Cell interactions and motility in human lung tumor cell lines HS-24 and SB-3 under the influence of extracellular matrix components and proteinase inhibitors

Anticancer Res. Mar-Apr 1992;12(2):349-59.

Abstract

The human NSCLC cell lines HS-24 (squamous cell carcinoma) and SB-3 (metastasis derived from an adenocarcinoma) were investigated in respect to cell interactions, motility and invasive properties. HS-24 revealed high self adhesion capacity. Testing the interactions with collagens type I/III or IV, laminin and fibronectin by adhesion, non directional motility and haptotaxis assays, tight interactions and stimulation, particularly with collagen type I/III, was detected. Proteinase inhibitors (E64, Stefin A or leupeptin) revealed a slightly negative influence. Invasion in vitro of lung explants was reduced by leupeptin in a dose dependent manner and slightly increased by plasmin. SB-3 cells revealed low self adhesion. As judged from interaction with fibronectin, these cells have low integrin receptor concentrations and thus reduced adhesiveness to extracellular matrix. Collagen type I/III was inhibitory for undirectional motility and not permissive for haptotaxis. Therefore, it may play a restrictive role during the spread in vivo of these cells. Colonization of lung explants was low and was not influenced by cathepsin B proteinase inhibitors. The results emphasize a particular role of collagens for primary site tumor and metastasis development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carcinoma, Non-Small-Cell Lung / pathology*
  • Cathepsin B / pharmacology
  • Cell Aggregation
  • Cell Communication / drug effects*
  • Cell Movement / drug effects
  • Collagen / pharmacology
  • Extracellular Matrix Proteins / pharmacology*
  • Humans
  • Laminin / pharmacology
  • Lung Neoplasms / pathology*
  • Neoplasm Invasiveness
  • Oligopeptides / pharmacology
  • Protease Inhibitors / pharmacology*
  • Tumor Cells, Cultured

Substances

  • Extracellular Matrix Proteins
  • Laminin
  • Oligopeptides
  • Protease Inhibitors
  • Collagen
  • glycyl-arginyl-glycyl-aspartyl-seryl-proline
  • Cathepsin B