Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells
The ability of tumor cells to adhere to, migrate on, and remodel extracellular matrices is mediated by cell surface receptors such as β 1 -integrins. Here we conducted functional live-cell imaging in real time to investigate the effects of modulating β 1 -integrin expression and function on proteoly...
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| Format: | Article |
| Language: | English |
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SAGE Publishing
2008-09-01
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| Series: | Molecular Imaging |
| Online Access: | https://doi.org/10.2310/7290.2008.00019A |
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| _version_ | 1841561891361521664 |
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| author | Mansoureh Sameni Julie Dosescu Kenneth M. Yamada Bonnie F. Sloane Dora Cavallo-Medved |
| author_facet | Mansoureh Sameni Julie Dosescu Kenneth M. Yamada Bonnie F. Sloane Dora Cavallo-Medved |
| author_sort | Mansoureh Sameni |
| collection | DOAJ |
| description | The ability of tumor cells to adhere to, migrate on, and remodel extracellular matrices is mediated by cell surface receptors such as β 1 -integrins. Here we conducted functional live-cell imaging in real time to investigate the effects of modulating β 1 -integrin expression and function on proteolytic remodeling of the extracellular matrix. Human breast and prostate cancer cells were grown on reconstituted basement membrane containing a quenched fluorescent form of collagen IV. Generation of cleavage products and the resulting increases in fluorescence were imaged and quantified. Decreases in the expression and activity of β 1 -integrin reduced digestion of quenched fluorescent-collagen IV by the breast and prostate cancer cells and correspondingly their invasion through and migration on reconstituted basement membrane. Decreased extracellular matrix degradation also was associated with changes in the constituents of proteolytic pathways: decreases in secretion of the cysteine protease cathepsin B, the matrix metalloproteinase (MMP)-13, and tissue inhibitors of metalloproteinases (TIMP)-1 and 2; a decrease in expression of MMP-14 or membrane type 1 MMP; and an increase in secretion of TIMP-3. This is the first study to demonstrate through functional live-cell imaging that downregulation of β 1 -integrin expression and function reduces proteolysis of collagen IV by breast and prostate cancer cells. |
| format | Article |
| id | doaj-art-e715083459d147c0a5dd63e1c675d3de |
| institution | Kabale University |
| issn | 1536-0121 |
| language | English |
| publishDate | 2008-09-01 |
| publisher | SAGE Publishing |
| record_format | Article |
| series | Molecular Imaging |
| spelling | doaj-art-e715083459d147c0a5dd63e1c675d3de2025-01-03T01:20:00ZengSAGE PublishingMolecular Imaging1536-01212008-09-01710.2310/7290.2008.00019A10.2310_7290.2008.00019AFunctional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer CellsMansoureh SameniJulie DosescuKenneth M. YamadaBonnie F. SloaneDora Cavallo-MedvedThe ability of tumor cells to adhere to, migrate on, and remodel extracellular matrices is mediated by cell surface receptors such as β 1 -integrins. Here we conducted functional live-cell imaging in real time to investigate the effects of modulating β 1 -integrin expression and function on proteolytic remodeling of the extracellular matrix. Human breast and prostate cancer cells were grown on reconstituted basement membrane containing a quenched fluorescent form of collagen IV. Generation of cleavage products and the resulting increases in fluorescence were imaged and quantified. Decreases in the expression and activity of β 1 -integrin reduced digestion of quenched fluorescent-collagen IV by the breast and prostate cancer cells and correspondingly their invasion through and migration on reconstituted basement membrane. Decreased extracellular matrix degradation also was associated with changes in the constituents of proteolytic pathways: decreases in secretion of the cysteine protease cathepsin B, the matrix metalloproteinase (MMP)-13, and tissue inhibitors of metalloproteinases (TIMP)-1 and 2; a decrease in expression of MMP-14 or membrane type 1 MMP; and an increase in secretion of TIMP-3. This is the first study to demonstrate through functional live-cell imaging that downregulation of β 1 -integrin expression and function reduces proteolysis of collagen IV by breast and prostate cancer cells.https://doi.org/10.2310/7290.2008.00019A |
| spellingShingle | Mansoureh Sameni Julie Dosescu Kenneth M. Yamada Bonnie F. Sloane Dora Cavallo-Medved Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells Molecular Imaging |
| title | Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells |
| title_full | Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells |
| title_fullStr | Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells |
| title_full_unstemmed | Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells |
| title_short | Functional Live-Cell Imaging Demonstrates that β-Integrin Promotes Type IV Collagen Degradation by Breast and Prostate Cancer Cells |
| title_sort | functional live cell imaging demonstrates that β integrin promotes type iv collagen degradation by breast and prostate cancer cells |
| url | https://doi.org/10.2310/7290.2008.00019A |
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