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In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells

Degradation of the extracellular matrix occurs under physiological and pathological conditions, thought to be principally mediated by a family of neutral proteolytic enzymes termed the matrix metalloproteinases (MMPs). The present study was initiated to determine whether mast cells have the ability...

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Detalles Bibliográficos
Autores principales: Di Girolamo, Nick, Wakefield, Denis
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2000
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276052/
https://www.ncbi.nlm.nih.gov/pubmed/11097207
http://dx.doi.org/10.1155/2000/82708
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author Di Girolamo, Nick
Wakefield, Denis
author_facet Di Girolamo, Nick
Wakefield, Denis
author_sort Di Girolamo, Nick
collection PubMed
description Degradation of the extracellular matrix occurs under physiological and pathological conditions, thought to be principally mediated by a family of neutral proteolytic enzymes termed the matrix metalloproteinases (MMPs). The present study was initiated to determine whether mast cells have the ability to produce these proteases in diseased and normal human tissue. Immunohistochemistry and in situ hybridization was performed to localize interstitial collagenase protein and mRNA transcripts in diseased human tissue. The human mast cell line HMC-1 was cultured under serum free conditions, stimulated with phorbol mystrate acetate (PMA) and supernatants analyzed by Western blotting and zymography to determine the profile of secreted MMPs. The dog mast cell line BR, known to secrete gelatinolytic enzymes, was used in parallel studies. Total RNA was extracted and analyzed by RT-PCR for the expression of tissue inhibitors of MMP (TIMPs). Collagenase-1 protein and mRNA were expressed by tryptase and chymase positive human mast cells in all tissue analyzed. This proteinase wa also detected in the cytoplasm and conditioned media of HMC-1 cells. PMA induced gelatinolytic activity in both mast cell lines examined. TIMP-1 immunoreactivity was detected and TIMP-1, and-2 (but not TIMP-3) mRNA transcripts were amplified from HMC-1 cells. This is the first demonstration of the expression of collagenase-1 by human mast cells in both inflamed and normal tissues, and by a human mast cell line. MMPs secreted by these cells could contribute to the extensive matrix lysis characteristic of diseases such as rheumatoid arthritis and inflammatory ocular disorders. Alternatively collagenase-1 production by mast cells may play a critical role in cell invasion and migration into sites of inflammation.
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spelling pubmed-22760522008-03-31 In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells Di Girolamo, Nick Wakefield, Denis Dev Immunol Research Article Degradation of the extracellular matrix occurs under physiological and pathological conditions, thought to be principally mediated by a family of neutral proteolytic enzymes termed the matrix metalloproteinases (MMPs). The present study was initiated to determine whether mast cells have the ability to produce these proteases in diseased and normal human tissue. Immunohistochemistry and in situ hybridization was performed to localize interstitial collagenase protein and mRNA transcripts in diseased human tissue. The human mast cell line HMC-1 was cultured under serum free conditions, stimulated with phorbol mystrate acetate (PMA) and supernatants analyzed by Western blotting and zymography to determine the profile of secreted MMPs. The dog mast cell line BR, known to secrete gelatinolytic enzymes, was used in parallel studies. Total RNA was extracted and analyzed by RT-PCR for the expression of tissue inhibitors of MMP (TIMPs). Collagenase-1 protein and mRNA were expressed by tryptase and chymase positive human mast cells in all tissue analyzed. This proteinase wa also detected in the cytoplasm and conditioned media of HMC-1 cells. PMA induced gelatinolytic activity in both mast cell lines examined. TIMP-1 immunoreactivity was detected and TIMP-1, and-2 (but not TIMP-3) mRNA transcripts were amplified from HMC-1 cells. This is the first demonstration of the expression of collagenase-1 by human mast cells in both inflamed and normal tissues, and by a human mast cell line. MMPs secreted by these cells could contribute to the extensive matrix lysis characteristic of diseases such as rheumatoid arthritis and inflammatory ocular disorders. Alternatively collagenase-1 production by mast cells may play a critical role in cell invasion and migration into sites of inflammation. Hindawi Publishing Corporation 2000 /pmc/articles/PMC2276052/ /pubmed/11097207 http://dx.doi.org/10.1155/2000/82708 Text en Copyright © 2000 Hindawi Publishing Corporation. http://creativecommons.org/licenses/by/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Di Girolamo, Nick
Wakefield, Denis
In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells
title In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells
title_full In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells
title_fullStr In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells
title_full_unstemmed In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells
title_short In vitro and in vivo Expression of Interstitial Collagenase/MMP-1 by Human Mast Cells
title_sort in vitro and in vivo expression of interstitial collagenase/mmp-1 by human mast cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276052/
https://www.ncbi.nlm.nih.gov/pubmed/11097207
http://dx.doi.org/10.1155/2000/82708
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