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:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the human adenocarcinoma cell line Caco-2 a substantial amount of a precursor form of the lysosomal enzyme alpha-glucosidase is not segregated into lysosomes, but instead secreted from the apical membrane. In this study we addressed the question whether this process is mediated by mannose 6-phosphate receptors. The subcellular distribution of the cation-independent mannose 6-phosphate receptor was studied by means of electron microscopic immunocytochemistry. The bulk of label was found in the perinuclear region in electron-lucent and dense vesicles, some of the latter bearing a coat. Receptor-containing dense vesicles were also found throughout the cytoplasm. In the apical part of the cells, label for the receptor was present over the surrounding membrane and the interior vesicles of multivesicular bodies, but not over lysosomes. Label on the plasma membrane was mainly restricted to the apical domain. In contrast to alpha-glucosidase, the secreted forms of the lysosomal enzymes cathepsin D, beta-hexosaminidase and beta-glucuronidase are mainly found in the basolateral medium. Enzyme activity measurements and immunoprecipitation of metabolically labeled cells showed that incubation with NH4Cl leads to an enhanced secretion of these enzymes into the basolateral medium, but has no effect on the basolateral secretion of alpha-glucosidase. In addition, NH4Cl caused a minor decrease in the secretion of these enzymes from the apical side and had little or no effect on the secretion of alpha-glucosidase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The cation-independent mannose 6-phosphate receptor is not involved in the polarized secretion of lysosomal alpha-glucosidase from Caco-2 cells. 132 37

The study was designed to evaluate (a) the role of reduced renal phosphate reabsorptive capacity assessed as the ratio of maximum capacity for renal phosphate reabsorption (TmPO4) to glomerular filtration rate (GFR) in the pathogenesis of hypophosphatemia in alcoholics, (b) possible mechanisms leading to reduced TmPO4/GFR, and (c) the effect of liver function impairment on TmPO4/GFR. The TmPO4/GFR, its major extrarenal determinants, ratios of urinary excretion gamma-glutamyl transpeptidase and of alpha-glucosidase to GFR (uGGT/GFR and uAGL/GFR), indices of structural damage of renal tubular cells, and fractional clearance of lysozyme, an index of proximal renal function, were evaluated in 31 alcoholics with alcohol-related liver disease, 24 alcoholics without alcohol-related liver disease, 14 patients with non-alcohol-related liver disease, and 25 control subjects. Hypophosphatemia was found in 35% of alcoholics with alcohol-related liver disease, 29% of alcoholics without alcohol-related liver disease, and no patients with non-alcohol-related liver disease. A reduced TmPO4/GFR was the major determinant of hypophosphatemia in both groups of alcoholics. No difference in extrarenal determinants of TmPO4/GFR was found between alcoholics with and without hypophosphatemia. Alcoholics with and without alcohol-related liver disease had increased uGGT/GFR and normal uAGL/GFR regardless of serum phosphate level. Fractional clearance of lysozyme, instead, was increased only in hypophosphatemic alcoholics with and without alcohol-related liver disease. The TmPO4/GFR correlated inversely with the fractional clearance of lysozyme in both groups of alcoholics (P less than 0.01). The TmPO4/GFR and urinary enzymes were normal in patients with non-alcohol-related liver disease. It was concluded that a reduced TmPO4/GFR is involved in the pathogenesis of hypophosphatemia in alcoholics. A proximal tubular dysfunction seems to be responsible for the reduced TmPO4/GFR. Liver function impairment is not required for the expression of this tubular dysfunction.
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PMID:Hypophosphatemia and renal tubular dysfunction in alcoholics. Are they related to liver function impairment? 172 78

Various aspects of lysosome biogenesis have been studied in Chinese hamster ovary (CHO) cells of the End3 complementation group (designated G.7.1 cells), which display a temperature-sensitive defect in the acidification of endosomes, but not lysosomes. In G.7.1 and normal wild-type cells grown at the permissive temperature (34 degrees C), the lysosomal enzymes alpha-glucosidase and cathepsin D were synthesized as high-molecular-weight precursors that subsequently underwent intracellular proteolytic processing to yield lower molecular weight mature forms. The mature forms of the enzymes were retained in cells, and small amounts of each precursor were secreted. However, in G.7.1 cells grown at the restrictive temperature (41 degrees C), there was a massive and inappropriate oversecretion of lysosomal enzyme precursors, which resulted in very little of the mature forms being processed and retained by the cells. This mistargeting of lysosomal enzymes was not due to an absence of phosphorylated oligosaccharides on the enzymes, nor to a defect in mannose 6-phosphate (Man6P) receptors. However, it was found that whereas G.7.1 cells had the same number of cell surface Man6P receptors at 34 degrees C and 41 degrees C, the rate of accumulation and degradation of Man6P-containing ligands was about two to three times more rapid in cells maintained at the permissive temperature. There did not appear to be any gross changes in Golgi function as the oligosaccharides of alpha-glucosidase and the Man6P receptor were processed in a similar fashion at both 34 degrees C and 41 degrees C. In addition to these studies, electron microscopic observations revealed that at 41 degrees C, G.7.1 cells accumulated inclusion-type bodies reminiscent of those found in I-cell disease fibroblasts. Thus, the biochemical and electron microscopic results on G.7.1 cells provide further evidence that acidified endosomes are important for the biogenesis of lysosomes.
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PMID:Biosynthesis of lysosomal enzymes in cells of the End3 complementation group conditionally defective in endosomal acidification. 184 19

Gentamicin nephrotoxicity is associated with impairments in proximal tubular function. This study determined whether gentamicin administration to the rat, before a reduction in glomerular filtration rate (GFR), causes early and selective alterations in renal cortical brush-border membrane (BBM) enzyme and transport activity, lipid composition, and fluidity. Three days of gentamicin administration caused significant decreases in the Vmax of alkaline phosphatase, the Vmax of sodium gradient-dependent phosphate transport (Na-Pi cotransport), and the Vmax of pH gradient-dependent sodium transport (Na-H exchange). Gentamicin did not affect BBM-bound maltase or leucine aminopeptidase activities and sodium gradient-dependent glucose or proline transport activities. Gentamicin also caused a significant decrease in BBM sphingomyelin, significant increases in BBM phosphatidylcholine and phosphatidylinositol, a significant decrease in the phospholipid fatty acid saturation index, and a significant increase in BBM fluidity, i.e., decrease in the fluorescence anisotropy of diphenylhexatriene. These BBM functional and compositional effects of gentamicin were independent of endogenous parathyroid hormone activity. We conclude that gentamicin causes early and specific alterations in BBM enzyme and transport activity and also lipid composition, which may play an important role in the progression of renal cell injury.
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PMID:Early selective effects of gentamicin on renal brush-border membrane Na-Pi cotransport and Na-H exchange. 215 23

Experiments were conducted to establish a stunting syndrome (SS) model to facilitate research on nutritional aspects of enteric disorders of poults. One-day-old turkeys were dosed per os with tryptose phosphate broth (TPB) (controls) or inoculum (inoculated). The inoculum was prepared by homogenizing intestines from 11-day-old commercial poults diagnosed to have SS in TPB (1:0.5 [wt:wt]). Subsequently, intestines from 8-day-old inoculated poults from the previous experiment were used. Inoculation reduced growth (P less than 0.001) and feed consumption (P less than 0.001) at 8 and 14 days of age. In Expts. 1, 2, and 3, gain of inoculated poults was 60.9%, 58.8%, and 52.6% that of controls up to 8 days of age and 77.9%, 76.6%, and 80.9% that of controls from 8 to 15 days of age, respectively. Feed conversion was impaired (P less than 0.001) up to 8 days of age. The activity of maltase and sucrase in the jejunum and of pancreatic enzymes was determined every 2 days up to 13 days of age. Inoculation decreased (P less than 0.001) maltase and sucrase starting at 3 days of age (i.e., maltase activity was 17.45 and 1.70 mumols maltose hydrolyzed/hr.mg protein in control and inoculated poults, respectively). Inoculation had no effect on pancreatic lipase, amylase, or trypsin.
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PMID:Stunting syndrome in turkeys. Development of an experimental model. 219 47

Enzymatic transglucosylation from maltose to L-ascorbic acid (AA) with mammalian tissue homogenates was determined by a high-performance liquid chromatography method and compared with the reaction catalyzed by alpha-glucosidase from Aspergillus niger. The homogenates of small intestine and kidney had a high transglucosylase activity to form a new type of glucosylated AA, which was associated with alpha-glucosidase activity. The new compound was demonstrated to be an equimolar conjugate of AA and glucose by the spectral and quantitative analyses. In particular, it showed a high stability in a neutral solution and no reducing activity toward cytochrome c and a dye. These properties were very different from those of AA and L-ascorbic acid alpha-glucoside formed with alpha-glucosidase from A. niger, but they were consistent with those of L-ascorbic acid 2-O-phosphate and L-ascorbic acid 2-O-sulfate. Moreover, it exhibited a reducing power associated with AA after mild acid hydrolysis or treatment with rat intestinal alpha-glucosidase. These results indicate that it should be assigned the 2-O-alpha-glucoside structure. Consequently, it is concluded that mammalian alpha-glucosidase is able to form a very stable and nonreducing form of glucosylated AA through a specific transglucosylation reaction distinct from that of microbial alpha-glucosidase.
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PMID:Formation of a stable L-ascorbic acid alpha-glucoside by mammalian alpha-glucosidase-catalyzed transglucosylation. 220 May 20

Phosphoglycans from the cell wall of many strains of Streptococci contain terminal carbohydrate units linked by phosphodiester bridges to other residues of the glycans. In the immune response to phosphoglycans, the terminal carbohydrate-phosphate moieties function as antigenic determinants and induce the synthesis of antibodies with specificity for the glycosyl-phosphoryl units. It has now been found that such terminal carbohydrate units can be removed by treatment of the glycans with appropriate glycosidases. Thus, an almond beta-glucosidase releases glucose from a streptococcal Group D phosphoglycan with beta-glucosyl phosphate units, a jack bean N-acetyl-beta-glucosaminidase releases N-acetylglucosamine from a streptococcal Group L phosphoglycan with N-acetyl-beta-glucosaminyl phosphate units, and a rice alpha-glucosidase releases glucose from a yeast phosphoglycan with alpha-glucosyl phosphate units. The glycosidases also hydrolyze the hexose phosphates of the proper anomeric configuration and structure. The preparations of glycosidases used in this study exhibit specificity for single types of carbohydrate residues and are devoid of phosphatase and phosphodiesterase activities. The glycosidases act on glycosyl-phosphoryl linkages by a stereospecific mechanism and can therefore be used for the determination of the anomeric configuration of glycosyl-phosphoryl units of complex carbohydrates.
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PMID:The determination of the anomeric configuration of glycosyl-phosphoryl linkages of immunogenic phosphoglycans. 240 37

Some days after the administration of a third bolus of ABVD (adriamycin, bleomycin, vinblastine, dacarbazine) a patient affected by immunoblastic lymphoma underwent a neurotoxic crisis. The episode lasted 1 week and was followed by a dramatic fall in plasma sodium (104 mEq I-1), associated with a proportionally lesser decrease in plasma chloride and phosphate. Despite the lowest plasma osmolality, detectable levels of circulating ADH were present. After 36 h the hyponatremic episode improved after the infusion of hypertonic sodium chloride. Nevertheless the patient lapsed into a hypotonic coma. The urinary concentrations of the main tubular enzymes (gamma-glutamyltranspeptidase, N-acetyl-glucosaminidase, alpha-glucosidase) proved very high and successively decreased slowly. The most likely cause of such hyponatremic episode is vinblastine. The drug acted through: (a) an already known inappropriate release of ADH, and (b) a hitherto unreported tubular lesion, which impaired the reabsorption of sodium and other coupled solutes.
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PMID:Life-threatening hyponatremia caused by vinblastine. 245 36

1. Brush border membrane vesicles were prepared from lamb enterocytes. These were used to study the changes in the enzyme contents and the transport capacities which occur during the change from a milk to a roughage diet. 2. Na+-dependent transport of D-glucose was present in all regions of the small intestine of pre-ruminant lambs and absent in ruminants. 3. Na+-dependent transport of L-proline was present in all regions of the small intestine irrespective of the age of the animal. 4. Phosphate transport was seen only in the presence of a transmembrane pH gradient (acid outside). The transport was not stimulated by either Na+ or K+. The transport capacity increases 2-fold as the animal becomes ruminant. 5. The activities of lactase and maltase diminished with age. Alkaline phosphatase and aminopeptidase N activities remain constant. Sucrase activity cannot be detected in lambs of any age.
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PMID:Changes in the functions of the intestinal brush border membrane during the development of the ruminant habit in lambs. 251 73

Cultured human renal cortical epithelial cells (NHK-C) were examined for functional and morphologic characteristics of the proximal tubule. Cultures were established by using cells isolated by progressive enzymatic dissociation from the extreme outer cortex of the normal human kidney. Cells were subcultured and used at passages 3 through 8. Cell uptake of alpha-methyl-D-glucoside (AMG), inorganic phosphate (Pi) and L-alanine was found to be dependent on the presence of Na+ in the incubation medium, and uptake increased with incubation time up to 30 minutes. Na+-dependent AMG uptake was inhibited 67% by phlorizin (1 mmol/L), and Pi uptake was inhibited 89% by parathyroid hormone (PTH) (10(-6) mol/L). Intracellular cyclic adenosine monophosphate was increased 28-fold after exposure to 10(-6) mol/L PTH but was increased only 2-fold by the same concentration of vasopressin. The cells exhibited endocytotic activity and possessed maltase, leucine aminopeptidase, and gamma-glutamyltranspeptidase, enzymes located exclusively in the brush border membranes of proximal tubule cells. NHK-C cultures were structurally heterogeneous, made up of a mixed-cell population with predominant epithelial-like morphology. Epithelial cells had cuboidal form, solitary cilia, and short, irregularly distributed apical microvilli. These cultures also formed multicellular hemicysts, but only through passage 3. NHK-C cultures showed a dramatic attenuation of proliferative activity at passages 8 through 10. These data show that subcultured cells derived from the outer cortex of the normal human kidney retain a number of functional characteristics typical of the proximal tubule.
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PMID:Proximal tubule characteristics of cultured human renal cortex epithelium. 253 26


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