Reduction of tumorigenicity by alpha 3 integrin in a rhabdomyosarcoma cell line

Cell Adhes Commun. 1996 Jul;4(1):41-52. doi: 10.3109/15419069609010762.

Abstract

The expression levels of integrin adhesion receptors have often been correlated with neoplastic transformation and invasiveness. To investigate more definitively the role of the integrin VLA-3 (alpha 3 beta 1) in tumor cell behavior, we transfected alpha 3 subunit cDNA into human rhabdomyosarcoma (RD) cells. Transfectants expressing high levels of alpha 3 beta 1 on their cell surface displayed an altered morphology and decreased anchorage-dependent growth in vitro. Cells expressing alpha 3 also displayed marked reduction in anchorage-independent growth in soft agar and in their ability to form tumors when injected subcutaneously into athymic nude mice. Thus, VLA-3 can repress the transformed phenotype of rhabdomyosarcoma tumor cells. Similar changes in morphology and growth characteristics were observed in cells expressing a chimeric molecule X3C4 in which the alpha 3 cytoplasmic domain had been exchanged with that of the alpha 4 integrin subunit. Therefore, alpha 3 inhibitory effects in RD cells appear not to require specific signalling through the alpha 3 cytoplasmic domain.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, CD / chemistry
  • Antigens, CD / genetics
  • Antigens, CD / physiology*
  • Cell Adhesion
  • Cell Division
  • Cell Size
  • Cell Transformation, Neoplastic / metabolism*
  • DNA, Complementary / genetics
  • Flow Cytometry
  • Humans
  • Integrin alpha3
  • Integrin alpha3beta1
  • Integrin alpha4
  • Integrins / genetics
  • Integrins / physiology*
  • Male
  • Mice
  • Mice, Nude
  • Molecular Sequence Data
  • Neoplasm Proteins / physiology*
  • Neoplasm Transplantation
  • Recombinant Fusion Proteins / metabolism
  • Rhabdomyosarcoma / pathology*
  • Signal Transduction
  • Transfection
  • Tumor Cells, Cultured

Substances

  • Antigens, CD
  • DNA, Complementary
  • Integrin alpha3
  • Integrin alpha3beta1
  • Integrins
  • Neoplasm Proteins
  • Recombinant Fusion Proteins
  • Integrin alpha4