Preventing the activation or cycling of the Rap1 GTPase alters adhesion and cytoskeletal dynamics and blocks metastatic melanoma cell extravasation into the lungs

Cancer Res. 2010 Jun 1;70(11):4590-601. doi: 10.1158/0008-5472.CAN-09-3414. Epub 2010 May 18.

Abstract

The Rap1 GTPase is a master regulator of cell adhesion, polarity, and migration. We show that both blocking Rap1 activation and expressing a constitutively active form of Rap1 reduced the ability of B16F1 melanoma cells to extravasate from the microvasculature and form metastatic lesions in the lungs. This correlated with a decreased ability of the tumor cells to undergo transendothelial migration (TEM) in vitro and form dynamic, F-actin-rich pseudopodia that penetrate capillary endothelial walls in vivo. Using multiple tumor cell lines, we show that the inability to form these membrane protrusions, which likely promote TEM and extravasation, can be explained by altered adhesion dynamics and impaired cell polarization that result when Rap1 activation or cycling is perturbed. Thus, targeting Rap1 could be a useful approach for reducing the metastatic dissemination of tumor cells that undergo active TEM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion / physiology
  • Cell Communication / physiology
  • Cytoskeleton / enzymology
  • Cytoskeleton / pathology
  • Endothelial Cells / cytology
  • Endothelial Cells / enzymology
  • Enzyme Activation
  • Focal Adhesions / enzymology
  • Focal Adhesions / pathology
  • Humans
  • Lung Neoplasms / blood supply
  • Lung Neoplasms / enzymology*
  • Lung Neoplasms / prevention & control
  • Lung Neoplasms / secondary*
  • Melanoma, Experimental / blood supply
  • Melanoma, Experimental / enzymology*
  • Melanoma, Experimental / prevention & control
  • Melanoma, Experimental / secondary*
  • Mice
  • Mice, Inbred C57BL
  • rap1 GTP-Binding Proteins / metabolism*

Substances

  • rap1 GTP-Binding Proteins