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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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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2000
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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. |
format | Text |
id | pubmed-2276052 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT digirolamonick invitroandinvivoexpressionofinterstitialcollagenasemmp1byhumanmastcells AT wakefielddenis invitroandinvivoexpressionofinterstitialcollagenasemmp1byhumanmastcells |