities of 11 marker enzymes from the brush border, basolateral membrane, and lysosomes of 45 patients with an active duodenal ulcer (DU) were determined by analysis of homogenized biopsy specimens obtained from the duodenal bulb and descending duodenum at endoscopy. They were compared with activities measured in 22 controls. In the duodenal bulb lactase (p less than 0.005), neutral-alpha-glucosidase (p less than 0.0005), and monoamine oxidase (p less than 0.0005) were significantly decreased in DU patients. In the descending duodenum all the brush border enzymes except sucrase were significantly decreased when compared with controls. DU patients with inflammation in the biopsy specimens from the duodenal bulb had decreased levels of lactase (p less than 0.05), sucrase (p less than 0.05), neutral-alpha-glucosidase (p less than 0.05), leucyl-beta-naphthylamidase (p less than 0.05), and acid phosphatases (p less than 0.05) when compared with DU patients with normal histology in this region. In the descending duodenum the activities of leucyl-beta-naphthylamidase (p less than 0.05) were decreased in patients with inflammation compared with those without such histologic changes. DU patients who had taken antacids before the investigation had decreased activities of lactase (p less than 0.05) in the descending duodenum when compared with those who had not taken antacids. Activities of lactase (p less than 0.005), sucrase (p less than 0.005), neutral-alpha-glucosidase (p less than 0.05), and acid beta-glucuronidase (p less than 0.0005) in the descending duodenum were significantly lower in smokers than in non-smokers with active DU.
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PMID:Enzyme activities in the duodenal mucosa in duodenal ulcer patients. 292 38

Comparative histochemical studies of glycosidase activity were carried out in Clonorchis sinensis, Eurytrema pancreaticum, Fasciola hepatica, Dipylidium caninum, Hymenolepis nana, Ascaris suum, Toxocara canis, Ancylostoma caninum, Trichuris vulpis and Dirofilaria immitis. The enzymes examined were: N-acetyl-beta-glucosaminidase (EC 3.2.1.30), beta-glucuronidase (EC 3.2.1.31) and beta-galactosidase (EC 3.2.1.23). There were variations in enzyme distribution and intensity among the species and also between trematodes and nematodes; no marked positive reaction for these enzymes occurred in cestodes. In some trematodes, the caeca, especially in the brush border, and the tegument, subtegumental cells and testes, were reactive to the enzymes. In nematodes, although there was variation in reactions among species, N-acetyl-beta-glucosaminidase and beta-galactosidase were localized in the hypodermis and lateral cords excluding the excretory canal, and coelomocytes, intestinal epithelium and the walls of the reproductive systems.
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PMID:Comparative histochemical studies of glycosidase activity in some helminths. 308 22

A series of mucosal enzymes were estimated by analysis of homogenized biopsy specimens from the lower duodenal flexure, obtained from 10 large-bowel carcinoma patients, 15 patients with morbid obesity, and 15 controls. In 11 subjects the distribution along the upper small intestine was determined. The activities of the brush border enzymes lactase (p less than 0.01), neutral-alpha-glucosidase (p less than 0.01), and alkaline phosphatase (p less than 0.05) were significantly lower in the large-bowel carcinoma patients than in the controls. In obese subjects significantly lower activities (p less than 0.05) were demonstrated for the basolateral membrane enzyme 5'-nucleotidase and the lysosomal enzymes N-acetyl-beta-D-glucosaminidase and acid beta-glucuronidase, when compared with those in controls. Compared with the enzyme levels of the duodenal bulb, significantly higher activities of a series of enzymes were demonstrated at both the lower duodenal flexure and the angle of Treitz.
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PMID:Influence of remote cancer and obesity on, and distribution of mucosal enzymes in, the upper small intestine. 377 58


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