Inhibition of human platelet aggregation by eosinophils

dc.creatorMaziero, AM
dc.creatorLorenzetti, R
dc.creatorDonato, JL
dc.creatorLilla, S
dc.creatorDe Nucci, G
dc.date2013
dc.dateSEP 17
dc.date2014-08-01T18:32:55Z
dc.date2015-11-26T17:59:53Z
dc.date2014-08-01T18:32:55Z
dc.date2015-11-26T17:59:53Z
dc.date.accessioned2018-03-29T00:42:22Z
dc.date.available2018-03-29T00:42:22Z
dc.identifierLife Sciences. Pergamon-elsevier Science Ltd, v. 93, n. 41952, n. 416, n. 422, 2013.
dc.identifier0024-3205
dc.identifierWOS:000324507700009
dc.identifier10.1016/j.lfs.2013.07.012
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80582
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80582
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1291825
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionAims: The relationship between the activity of eosinophils and platelets has been observed in recent decades by many scientists. These observations include increased numbers of eosinophils associated with platelet disorders, including changes in the coagulation cascade and platelet aggregation. Based on these observations, the interaction between eosinophils and platelets in platelet aggregation was analyze. Main methods: Human platelets were incubated with eosinophil cytosolic fraction, promyelocytic human HL-60 clone 15 cell lineage, and eosinophil cationic protein (ECP). Platelet rich plasma (PRP) aggregation was induced by adenosine diphosphate, platelet activating factor, arachidonic acid, and collagen, and washed platelets (WP) were activated by thrombin. Key findings: Aggregation induced by all agonists was dose dependently inhibited by eosinophil cytosolic fraction. This inhibition was only partially reversed by previous incubation of the eosinophils with L-Nitro-Arginine-Methyl-Ester (L-NAME). Previous incubation with indomethacin did not prevent the cytosolic fraction induced inhibition. The separation of eosinophil cytosolic fraction by gel filtration on Sephadex G-75 showed that the inhibitory activity was concentrated in the lower molecular weight fraction. HL-60 clone 15 cells differentiated into eosinophils for 5 and 7 day were able to inhibit platelet aggregation. The ECP protein inhibited the platelet aggregation on PRP and WP. This inhibition was more evident in WP, and the citotoxicity MTT assay proved the viability of tested platelets, showing that the observed inhibition by the ECP protein does not occur simply by cell death. Significance: Our results indicate that eosinophils play a fundamental role in platelet aggregation inhibition. (C) 2013 Elsevier Inc All rights reserved.
dc.description93
dc.description41952
dc.description416
dc.description422
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageen
dc.publisherPergamon-elsevier Science Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationLife Sciences
dc.relationLife Sci.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectEosinophil proteins
dc.subjectEosinophil cytosolic fraction
dc.subjectPlatelet aggregation inhibition
dc.subjectEosinophil cationic protein
dc.subjectCationic Protein
dc.subjectPolymorphonuclear Leukocytes
dc.subjectGranule Proteins
dc.subjectNitric-oxide
dc.subjectBiological-properties
dc.subjectActivation
dc.subjectDysfunction
dc.subjectNeutrophils
dc.subjectCells
dc.subjectChildren
dc.titleInhibition of human platelet aggregation by eosinophils
dc.typeArtículos de revistas


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