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)

The differential effects of phagocytic and chemical stimuli on neutrophil enzyme and specific protein release were compared. Phorbol myristate acetate (PMA) stimulated release of the specific granule matrix marker, vitamin B-12-binding protein in a dose-dependent manner. Subcellular fractionation by sucrose density gradient centrifugation indicated that the residual vitamin B-12-binding protein is associated with the specific granule fraction. In contrast, neutral alpha-glucosidase and adenosine diphosphatase, associated with specific granule membranes, were not released by PMA. Subcellular fractionation studies suggest that fusion of the specific granule membrane and plasma membrane occurs, thus translocating the adenosine diphosphatase to the cell surface. The relevance of this finding to the possible role of nucleoside phosphatases in limiting platelet aggregation is discussed. Serum-treated zymosan particles also caused a selective release of vitamin B-12-binding protein from the specific granule without release of alpha-glucosidase and adenosine diphosphatase. Neither PMA nor opsonized zymosan caused significant release of azurophil, tertiary granule or cytosol marker enzymes.
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PMID:The release of granule components from human polymorphonuclear leukocytes in response to both phagocytic and chemical stimuli. 715 Jun 43

An apyrase and an alpha-glucosidase were detected in the salivary glands extracts of adult Aedes albopictus. The apyrase is a 61,000 Da secreted protein that hydrolyses ATP and ADP. This protein is synthe-sized in adults and is preferentially accumulated in the distal lateral lobes of the female salivary glands. The alpha-glucosidase is a secreted 67,000 Da protein. This enzyme is synthesized during adult life and accumulated in the proximal-lateral lobes of both males and females. The results are discussed and compared with data previously obtained with Aedes aegypti salivary glands.
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PMID:Apyrase and alpha-glucosidase in the salivary glands of Aedes albopictus. 892 36

Adult Anopheles darlingi salivary glands are paired organs located on either side of the esophagus. The male glands consist of a single small lobe. The female gland is composed of two lateral lobes, with distinct proximal and distal portions, and a medial lobe. The lobes are acinar structures, organized as a unicellular epithelium that surrounds a salivary canal. The general cellular architecture is similar among the lobes, with secretory material appearing as large masses that push the cellular structures to the periphery of the organ. Cells of the proximal-lateral lobes show asynchronous cycles of secretory activity and contain secretory masses with finely filamentous aspect. In the distal-lateral lobes, cells display synchronous cycles of activity, and have a dense secretory product with mottled pattern. Cells of the medial lobe have secretory masses uniformly stained and highly electrondense. Biochemical analysis of the adult female salivary glands revealed apyrase, alpha-glucosidase and lysozyme activities. Alpha-glucosidase and lysozyme activities are detected mostly in the proximal lobes while apyrase is mainly accumulated in the distal lobes. This differential distribution of the analyzed enzymes reflects a specialization of different regions for sugar and blood feeding. Thus, the morphological differences observed in the lobes correlate with functional ones.
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PMID:Morphological and biochemical analyses of the salivary glands of the malaria vector, Anopheles darlingi. 1048 Dec 98

Several properties of the salivary glands of Culex quinquefasciatus mosquitoes were analysed. The amount of protein in female salivary glands increased from 0.26 microg on day one after emergence to about 1.4 microg on day seven. The major polypeptides found in the female salivary glands had molecular weights of 35.7, 28.3, and 20.5 kDa. Antibodies produced by mice immunized by bites of Culex quinquefasciatus female mosquitoes reacted with the 35.7 and 28.3 kDa polypeptides, showing that these molecules were secreted by mosquitoes during blood feeding. The salivary glands of C. Quinquefasciatus females displayed the same morphological and biochemical organization as that of Aedes aegypti mosquitoes, accumulating apyrase in the distal portions and alpha-glucosidase in the proximal portions of the gland. Arch.
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PMID:Salivary gland proteins of the mosquito Culex quinquefasciatus. 1061 58

Salivary gland proteins of the human malaria vector, Anopheles dirus B were determined and analyzed. The amount of salivary gland proteins in mosquitoes aged between 3--10 days was approximately 1.08 +/- 0.04 microg/female and 0.1 +/- 0.05 microg/male. The salivary glands of both sexes displayed the same morphological organization as that of other anopheline mosquitoes. In females, apyrase accumulated in the distal regions, whereas alpha-glucosidase was found in the proximal region of the lateral lobes. This differential distribution of the analyzed enzymes reflects specialization of different regions for sugar and blood feeding. SDS-PAGE analysis revealed that at least seven major proteins were found in the female salivary glands, of which each morphological region contained different major proteins. Similar electrophoretic protein profiles were detected comparing unfed and blood-fed mosquitoes, suggesting that there is no specific protein induced by blood. Two-dimensional polyacrylamide gel analysis showed the most abundant salivary gland protein, with a molecular mass of approximately 35 kilodaltons and an isoelectric point of approximately 4.0. These results provide basic information that would lead to further study on the role of salivary proteins of An. dirus B in disease transmission and hematophagy.
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PMID:Salivary gland proteins of the human malaria vector, Anopheles dirus B (Diptera: Culicidae). 1738 13