Endothelial lumen signaling complexes control 3D matrix-specific tubulogenesis through interdependent Cdc42- and MT1-MMP-mediated events

Blood. 2010 Jun 24;115(25):5259-69. doi: 10.1182/blood-2009-11-252692. Epub 2010 Mar 9.

Abstract

Here, we define an endothelial cell (EC) lumen signaling complex involving Cdc42, Par6b, Par3, junction adhesion molecule (Jam)-B and Jam-C, membrane type 1-matrix metalloproteinase (MT1-MMP), and integrin alpha(2)beta(1), which coassociate to control human EC tubulogenesis in 3D collagen matrices. Blockade of both Jam-B and Jam-C using antibodies, siRNA, or dominant-negative mutants completely interferes with lumen and tube formation resulting from a lack of Cdc42 activation, inhibition of Cdc42-GTP-dependent signal transduction, and blockade of MT1-MMP-dependent proteolysis. This process requires interdependent Cdc42 and MT1-MMP signaling, which involves Par3 binding to the Jam-B and Jam-C cytoplasmic tails, an interaction that is necessary to physically couple the components of the lumen signaling complex. MT1-MMP proteolytic activity is necessary for Cdc42 activation during EC tube formation in 3D collagen matrices but not on 2D collagen surfaces, whereas Cdc42 activation is necessary for MT1-MMP to create vascular guidance tunnels and tube networks in 3D matrices through proteolytic events. This work reveals a novel interdependent role for Cdc42-dependent signaling and MT1-MMP-dependent proteolysis, a process that occurs selectively in 3D collagen matrices and that requires EC lumen signaling complexes, to control human EC tubulogenesis during vascular morphogenesis.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adaptor Proteins, Signal Transducing / antagonists & inhibitors
  • Adaptor Proteins, Signal Transducing / metabolism
  • Antibodies / pharmacology
  • Cell Adhesion Molecules / metabolism
  • Cell Cycle Proteins / antagonists & inhibitors
  • Cell Cycle Proteins / metabolism
  • Cells, Cultured
  • Collagen
  • Endothelial Cells / enzymology*
  • Humans
  • Matrix Metalloproteinase 14 / metabolism*
  • Membrane Proteins / antagonists & inhibitors
  • Membrane Proteins / metabolism
  • Neovascularization, Physiologic / drug effects
  • Neovascularization, Physiologic / physiology*
  • Signal Transduction / drug effects
  • Signal Transduction / physiology*
  • cdc42 GTP-Binding Protein / metabolism*

Substances

  • Adaptor Proteins, Signal Transducing
  • Antibodies
  • Cell Adhesion Molecules
  • Cell Cycle Proteins
  • JAM3 protein, human
  • Membrane Proteins
  • PARD3 protein, human
  • PARD6A protein, human
  • Collagen
  • Matrix Metalloproteinase 14
  • cdc42 GTP-Binding Protein