Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To assess the effect of eicosapentaenoic acid (EPA) intake on fibrinolysis and coagulation, 30 male subjects, approximately 19-23 y old, were examined for plasma fibrinolytic and coagulation activity by using a bicycle ergometer load (90 W, 20 min) before and after EPA intake of 1.125 g/d for 2 wk. Because of the EPA intake, the fibrinolytic activity was promoted, the plasmin-alpha 2 plasmininhibitor complex (PIC) level was decreased by 16.7%, and the thrombin-antithrombin III complex (TAT) level was increased by 75.4%; conversely, the D-dimer of the fibrin degradation peptide (D-dimer) level did not change from that before EPA intake. By the physical load, 1 h after ingesting the load, the PIC level was significantly decreased by 26.7%, the TAT level was significantly increased by 51.1%, and the D-dimer level was significantly decreased by 24% in comparison with levels before EPA intake. Thus, as determined by the load, a small amount of daily EPA intake clearly decreased fibrinolytic activity and increased coagulation activity. One hour after a physical load, the rate of change of the gamma-glutamyl transpeptidase (gamma-GTP) level correlated significantly and negatively to the rate of change in the PIC and TAT levels. Thus, EPA intake may affect liver and kidney function. EPA intake decreased systolic blood pressure by 5 mmHg and diastolic blood pressure by 10 mmHg.
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PMID:Effects of eicosapentaenoic acid intake on plasma fibrinolytic and coagulation activity by using physical load in the young. 1067 28

The molecular bases of the host-parasitoid interactions in the biological system Acyrthosiphon pisum (Harris) (Homoptera, Aphididae) and Aphidius ervi (Haliday) (Hymenoptera, Braconidae) have been elucidated allowing the identification of a gamma-glutamyl transpeptidase, the active component of maternal venom secretion, and teratocytes, the embryonic parasitic factors responsible for host physiology regulation after parasitization. Teratocytes, cells deriving from the dissociation of the serosa, the parasitoid embryonic membrane, are responsible for extra-oral digestion of host tissues in order to provide a suitable nutritional environment for the development of parasitoid larvae. Teratocytes rapidly grow in size without undergoing any cell division, synthesize, and release in the host hemolymph two proteins: a fatty acid binding protein (Ae-FABP) and an enolase (Ae-ENO). Ae-FABP is involved in transport of fatty acids deriving from host tissues to the parasitoid larva. Ae-ENO is an extracellular glycolytic enzyme that functions as a plasminogen like receptor inducing its activation to plasmin. Both Ae-FABP and Ae-ENO lack their signal peptides, and they are released in the extracellular environment through an unknown secretion pathway. Here, we investigated the unconventional mechanism by which teratocytes release Ae-FABP and Ae-ENO in the extracellular space. Our results, obtained using immunogold staining coupled with TEM and western blot analyses, show that these two proteins are localized in vesicles released by teratocytes. The specific dimension of these vesicles and the immunodetection of ALIX and HSP70, two exosome markers, strongly support the hypothesis that these vesicles are exosomes.
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PMID:Aphidius ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles. 3127 55