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)

In the female urethra, the activity and distribution of 15 enzymes was determined by using both conventional and special histochemical methods. The enzymatic equipment differed according to the type of epithelial lining whose variation is characteristic for the female urethra. In the stratified squamous epithelium of the urethra, alkaline phosphatase, beta-glucuronidase, acetyl-beta-D-glucosaminidase, thiamine pyrophosphatase, and glucose-6-phosphatase exhibited but minimal or no activity, yet the other 10 enzymes studied displayed activity particularly in basally situated cells. Nearer to the lumen of the urethra, the activity in the epithelium kept decreasing and was mostly absent in superficial and desquamated cells. In the pseudostratified columnar and in the transitional epithelium of the urethra, the majority of enzymes showed an evenly distributed activity at all epithelial levels. In the apical parts of the most superficially situated cells bounding the lumen of the urethra, a distinct narrow zone of higher activity was observed. It was seen not only on determining the majority of dehydrogenases but also on examining acid phosphatase and naphthyl esterase. The endocrine cells occurring in the uroepithelial lining of the female urethra displayed, yet always with the exception of squamous epithelium (Zaviacic et al. 1983), distinct activity of acid hydrolytic enzymes, and of the enzymes studied it was particularly acid phosphatase. The majority of the demonstrated enzymes, of the dehydrogenases priority, is to be given to succinate dehydrogenase, enabled to differentiate readily between the highly active striated muscle fibers located in the most peripheral parts of the excisions along the urethral circumference and the smooth musculature of the urethral wall with a lower or only minimal activity.
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PMID:The adult human female urethra. Enzyme-histochemical study. 242 Jan 38

Activity changes of thiamine pyrophosphatase (TPPase), acid phosphatase (aP), non-specific esterase (nE), acid beta-galactosidase (a beta Gal), beta-glucuronidase (beta-Gluc), and beta-D-N-acetylglucosaminidase (NAG) in follicles during atresia were investigated in the ovaries of mice, rats, Mongolian gerbils, hamsters, guines pigs, rabbits, cats, and pigs. Changes of hydrolase activity were highly enzyme dependent, species-specific and mostly confined to the granulosa. Decrease of TPPase activity and increase of lysosomal enzyme activities during atresia appeared to be true for all mammals. The start of activity changes in the time course of atresia depended on the occurrence of the enzyme in the growing granulosa. Continuous increase of lysosomal enzyme activity appeared in follicles where these enzymes could also be found in the growing granulosa. In contrast, when lysosomal enzyme activity was low or could not be detected in the growing granulosa, increased enzyme activity could only be observed at a time when degenerative processes have already progressed considerably. This distribution pattern suggests that hydrolytic enzymes in the granulosa cells as well as hydrolases of invading macrophages participate in this degenerative process. In some mammals, enzyme activity changes appeared in the cumulus oophorus for the first time in advanced stages of degeneration. In some mammals enzyme activity changes were dependent on the developmental stage of the follicle. This stage dependency argues for an interrelationship between activation of lysosomal enzymes and androgen metabolism.
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PMID:Hydrolase cytochemistry during follicular atresia in mammals. 313 20

1. The conditions that promoted the solubilization of particulate lactose synthetase were effective for solubilizing the thiamine pyrophosphatase of the Golgi apparatus but differed from those effective for beta-glucuronidase or acid phosphatase of lysosomes. 2. Lactose synthetase-containing particles did not bind Mg(2+) or Cs(+) ions, suggesting that they are not related to endoplasmic reticulum membranes. 3. Intact lactose synthetase and thiamine pyrophosphatase particles banded isopycnically at a density of 1.143 in a sucrose gradient. The dissociated ;A' sub-unit of lactose synthetase, UDP-galactose hydrolase, p-nitrophenyl phosphate acid phosphatase, alkaline phosphatase and phosphodiesterase I were associated with particles of a broad density range from 1.12 to 1.20. Lysosomal enzymes beta-glucuronidase, arylsulphatase and beta-glycerophosphate acid phosphatase were associated with particles of density 1.20, 1.175 and 1.15 respectively. 4. Rate-zonal sedimentation studies indicated that lactose synthetase particles have S(20,w) values exceeding 24000s, corresponding to spherical particles of diameter exceeding 5.4x10(-5)cm. 5. Electron micrographs of lactose synthetase particles purified over 20-fold revealed small spherical bodies (0.1-0.5mu) resembling lysosomes, the smaller of which were attached to membranes, and larger heterogeneous spherical or oval bodies (0.7-1.8mu) resembling lipofuscin secretory granules. 6. The relationship between lactose synthetase particles and the Golgi origin of secretion granules is discussed.
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PMID:The lactose synthetase particles of lactating bovine mammary gland. Characteristics of the particles. 430 May 7

Subcellular fractions were prepared from mouse kidney homogenates by differential and sucrose-gradient centrifugation. A fraction enriched in Golgi apparatus was obtained, which had considerably enriched galactosyltransferase and thiamin pyrophosphatase activities, and was morphologically typical of Golgi material. This preparation also had high beta-glucuronidase activity, which increased concomitantly with microsomal beta-glucuronidase activity during the specific stimulation of the enzyme in male mouse kidney after androgen administration. The degree of stimulation was much greater in the Golgi fraction. Gel-electrophoretic patterns of Golgi beta-glucuronidase resembled more closely those of the enzyme located within lysosomes, but contained minor bands similar to those described previously (Swank & Paigen, 1973) as characteristic of the microsomal enzyme. It was concluded that the Golgi complex is involved in the distribution of the enzyme after its synthesis to both lysosomal and microsomal fractions.
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PMID:Golgi beta-glucuronidase of androgen-stimulated mouse kidney. 437 7

Studies on the activity of the glucuronic acid pathway in alloxan diabetic rabbits were carried out. Amount of D-glucaric acid, L-ascorbic acid, and D-glucuronic acid in urine increased in the case of the alloxan diabetic rabbits. The transformation from D-glucuronolactone to D-glucaric acid was higher than normal in the diabetic animals. The expired 14-CO2 decreased and urinary excretion of labeled L-gulonic acid increased after administration of 6-14-C-glucuronolactone in the diabetic rabbits. L-Gulonic acid dehydrogenase, lactonase II, and beta-glucuronidase activities were reduced, and UDPGA-pyrophosphatase, D-glucuronic acid-1-phosphatase, and UDPGA-transferase activities increased in the diabetic rabbit liver. From these results, it may be concluded that an increase of endogenous D-glucuronic acid in the diabetic states could be attributed to a metabolid defect in the step of L-gulonic acid dehydrogenation and to the enhancement of UDPGA-pyrophosphatase and D-glucuronic acid-1-phosphate phosphatase activities.
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PMID:Glucuronic acid pathway in alloxan diabetic rabbits. (I). Urinary excretion of metabolites related to the glucuronic acid pathway. 446 73

The lysosomal enzymes beta-glucuronidase and acid phosphatase were studied in 112 patients with cholecystitis. Acid phosphatase activity was generally lower in patients with cholesterol stones compared with cases with pigment stones. beta-glucuronidase activity was higher in acalculous cholecystitis than in any other group, a fact compatible with the concept that in lithiasis the enzyme is secreted into the bile and therefore may participate in nidus formation. Histochemistry at light microscopical level clearly demonstrates the lysosomal distribution of these enzymes and their presence in the macrophages infiltrating lamina propria in cholesterolosis. Electron histochemistry in 45 patients showed acid phosphatase activity in lysosomes and some in mucous droplets. Thiamine pyrophosphatase activity, a marker for the Golgi system, showed a close association with these mucous droplets. The secretion of mucus will be accompanied by a secretion of acid phosphatase, and by implication other acid hydrolases, into the bile.
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PMID:Gallbladder epithelial acid hydrolases in human cholecystitis. 613 Nov 15

The dietary addition of several xenobiotics, such as PCB, DDT, aminopyrine, chloretone, BHT and BHA, caused significant increases in the ascorbic acid in urine and liver of rats. The administration of all types of xenobiotics used in the present experiments increased the activity of hepatic UDP-glucose dehydrogenase (1.3-2.8-fold), and the administration of PCB, DDT, BHT or BHA significantly increased the activity of hepatic UDP-glucuronyl transferase (2.2-13.1-fold). The activity of beta-glucuronidase was slightly increased with feeding of PCB, DDT, chloretone or aminopyrine. However, the activity of hepatic UDP-glucuronic acid pyrophosphatase, the conversion of D-glucuronic acid or D-glucuronolactone into L-ascorbic acid and the activity of hepatic L-gulonolactone oxidase did not increase with the administration of PCB or DDT. It is suggested that the increases in the activities of UDP-glucose dehydrogenase and UDP-glucuronyl transferase would have a major role in the stimulation of ascorbic acid synthesis in xenobiotic treated rats.
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PMID:Effect of several xenobiotics on the activities of enzymes affecting ascorbic acid synthesis in rats. 613 23

1. Cutaneous UDP-glucuronosyltransferase activity (E.C.2.4.1.17) was demonstrated in rat- and hairless mouse-skin microsomes using 1-naphthol as substrate. 2. Addition of the detergent Brij 35 increased the activity by approximately twofold in both species. 3. Inhibitor studies demonstrated that under the assay conditions used any UDP-glucuronic acid pyrophosphatase or beta-glucuronidase present did not interfere with the conjugation reaction. 4. Substrate inhibition was observed in hairless mouse-skin preparations and biphasic response to increasing naphthol concentration was seen in rat-skin microsomes. 5. The apparent Km values were considerably lower than those reported for liver. The sp. activity (per mg microsomal protein) in unactivated rat-skin microsomes was about 50% of that reported in unactivated rat-liver microsomes. 6. Pretreatment with 3-methylcholanthrene resulted in a small increase in cutaneous UDP-glucuronosyltransferase activities in both species.
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PMID:UDP-glucuronosyltransferase activity in rat-and hairless mouse skin-microsomes. 681 5

Submandibular glands obtained post-mortem from mature ferrets of both sexes were examined with the use of light microscopical histochemical methods for proteins, mucosubstances and enzymes associated with cell functions or organelles. Demilunar cells showed carboxylated mucosubstances that were mainly non-sulphated, and diffuse activity for peroxidase, E600-sensitive esterase and acid phosphatase. Thiol groups were also detected in these cells. Central acinar cells showed sulphated mucosubstances, disulphides and reticular staining for thiamine pyrophosphatase. Intercalary ducts showed diffuse activity for NADH and NAD(P)H dehydrogenases. Striated ducts contained protein, tryptophan, disulphides, neutral mucosubstances and E600-sensitive esterase periluminally. Basally, the striated ductal cells showed variable activity for peroxidase, cytochrome oxidase, succinate dehydrogenase and acid phosphatase. Basolateral plasma membranes of these cells exhibited ouabain-sensitive Na,K-ATPase activity. The collecting ducts were characterized by variable periluminal staining for acid phosphatase, beta-glucuronidase, acid beta-galactosidase and E600-resistant esterase. The results suggest that the histological appearances of the acini of the submandibular gland of the ferret are dependent on the synthesis of secretory acid glycoproteins, that the striated ducts are involved with the secretion of tryptophan-rich product comprising neutral glycoproteins and showing esterase activity and with marked transport of ions and that the collecting ducts are involved with absorption.
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PMID:Morphological phenotypes and functional capabilities of submandibular parenchymal cells of the ferret investigated by protein, mucosubstance and enzyme histochemistry. 1066 22

Von Ebner's gland of ferret was examined by means of light microscopy, protein, mucosubstance and enzyme histochemistry, and neurohistology. Acinar cells were replete with granules containing neutral mucosubstances and disulphides, and showed strong diffuse acid phosphatase activity and weak granular staining for peroxidase. Staining for cytochrome oxidase, succinate dehydrogenase, and NADH and NAD(P)H dehydrogenases was also seen. Basolateral plasmalemma of acinar cells showed weak, ouabain-sensitive Na+,K+-ATPase activity. Ductal cells were of a simple appearance, contained thiols and showed variable staining for acid phosphatase, dehydrogenases and cytochrome oxidase. Variable amounts of beta-glucuronidase reaction product were localized in the glandular parenchyma, being marked in atrophic areas. Prominent stellate myoepithelial cells embracing acini and also basal ductal cells were demonstrated by alkaline phosphatase. Thiamine pyrophosphatase reaction product was concentrated in blood vessels around parenchyma, with little Golgi-like staining in acinar cells. Acetylcholinesterase activity was associated with an extensive network of nerve fibres embracing parenchyma, whereas catecholamine fluorescence was not seen. The results suggest that the acini of von Ebner's gland of ferret synthesise neutral secretory glycoproteins and peroxidase. Water mobilization is inconspicuous. Lysosomal activities feature in the parenchyma, possibly a consequence of processing secretory products in acini, absorption in ducts and/or adaptation atrophy. The gland receives a rich cholinergic-type innervation, and has extensive myoepithelial and microvascular networks.
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PMID:Histochemical phenotypes of von Ebner's gland of ferret and their functional implications. 1150 41


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