Cargando…
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...
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 |
_version_ | 1782141153694449664 |
---|---|
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. |
format | Text |
id | pubmed-2118984 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1991 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |