Integrin alpha 2 beta 1 (VLA-2) mediates reorganization and contraction of collagen matrices by human cells

Cell. 1991 Oct 18;67(2):403-10. doi: 10.1016/0092-8674(91)90191-z.

Abstract

The capacity of cells to organize and contract collagen fibrils is fundamental to processes as diverse as embryogenesis and wound healing. We analyzed different beta 1 integrins on diploid fibroblasts for their role in modifying the tertiary structure of collagen matrices. Using monoclonal antibodies that block the interaction of integrins with their ligands, evidence was obtained that alpha 2 beta 1 integrin is required for the contraction of a type I collagen matrix. Further supporting the role of alpha 2 beta 1, cell lines expressing minimal levels of this integrin uniformly failed to contract collagen matrices. In addition, transfection of a full-length alpha 2 cDNA into one such cell line led to enhanced cell surface expression of alpha 2 beta 1 and conferred the de novo capacity to contract collagen matrices.

Publication types

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

MeSH terms

  • Antibodies, Monoclonal / metabolism
  • Cell Adhesion / physiology
  • Cell Line
  • Cells, Cultured
  • Collagen / chemistry
  • Collagen / metabolism*
  • Extracellular Matrix / chemistry
  • Extracellular Matrix / metabolism*
  • Fibroblasts / metabolism*
  • Flow Cytometry
  • Gene Expression / physiology
  • Humans
  • Kinetics
  • Protein Conformation
  • Receptors, Very Late Antigen / metabolism*
  • Transfection / genetics

Substances

  • Antibodies, Monoclonal
  • Receptors, Very Late Antigen
  • Collagen