TPA-induced cohort migration of well-differentiated human rectal adenocarcinoma cells: cells move in a RGD-dependent manner on fibronectin produced by cells, and phosphorylation of E-cadherin/catenin complex is induced independently of cell-extracellular matrix interactions

Virchows Arch. 1998 Sep;433(3):243-53. doi: 10.1007/s004280050243.

Abstract

We have already presented a two-dimensional cell motility assay using a highly metastatic variant (L-10) of human rectal adenocarcinoma cell line RCM-1 as a motility model of tumour cells of epithelial origin. In this model, L-10 cells showed locomotion as a coherent sheet when stimulated with 12-O-tetradecanoylphorbol-13-acetate (TPA), and we called this type of movement "cohort migration". Electron and immunoelectron microscopic study of the migrating cell sheets demonstrated localized release from cell-cell adhesion only at the lower portion of the cells with loss of E-cadherin immunoreactivity, and this change was associated with increased tyrosine phosphorylation of the E-cadherin-catenin complex, including beta-catenin. Cell-extracellular matrix (ECM) interactions involved in this TPA-induced cohort migration and their effect on tyrosine phosphorylation of the E-cadherin-catenin complex have now been investigated. L-10 cell cohort migration was almost completely inhibited by addition of Arg-Gly-Asp (RGD) peptide into the medium, and thus RGD dependent. Cohort migration was stimulated on type I and IV collagens, fibronectin (FN)- and laminin-coated substratum, but was inhibited by RGD only on FN-coated surface. By using immunofluorescent techniques, FN was demonstrated preferentially around migrating cells, and a protein synthesis inhibitor, cycloheximide, inhibited the migration by about 75%. FN produced by L-10 cells were found to be mostly EDA+ FN when analysed by RT-PCR. Moreover, anti-FN antibody, but not anti-vitronectin antibody, inhibited the TPA-induced cohort migration almost completely. Thus, it was likely that L-10 cells produced FN themselves and moved on the FN substrate in an RGD-dependent manner. However, stimulation of migration by type I collagen coating and inhibition by RGD treatment did not affect the tyrosine phosphorylation of the E-cadherin-catenin complex induced by TPA, indicating that cell-cell interactions were adjusted to suit cell migration, irrespective of the condition of cell-ECM adhesion, during TPA-induced cohort migration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / metabolism
  • Adenocarcinoma / pathology*
  • Antibodies, Monoclonal / pharmacology
  • Cadherins / metabolism*
  • Cell Adhesion
  • Cell Communication
  • Cell Movement / drug effects*
  • Cell Movement / physiology
  • Cytoskeletal Proteins / metabolism*
  • DNA Primers / chemistry
  • Extracellular Matrix / metabolism
  • Fibronectins / genetics
  • Fibronectins / metabolism*
  • Humans
  • Microscopy, Immunoelectron
  • Oligopeptides / pharmacology*
  • Phosphorylation
  • Polymerase Chain Reaction
  • RNA, Messenger / metabolism
  • Rectal Neoplasms / metabolism
  • Rectal Neoplasms / pathology*
  • Tetradecanoylphorbol Acetate / pharmacology*
  • Trans-Activators*
  • Tumor Cells, Cultured
  • beta Catenin

Substances

  • Antibodies, Monoclonal
  • CTNNB1 protein, human
  • Cadherins
  • Cytoskeletal Proteins
  • DNA Primers
  • Fibronectins
  • Oligopeptides
  • RNA, Messenger
  • Trans-Activators
  • beta Catenin
  • arginyl-glycyl-aspartic acid
  • Tetradecanoylphorbol Acetate