Clinical & Experimental Metastasis

, Volume 19, Issue 2, pp 127–134

Regulation of melanoma cell migration and invasion by laminin-5 and α3β1 integrin (VLA-3)

Authors

  • Tsutomu Tsuji
    • Department of MicrobiologyHoshi University
  • Yoko Kawada
    • Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical SciencesThe University of Tokyo
  • Mieko Kai-Murozono
    • Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical SciencesThe University of Tokyo
  • Shinya Komatsu
    • Department of MicrobiologyHoshi University
  • Seon Ae Han
    • Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical SciencesThe University of Tokyo
  • Ken-ichi Takeuchi
    • Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical SciencesThe University of Tokyo
  • Hiroto Mizushima
    • Division of Cell Biology, Kihara Institute for Biological ResearchYokohama City University
  • Kaoru Miyazaki
    • Division of Cell Biology, Kihara Institute for Biological ResearchYokohama City University
  • Tatsuro Irimura
    • Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical SciencesThe University of Tokyo
Article

DOI: 10.1023/A:1014573204062

Cite this article as:
Tsuji, T., Kawada, Y., Kai-Murozono, M. et al. Clin Exp Metastasis (2002) 19: 127. doi:10.1023/A:1014573204062

Abstract

We evaluated the role of soluble factors produced from epidermal cells in melanoma cell motility by using the Boyden chamber chemoinvasion system. The migration of two melanoma cell lines, A375 and Mewo, was potentiated by conditioned media of A431 epidermoid cells in a concentration-dependent manner. The enhancement of A375 melanoma cell motility induced by the conditioned medium was blocked by antibodies against either α3 or β1 integrin subunit. The motility-stimulating activity was recovered in the same fraction as the α3 integrin-dependent adhesion-promoting activity in a high-molecular-weight (>200 kDa) fraction on Superose 12 gel chromatography, and adsorbed with an anti-laminin-5 antibody. Purified laminin-5 was capable of potentiating melanoma cell migration as measured in either the chemotaxis assay with a soluble form of laminin-5 or the haptotaxis assay with membranes coated with a mixture of laminin-5 and Matrigel. Furthermore, immobilized laminin-5 induced A375 melanoma cells to secrete matrix metalloproteinase-9 (type IV collagenase) into the culture medium. These results strongly suggest that the interaction of laminin-5 produced in the epidermis with α3β1 integrin on melanoma cells is involved in cell migration, invasion, and degradation of extracellular matrix proteins.

α3β1 integrincell migrationepidermoid cellslaminin-5matrix metalloproteinasemelanoma

Copyright information

© Kluwer Academic Publishers 2002