The amount and proteolytic content of vesicles shed by human cancer cell lines correlates with their in vitro invasiveness

Anticancer Res. Sep-Oct 1998;18(5A):3433-7.

Abstract

Cancer cells are known to shed extracellular membrane vesicles both in vitro and in vivo. To analyse their possible involvement in the metastatic behaviour of tumours, we measured the Matrigel invasion capability and amounts of vesicles shed by four human tumour cell lines (8701-BC, MCF-7, MDA-MB-231 and HT-1080), and by MCF-10A, an immortalised human breast cell line. The proteolytic activity content of vesicles was analysed by gelatin and casein zymographies. While MCF-10A cells do not release a measurable amount of vesicles, all tumour lines analysed, when cultured in presence of serum, shed vesicles rich in MMP-9. Other vesicle-associated proteinases include MMP-2 and uPA. Amounts and proteolytic activities of shed vesicles correlate with the in vitro invasiveness of cells. Since vesicles appear to promote the proteolytic cascade required for the localised degradation of the extracellular matrix, their shedding from cancer cells might represent an important feature of tumour progression.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Breast Neoplasms / enzymology
  • Breast Neoplasms / pathology
  • Collagen
  • Collagenases / analysis*
  • Culture Media / chemistry
  • Drug Combinations
  • Endosomes / enzymology*
  • Female
  • Gelatinases / analysis*
  • Humans
  • Laminin
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9
  • Metalloendopeptidases / analysis*
  • Neoplasm Invasiveness*
  • Neoplasm Proteins / analysis*
  • Proteoglycans
  • Tumor Cells, Cultured
  • Urokinase-Type Plasminogen Activator / analysis

Substances

  • Culture Media
  • Drug Combinations
  • Laminin
  • Neoplasm Proteins
  • Proteoglycans
  • matrigel
  • Collagen
  • Urokinase-Type Plasminogen Activator
  • Collagenases
  • Gelatinases
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9