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Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor

An eosinophil cytotoxicity inhibitor (ECI) was purified from serum of a human subject with severe allergic dermatitis. Molecular weight of the isolated polypeptide (75,000) and its NH2-terminal amino acid sequence identified it as the beta chain of the C3 complement component (apparently free, but p...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1991
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118984/
https://www.ncbi.nlm.nih.gov/pubmed/1940803
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collection PubMed
description An eosinophil cytotoxicity inhibitor (ECI) was purified from serum of a human subject with severe allergic dermatitis. Molecular weight of the isolated polypeptide (75,000) and its NH2-terminal amino acid sequence identified it as the beta chain of the C3 complement component (apparently free, but perhaps attached to very small fragments of the alpha chain). Free beta chain, prepared from normal plasma by reduction of C3, inhibited both eosinophil cytotoxicity and neutrophil adherence functions, with half-maximal activity at approximately 250 ng/ml. Apparently free C3 beta chain was detected in certain human biological fluids associated with inflammation; the presence of C3 beta chain correlated with ECI activity. This evidence demonstrates a potential role for free C3 beta chain as a suppressor of eosinophil and neutrophil functions in inflammation.
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spelling pubmed-21189842008-04-17 Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor J Exp Med Articles An eosinophil cytotoxicity inhibitor (ECI) was purified from serum of a human subject with severe allergic dermatitis. Molecular weight of the isolated polypeptide (75,000) and its NH2-terminal amino acid sequence identified it as the beta chain of the C3 complement component (apparently free, but perhaps attached to very small fragments of the alpha chain). Free beta chain, prepared from normal plasma by reduction of C3, inhibited both eosinophil cytotoxicity and neutrophil adherence functions, with half-maximal activity at approximately 250 ng/ml. Apparently free C3 beta chain was detected in certain human biological fluids associated with inflammation; the presence of C3 beta chain correlated with ECI activity. This evidence demonstrates a potential role for free C3 beta chain as a suppressor of eosinophil and neutrophil functions in inflammation. The Rockefeller University Press 1991-11-01 /pmc/articles/PMC2118984/ /pubmed/1940803 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
Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor
title Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor
title_full Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor
title_fullStr Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor
title_full_unstemmed Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor
title_short Identification of C3 beta chain as the human serum eosinophil cytotoxicity inhibitor
title_sort identification of c3 beta chain as the human serum eosinophil cytotoxicity inhibitor
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118984/
https://www.ncbi.nlm.nih.gov/pubmed/1940803