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AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS
The capacity of actively or passively sensitized guinea pig lung to react with antigen to release a factor specifically chemotactic for eosinophil leukocytes (ECF-A) has been demonstrated. The release of ECF-A was also accompanied by the elaboration of both histamine and SRS-A and the appearance of...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1971
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138951/ https://www.ncbi.nlm.nih.gov/pubmed/4106805 |
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author | Kay, A. B. Stechschulte, Daniel J. Austen, K. Frank |
author_facet | Kay, A. B. Stechschulte, Daniel J. Austen, K. Frank |
author_sort | Kay, A. B. |
collection | PubMed |
description | The capacity of actively or passively sensitized guinea pig lung to react with antigen to release a factor specifically chemotactic for eosinophil leukocytes (ECF-A) has been demonstrated. The release of ECF-A was also accompanied by the elaboration of both histamine and SRS-A and the appearance of all these mediators exhibited a similar response in terms of the time course of passve sensitization, the effect of antigen dose, the time course of release, divalent cation dependence and enhancement by the presence of succinate or maleate. Decomplementation by the administration of purified cobra venom factor had no effect on the antigen-induced release of ECF-A from actively or passively sensitized lung fragments. When fragments of guinea pig lung were passively sensitized with fractions of guinea pig 7S IgG, only the IgG(1)-containing fractions prepared tissue for the antigen-induced release of ECF-A. Histamine, SRS-A, bradykinin, serotonin, and the prostaglandins PGE(1), PGE(2), and PGF(2α) were not eosinophilotactic per se; neither was ECF-A detected following the incubation of these agents with sensitized lung in the absence of antigen. Both eosinophilotactic activity and SRS-A survived extraction in 80% ethanol and evaporation to dryness. SRS-A, however, withstood boiling in alkaline solution for 20 min, whereas ECF-A activity was abolished by this procedure. SRS-A and ECF-A could also be separated by gel filtration. ECF-A activity was completely recovered following its passage through a column of Sephadex G-25 and had an estimated molecular weight of between 500 and 1000. On the basis of size and a formation mechanism independent of the complement system, ECF-A is distinguishable from a previously described complement-dependent eosinophilotactic factor (ECF-C). Thus, ECF-A represents a hitherto undescribed agent which selectively attracts eosinophil leukocytes. |
format | Text |
id | pubmed-2138951 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1971 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21389512008-04-17 AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS Kay, A. B. Stechschulte, Daniel J. Austen, K. Frank J Exp Med Article The capacity of actively or passively sensitized guinea pig lung to react with antigen to release a factor specifically chemotactic for eosinophil leukocytes (ECF-A) has been demonstrated. The release of ECF-A was also accompanied by the elaboration of both histamine and SRS-A and the appearance of all these mediators exhibited a similar response in terms of the time course of passve sensitization, the effect of antigen dose, the time course of release, divalent cation dependence and enhancement by the presence of succinate or maleate. Decomplementation by the administration of purified cobra venom factor had no effect on the antigen-induced release of ECF-A from actively or passively sensitized lung fragments. When fragments of guinea pig lung were passively sensitized with fractions of guinea pig 7S IgG, only the IgG(1)-containing fractions prepared tissue for the antigen-induced release of ECF-A. Histamine, SRS-A, bradykinin, serotonin, and the prostaglandins PGE(1), PGE(2), and PGF(2α) were not eosinophilotactic per se; neither was ECF-A detected following the incubation of these agents with sensitized lung in the absence of antigen. Both eosinophilotactic activity and SRS-A survived extraction in 80% ethanol and evaporation to dryness. SRS-A, however, withstood boiling in alkaline solution for 20 min, whereas ECF-A activity was abolished by this procedure. SRS-A and ECF-A could also be separated by gel filtration. ECF-A activity was completely recovered following its passage through a column of Sephadex G-25 and had an estimated molecular weight of between 500 and 1000. On the basis of size and a formation mechanism independent of the complement system, ECF-A is distinguishable from a previously described complement-dependent eosinophilotactic factor (ECF-C). Thus, ECF-A represents a hitherto undescribed agent which selectively attracts eosinophil leukocytes. The Rockefeller University Press 1971-02-28 /pmc/articles/PMC2138951/ /pubmed/4106805 Text en Copyright © 1971 by The Rockefeller University Press 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 | Article Kay, A. B. Stechschulte, Daniel J. Austen, K. Frank AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS |
title | AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS |
title_full | AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS |
title_fullStr | AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS |
title_full_unstemmed | AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS |
title_short | AN EOSINOPHIL LEUKOCYTE CHEMOTACTIC FACTOR OF ANAPHYLAXIS |
title_sort | eosinophil leukocyte chemotactic factor of anaphylaxis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138951/ https://www.ncbi.nlm.nih.gov/pubmed/4106805 |
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