Role of mp 17O Seprase in Breast Cancer.

Abstract

Seprase, a cell surface serine type gelatinase with MT 170 kDa whose expression is associated with melanoma invasiveness, is composed of two identical subunits of MT 97 kDa. Recent evidence indicated that the Seprase subunit is identical to Fibroblast Activation Protein a (FAPa). To characterize and define the role of this molecule in cancer, human Seprase/FAPa cDNA was cloned and stable transfected in two human epithelial carcinoma cell lines SW-13 and MCF-7. Unexpectedly, overexpression of Seprase/FAPa has no apparent effect on the proliferation, matrix adhesion and matrigel invasion of these cells. Preliminary site-directed mutagenesis studies suggested that the region coding for the signal/anchorage domain of the molecule and this intact domain are probably essential for Seprase/FAPa mRNA stability and the dimerization of the subunits, respectively. Ribozyrne constructs targeted Seprase/FAPa mRNA%%A have been made. However, despite the in vitro cleavage activity, these ribozyrne constructs are not effective in abrogating the endogenous Seprase/FAPa level in highly metastatic melanoma l2O5LU cells.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1998
Accession Number
ADA358118

Entities

People

  • Quang Nguyen

Organizations

  • Georgetown University

Tags

DTIC Thesaurus Topics

  • Adhesion
  • Amino Acids
  • Biological Sciences
  • Breast Cancer
  • Cell Line
  • Cell Physiological Processes
  • Cells
  • Chemistry
  • Culture Media
  • Culture Techniques
  • Cultured Cells
  • Gene Expression
  • Genetic Code
  • Indicator Dyes
  • Molecules
  • Neoplasms
  • Tumor Cell Line

Fields of Study

  • Biology

Readers

  • Molecular Biology and Genetics