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Proteolytic Activity of Human Lymphoid Tumor Cells. Correlation with Tumor Progression
Matrix metalloproteinase (MMP) expression and production are associated with advanced-stage tumor and contribute to tumor progression, invasion and metastases. The current study was designed to determine the expression and production of MMP-2 (gelatinase A) and MMP-9 (gelatinase B) by human lymphoid...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2000
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276050/ https://www.ncbi.nlm.nih.gov/pubmed/11097203 http://dx.doi.org/10.1155/2000/74372 |
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author | Vacca, Angelo Ribatti, Domenico Ria, Roberto Pellegrino, Antonio Bruno, Michele Merchionne, Francesca Dammacco, Franco |
author_facet | Vacca, Angelo Ribatti, Domenico Ria, Roberto Pellegrino, Antonio Bruno, Michele Merchionne, Francesca Dammacco, Franco |
author_sort | Vacca, Angelo |
collection | PubMed |
description | Matrix metalloproteinase (MMP) expression and production are associated with advanced-stage tumor and contribute to tumor progression, invasion and metastases. The current study was designed to determine the expression and production of MMP-2 (gelatinase A) and MMP-9 (gelatinase B) by human lymphoid tumor cells. Changes in expression and production were also investigated during tumor progression of multiple myeloma and mycosis fungoides. In situ hybridization analysis revealed that lymphoblastic leukemia B cells (SB cell line), multiple myeloma (MM) cells (U266 cell line) and lymphoblastic leukemia T cells (CEM and Jurkat cell lines) express constitutively the mRNA for MMP-2 and/or MMP-9. We demonstrated by gelatin-zymography of cell culture medium that both enzymes were secreted in their cleaved (activated) form. In situ hybridization of bone marrow plasma cells and gelatin- zymography of the medium showed that patients with active MM (diagnosis, relapse, leukemic progression) express higher levels of MMP-2 mRNA and protein than patients with non-active MM (complete/objective response, plateau) and with monoclonal gammopathies of undetermined significance (MGUS). MMP-9 expression and secretion was similar in all patient groups. In patients with mycosis fungoides (MF), the expression of MMP-2 and MMP-9 mRNAs was significantly upregulated with advancing stage, in terms of lesions both positive for one of two mRNAs and with the greatest intensity of expression. Besides MF cells, the MMP-2 and/or MMP-9 mRNAs were expressed by some stromal cell populations (microvascular endothelial cells, fibroblasts, macrophages), suggesting that these cells cooperate in the process of tumor invasion. Our studies identify MMPs as an important class of proteinases involved in the extracellular matrix (ECM) degradation by human lymphoid tumors, and suggest that MMPs inhibitors may lead to important new treatment for their control. |
format | Text |
id | pubmed-2276050 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-22760502008-03-31 Proteolytic Activity of Human Lymphoid Tumor Cells. Correlation with Tumor Progression Vacca, Angelo Ribatti, Domenico Ria, Roberto Pellegrino, Antonio Bruno, Michele Merchionne, Francesca Dammacco, Franco Dev Immunol Research Article Matrix metalloproteinase (MMP) expression and production are associated with advanced-stage tumor and contribute to tumor progression, invasion and metastases. The current study was designed to determine the expression and production of MMP-2 (gelatinase A) and MMP-9 (gelatinase B) by human lymphoid tumor cells. Changes in expression and production were also investigated during tumor progression of multiple myeloma and mycosis fungoides. In situ hybridization analysis revealed that lymphoblastic leukemia B cells (SB cell line), multiple myeloma (MM) cells (U266 cell line) and lymphoblastic leukemia T cells (CEM and Jurkat cell lines) express constitutively the mRNA for MMP-2 and/or MMP-9. We demonstrated by gelatin-zymography of cell culture medium that both enzymes were secreted in their cleaved (activated) form. In situ hybridization of bone marrow plasma cells and gelatin- zymography of the medium showed that patients with active MM (diagnosis, relapse, leukemic progression) express higher levels of MMP-2 mRNA and protein than patients with non-active MM (complete/objective response, plateau) and with monoclonal gammopathies of undetermined significance (MGUS). MMP-9 expression and secretion was similar in all patient groups. In patients with mycosis fungoides (MF), the expression of MMP-2 and MMP-9 mRNAs was significantly upregulated with advancing stage, in terms of lesions both positive for one of two mRNAs and with the greatest intensity of expression. Besides MF cells, the MMP-2 and/or MMP-9 mRNAs were expressed by some stromal cell populations (microvascular endothelial cells, fibroblasts, macrophages), suggesting that these cells cooperate in the process of tumor invasion. Our studies identify MMPs as an important class of proteinases involved in the extracellular matrix (ECM) degradation by human lymphoid tumors, and suggest that MMPs inhibitors may lead to important new treatment for their control. Hindawi Publishing Corporation 2000 /pmc/articles/PMC2276050/ /pubmed/11097203 http://dx.doi.org/10.1155/2000/74372 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 Vacca, Angelo Ribatti, Domenico Ria, Roberto Pellegrino, Antonio Bruno, Michele Merchionne, Francesca Dammacco, Franco Proteolytic Activity of Human Lymphoid Tumor Cells. Correlation with Tumor Progression |
title | Proteolytic Activity of Human Lymphoid Tumor Cells.
Correlation with Tumor Progression |
title_full | Proteolytic Activity of Human Lymphoid Tumor Cells.
Correlation with Tumor Progression |
title_fullStr | Proteolytic Activity of Human Lymphoid Tumor Cells.
Correlation with Tumor Progression |
title_full_unstemmed | Proteolytic Activity of Human Lymphoid Tumor Cells.
Correlation with Tumor Progression |
title_short | Proteolytic Activity of Human Lymphoid Tumor Cells.
Correlation with Tumor Progression |
title_sort | proteolytic activity of human lymphoid tumor cells.
correlation with tumor progression |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2276050/ https://www.ncbi.nlm.nih.gov/pubmed/11097203 http://dx.doi.org/10.1155/2000/74372 |
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