Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cytochemical changes were studied in leukocytes in peripheral blood smears from rabbits chronically exposed to mercury vapor. Experimental animals were exposed in a toxicologic chamber to air containing metallic mercury in concentrations of 2.0-2.5 mg/m3 for 3 hours daily over 12 weeks. In the poisoned rabbits, as compared with controls, alkaline phosphatase activity was depressed in granulocytes, and lactate dehydrogenase activity in granulocytes and lymphocytes. The activities of acid phosphatase, arylsulphatase, 5'-nucleotidase, the color reaction with Sudan black B and the p.a.S. reaction were not affected.
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PMID:Cytochemical abnormalities of the leukocytes of peripheral blood of rabbits in chronic experimental intoxication with mercuric vapors. 122 12

Our aim was to contribute to the understanding of the synthesis, maturation and activation of lysosomal enzymes in an invertebrate cellular model: the endo-lysosomal system (ELS) of mussel digestive cells. The activities of 5'-nucleotidase (AMPase), arylsulphatase (ASase) and acid phosphatase (AcPase), which are transported towards acidic compartments as membrane proteins, were localised by enzyme cytochemistry. AcPase activity was found within large heterolysosomes and residual bodies. ASase was located in endosomes, endolysosomes and heterolysosomes. AcPase and ASase activities were recorded within small vesicles and cisterns of the trans-Golgi network. Conversely, AMPase activity was primarily found in microvilli and apical vesicles and, less conspicuously, in lysosomes and the cis-side of the Golgi and the cis-Golgi network (CGN). In order to understand the processes of synthesis and maturation of these lysosomal enzymes, selected glycoconjugates were localised after lectin cytochemistry. N-acetylglucosamine, mannose and fucose residues were almost ubiquitous in the ELS, as were galactose residues, which were apparently less abundant. N-acetylglucosamine residues occurred in the inner membrane co-localised with mannose residues within the lysosomal and pre-lysosomal acidic compartments. Based on these results, glycosylation and sorting pathways are proposed for both soluble and membrane enzymes. Unlike in mammalian cells, O-glycosylation is fully completed in the CGN, mannose addition in N-glycosylation extends beyond the CGN and galactose addition is fully achieved at the intermediate side. Sorting of soluble lysosomal enzymes, as in crustaceans, is mediated by the indirect transport of membrane-linked proteins with GlcNAc1-P6Man residues that are removed in endolysosomes and heterolysosomes.
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PMID:Glycosylation and sorting pathways of lysosomal enzymes in mussel digestive cells. 1645 Jan 24