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)

Changes in enzyme activities of the plasma membrane markers were examined during phagocytosis using guinea-pig polymorphonuclear neutrophils. Incubation of neutrophils with fresh serum-opsonized zymosan particles showed a significant reduction in leucine aminopeptidase activity, whereas 5'-nucleotidase and alkaline phosphodiesterase activities remained unchanged. Inactivation of leucine aminopeptidase activity was also observed by exposure of neutrophils to complement-opsonized zymosan particles, but not to non-opsonized zymosan, IgG-coated zymosan or polystyrene latex particles. Pretreatment of neutrophils with cytochalasin B, which prevents phagocytosis but not surface binding of particles, provoked inactivation to the same degree as when the cells were allowed to phagocytose the particles. However, the inactivation during phagocytosis was protected by serine protease inhibitors. These findings suggest that loss of leucine aminopeptidase activity from phagocytosing cells may be mediated by certain serine protease inhibitor-sensitive factor(s) which are probably activated by the attachment of an opsonized zymosan particle to a specific membrane receptor, probably the C3b receptor.
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PMID:Inactivation during phagocytosis of leucine aminopeptidase, an ecto-enzyme of polymorphonuclear neutrophils. 731 56

Salivary gland transcriptome analysis of the Asiatic Triatoma rubrofasciata was performed by high-throughput RNA sequencing. This analysis showed that the majority of reads accounting for 85.38% FPKM (fragments per kilobase of exon per million mapped fragments) were mapped with a secreted class. Of these, the most abundant subclass accounting for 89.27% FPKM was the lipocalin family. In the lipocalin family, the most dominant molecules making up 70.49% FPKM were homologues of procalin, a major allergen identified from T. protracta saliva, suggesting an important role in blood-sucking of T. rubrofasciata. Other lipocalins showed similarities to pallidipin and triplatin, inhibitors of collagen-induced platelet aggregation identified from T. pallidipennis and T. infestans, respectively, Td38 from T. dimidiata with unknown function, triatin-like lipocalin with unknown function, and triafestin, an inhibitor of the activation of the kallikrein-kinin system, identified from T. infestans saliva. Other than lipocalin family proteins, homologues of antigen-5 (3.38% FPKM), Kazal-type serine protease inhibitor (1.36% FPKM), inositol polyphosphate 5-phosphatase (1.32% FPKM), and apyrase/5'-nucleotidase (0.64% FPKM) were identified as abundant molecules in T. rubrofasciata saliva. Through this study, de novo assembly of 42,580,822 trimmed reads generated 35,781 trinity transcripts, and a total of 1,272 coding sequences for the secreted class were deposited in GenBank. The results provide further insights into the evolution of salivary components in blood-sucking arthropods.
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PMID:Salivary gland transcriptome of the Asiatic Triatoma rubrofasciata. 3250 96