Document Detail


Neoplastic progression of the human breast cancer cell line G3S1 is associated with elevation of cytoskeletal dynamics and upregulation of MT1-MMP.
MedLine Citation:
PMID:  20198326     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Ondrej Tolde; Daniel Rösel; Claudia T Mierke; Daniela Panková; Petr Folk; Pavel Vesely; Jan Brábek
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  International journal of oncology     Volume:  36     ISSN:  1791-2423     ISO Abbreviation:  Int. J. Oncol.     Publication Date:  2010 Apr 
Date Detail:
Created Date:  2010-03-03     Completed Date:  2010-06-04     Revised Date:  2013-06-03    
Medline Journal Info:
Nlm Unique ID:  9306042     Medline TA:  Int J Oncol     Country:  Greece    
Other Details:
Languages:  eng     Pagination:  833-9     Citation Subset:  IM    
Affiliation:
Department of Cell Biology, Faculty of Science, Charles University in Prague, 128 43 Prague, Czech Republic.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism*
Aprotinin / pharmacology
Breast Neoplasms / enzymology*,  pathology
Cell Line, Tumor
Cell Movement* / drug effects
Cytoskeleton / drug effects,  enzymology*,  pathology
Dipeptides / pharmacology
Disease Progression
Female
Gelatin / metabolism
Humans
Leucine / analogs & derivatives,  pharmacology
Marine Toxins / pharmacology
Matrix Metalloproteinase 14 / metabolism*
Matrix Metalloproteinase Inhibitors
Matrix Metalloproteinases, Secreted / metabolism
Neoplasm Invasiveness
Neoplastic Stem Cells / enzymology*,  pathology
Protease Inhibitors / pharmacology
Pseudopodia / enzymology
Up-Regulation
Chemical
Reg. No./Substance:
0/Actins; 0/Dipeptides; 0/Marine Toxins; 0/Matrix Metalloproteinase Inhibitors; 0/N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide; 0/Protease Inhibitors; 61-90-5/Leucine; 66701-25-5/E 64; 9000-70-8/Gelatin; 9087-70-1/Aprotinin; EC 3.4.24.-/Matrix Metalloproteinases, Secreted; EC 3.4.24.80/MMP14 protein, human; EC 3.4.24.80/Matrix Metalloproteinase 14

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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