Document Detail

Stromelysin-1 activation correlates with invasiveness in squamous cell carcinoma.
MedLine Citation:
PMID:  11982752     Owner:  NLM     Status:  MEDLINE    
The expression of selected metalloproteinases and tissue inhibitors of metalloproteinases (TIMP) was examined in three squamous cell carcinoma (SCC) cell lines (FaDu, SiHa, A431) and a keratinocyte cell line (HaCaT) to determine which metalloproteinases function in SCC invasiveness. A Matrigel invasion assay was used to assess invasiveness of the cell lines. Only the FaDu cell line showed invasiveness in this assay, and invasion of Matrigel by FaDu cells was inhibited by treatment with the metalloproteinase inhibitor, batimastat. No correlation was found between mRNA expression for matrilysin, stromelysins 1-3, TIMP-1, or TIMP-3 and secretion of these proteins, indicating that the extracellular activity of these molecules is regulated post-transcriptionally. The SCC cell lines differed from the HaCaT line in that matrilysin and TIMP-1 proteins were detected in conditioned medium from all SCC cell lines, but not in medium from HaCaT cells. Only the invasive cell line, FaDu, released active stromelysin-1 into the culture medium. These results indicate that while matrilysin contributes to the invasive phenotype, activation of stromelysin-1 is a key regulatory step for invasiveness in SCC cells.
Tiziana De Angelis; Adele Noè; Mitali Chatterjee; Joy Mulholland
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of investigative dermatology     Volume:  118     ISSN:  0022-202X     ISO Abbreviation:  J. Invest. Dermatol.     Publication Date:  2002 May 
Date Detail:
Created Date:  2002-05-01     Completed Date:  2002-06-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0426720     Medline TA:  J Invest Dermatol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  759-66     Citation Subset:  IM    
Department of Dermatology and Cutaneous Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Biocompatible Materials
Carcinoma, Squamous Cell*
Cell Movement / drug effects
Drug Combinations
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Neoplastic
Keratinocytes / enzymology*,  pathology
Matrix Metalloproteinase 3 / genetics*,  metabolism*
Neoplasm Invasiveness
Phenylalanine / analogs & derivatives*,  pharmacology
Protease Inhibitors / pharmacology
Skin Neoplasms*
Thiophenes / pharmacology
Tissue Inhibitor of Metalloproteinase-1 / genetics
Tumor Cells, Cultured / enzymology,  pathology
Reg. No./Substance:
0/Biocompatible Materials; 0/Drug Combinations; 0/Laminin; 0/Protease Inhibitors; 0/Proteoglycans; 0/Thiophenes; 0/Tissue Inhibitor of Metalloproteinase-1; 119978-18-6/matrigel; 130370-60-4/batimastat; 63-91-2/Phenylalanine; 9007-34-5/Collagen; EC Metalloproteinase 3

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

Previous Document:  Aging and survival of cutaneous microvasculature.
Next Document:  Overexpression of IL-4 alters the homeostasis in the skin.