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Activation of basophil and mast cell histamine release by eosinophil granule major basic protein
Major basic protein (MBP) is a primary constituent of eosinophil granules. In this report, we demonstrate that MBP from human eosinophil granules initiates a nonlytic histamine release from human leukocytes. A direct effect of MBP on basophils was confirmed using purified human basophils. The kineti...
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Lenguaje: | English |
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The Rockefeller University Press
1983
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187055/ https://www.ncbi.nlm.nih.gov/pubmed/6854212 |
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collection | PubMed |
description | Major basic protein (MBP) is a primary constituent of eosinophil granules. In this report, we demonstrate that MBP from human eosinophil granules initiates a nonlytic histamine release from human leukocytes. A direct effect of MBP on basophils was confirmed using purified human basophils. The kinetics of release were similar to those reported for poly-L-arginine, although MBP was less potent than poly-L-arginine of similar molecular weight. Reduction and alkylation of MBP diminished both the potency and efficacy of the molecule. Native MBP also stimulated histamine secretion from purified rat peritoneal mast cells in a manner characteristic of other polycations. These results emphasize the bidirectional nature of the basophil/mast cell-eosinophil regulatory axis. |
format | Text |
id | pubmed-2187055 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1983 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21870552008-04-17 Activation of basophil and mast cell histamine release by eosinophil granule major basic protein J Exp Med Articles Major basic protein (MBP) is a primary constituent of eosinophil granules. In this report, we demonstrate that MBP from human eosinophil granules initiates a nonlytic histamine release from human leukocytes. A direct effect of MBP on basophils was confirmed using purified human basophils. The kinetics of release were similar to those reported for poly-L-arginine, although MBP was less potent than poly-L-arginine of similar molecular weight. Reduction and alkylation of MBP diminished both the potency and efficacy of the molecule. Native MBP also stimulated histamine secretion from purified rat peritoneal mast cells in a manner characteristic of other polycations. These results emphasize the bidirectional nature of the basophil/mast cell-eosinophil regulatory axis. The Rockefeller University Press 1983-06-01 /pmc/articles/PMC2187055/ /pubmed/6854212 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 basophil and mast cell histamine release by eosinophil granule major basic protein |
title | Activation of basophil and mast cell histamine release by eosinophil granule major basic protein |
title_full | Activation of basophil and mast cell histamine release by eosinophil granule major basic protein |
title_fullStr | Activation of basophil and mast cell histamine release by eosinophil granule major basic protein |
title_full_unstemmed | Activation of basophil and mast cell histamine release by eosinophil granule major basic protein |
title_short | Activation of basophil and mast cell histamine release by eosinophil granule major basic protein |
title_sort | activation of basophil and mast cell histamine release by eosinophil granule major basic protein |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187055/ https://www.ncbi.nlm.nih.gov/pubmed/6854212 |