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Activation of platelets by eosinophil granule proteins
Two of the four principal cationic proteins of the eosinophil granule, major basic protein (MBP) and eosinophil peroxidase (EPO), were shown to be platelet agonists. Both MBP and EPO evoked a dose-dependent nonlytic secretion of platelet 5-hydroxytryptamine in unstirred platelet suspensions even in...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1990
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188607/ https://www.ncbi.nlm.nih.gov/pubmed/2212954 |
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collection | PubMed |
description | Two of the four principal cationic proteins of the eosinophil granule, major basic protein (MBP) and eosinophil peroxidase (EPO), were shown to be platelet agonists. Both MBP and EPO evoked a dose-dependent nonlytic secretion of platelet 5-hydroxytryptamine in unstirred platelet suspensions even in the presence of 10 microM indomethacin. MBP also evoked secretion of platelet alpha granule and lysosome components. Secretion by MBP and EPO was inhibited by 1 microM PGE1, but the nature of the inhibition differed from that observed with thrombin. Thus, MBP and EPO can be classified as strong platelet agonists with a distinct mechanism of activation. |
format | Text |
id | pubmed-2188607 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21886072008-04-17 Activation of platelets by eosinophil granule proteins J Exp Med Articles Two of the four principal cationic proteins of the eosinophil granule, major basic protein (MBP) and eosinophil peroxidase (EPO), were shown to be platelet agonists. Both MBP and EPO evoked a dose-dependent nonlytic secretion of platelet 5-hydroxytryptamine in unstirred platelet suspensions even in the presence of 10 microM indomethacin. MBP also evoked secretion of platelet alpha granule and lysosome components. Secretion by MBP and EPO was inhibited by 1 microM PGE1, but the nature of the inhibition differed from that observed with thrombin. Thus, MBP and EPO can be classified as strong platelet agonists with a distinct mechanism of activation. The Rockefeller University Press 1990-10-01 /pmc/articles/PMC2188607/ /pubmed/2212954 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Activation of platelets by eosinophil granule proteins |
title | Activation of platelets by eosinophil granule proteins |
title_full | Activation of platelets by eosinophil granule proteins |
title_fullStr | Activation of platelets by eosinophil granule proteins |
title_full_unstemmed | Activation of platelets by eosinophil granule proteins |
title_short | Activation of platelets by eosinophil granule proteins |
title_sort | activation of platelets by eosinophil granule proteins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188607/ https://www.ncbi.nlm.nih.gov/pubmed/2212954 |