Neoplastic progression of the human breast cancer cell line G3S1 is associated with elevation of cytoskeletal dynamics and upregulation of MT1-MMP
Language English Country Greece Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
20198326
DOI
10.3892/ijo_00000560
Knihovny.cz E-resources
- MeSH
- Actins metabolism MeSH
- Aprotinin pharmacology MeSH
- Cytoskeleton drug effects enzymology pathology MeSH
- Dipeptides pharmacology MeSH
- Matrix Metalloproteinase Inhibitors MeSH
- Protease Inhibitors pharmacology MeSH
- Neoplasm Invasiveness MeSH
- Leucine analogs & derivatives pharmacology MeSH
- Humans MeSH
- Matrix Metalloproteinase 14 metabolism MeSH
- Matrix Metalloproteinases, Secreted metabolism MeSH
- Marine Toxins pharmacology MeSH
- Cell Line, Tumor MeSH
- Neoplastic Stem Cells enzymology pathology MeSH
- Breast Neoplasms enzymology pathology MeSH
- Cell Movement * drug effects MeSH
- Disease Progression MeSH
- Pseudopodia enzymology MeSH
- Up-Regulation MeSH
- Gelatin metabolism MeSH
- Check Tag
- Humans MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Actins MeSH
- Aprotinin MeSH
- Dipeptides MeSH
- E 64 MeSH Browser
- Matrix Metalloproteinase Inhibitors MeSH
- Protease Inhibitors MeSH
- Leucine MeSH
- Matrix Metalloproteinase 14 MeSH
- Matrix Metalloproteinases, Secreted MeSH
- MMP14 protein, human MeSH Browser
- Marine Toxins MeSH
- N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide MeSH Browser
- Gelatin MeSH
The newly established breast cancer cell line G3S1, derived from EM-G3 breast cancer progenitors, was analyzed for functional changes related to neoplastic progression manifested by elevated invasiveness and enhanced capability to degrade gelatin. Degradation of gelatin and invasiveness of G3S1 cells was found to be dependent on the activity of matrix proteinases and actin cytoskeletal dynamics. Therefore, the expression and activity of these proteases was compared in G3S1 and EM-G3 cells. Despite enhanced capability of G3S1 cells to degrade gelatin, these cells exhibited lower levels of secreted extracellular matrix degrading proteases than parental EM-G3 cells. However, the expression of membrane-bound MT1-MMP was strongly elevated in G3S1 cells. While the degradation of gelatin was associated with invadopodia-like structures in both EM-G3 and G3S1 cells, the cytoskeletal remodeling dynamics was greatly elevated in G3S1 cells, suggesting that upregulation of MT1-MMP, together with elevation of cytoskeletal remodeling dynamics can effectively cause elevated invasiveness and enhanced matrix degrading capability in G3S1 cells.
Department of Cell Biology Faculty of Science Charles University Prague 128 43 Prague Czech Republic
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