Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture

Monocyte Chemoattractant Proteins 4 (MCP-4/CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. Recent evidence demonstrates that serum level of this protein strongly increases following high dose IL-2 im...

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Detalles Bibliográficos
Autores principales: Rossi, Leonardo, Moharram, Ramy, Martin, Brian M, White, Richard L, Panelli, Monica C
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Methodology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1397875/
https://www.ncbi.nlm.nih.gov/pubmed/16433902
http://dx.doi.org/10.1186/1479-5876-4-5
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author Rossi, Leonardo
Moharram, Ramy
Martin, Brian M
White, Richard L
Panelli, Monica C
author_facet Rossi, Leonardo
Moharram, Ramy
Martin, Brian M
White, Richard L
Panelli, Monica C
author_sort Rossi, Leonardo
collection PubMed
description Monocyte Chemoattractant Proteins 4 (MCP-4/CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. Recent evidence demonstrates that serum level of this protein strongly increases following high dose IL-2 immunotherapy. The physiological form of human MCP-4/CCL13 has yet to be purified. Therefore, the primary structure of the biologically relevant (mature) form has not been established. By using SELDI immunoaffinity capture technology we describe two mature isoforms both present in serum before and after high-dose IL-2 immunotherapy.
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spelling pubmed-13978752006-03-11 Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture Rossi, Leonardo Moharram, Ramy Martin, Brian M White, Richard L Panelli, Monica C J Transl Med Methodology Monocyte Chemoattractant Proteins 4 (MCP-4/CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. Recent evidence demonstrates that serum level of this protein strongly increases following high dose IL-2 immunotherapy. The physiological form of human MCP-4/CCL13 has yet to be purified. Therefore, the primary structure of the biologically relevant (mature) form has not been established. By using SELDI immunoaffinity capture technology we describe two mature isoforms both present in serum before and after high-dose IL-2 immunotherapy. BioMed Central 2006-01-24 /pmc/articles/PMC1397875/ /pubmed/16433902 http://dx.doi.org/10.1186/1479-5876-4-5 Text en Copyright © 2006 Rossi et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Methodology
Rossi, Leonardo
Moharram, Ramy
Martin, Brian M
White, Richard L
Panelli, Monica C
Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture
title Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture
title_full Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture
title_fullStr Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture
title_full_unstemmed Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture
title_short Detection of human MCP-4/CCL13 isoforms by SELDI immunoaffinity capture
title_sort detection of human mcp-4/ccl13 isoforms by seldi immunoaffinity capture
topic Methodology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1397875/
https://www.ncbi.nlm.nih.gov/pubmed/16433902
http://dx.doi.org/10.1186/1479-5876-4-5
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