Conformational changes in adhesive proteins modulate their adhesive function

Thromb Haemost. 1995 Jul;74(1):253-7.

Abstract

A large family of glycoproteins mediates cell adhesion by binding to cellular receptors. As a group, these adhesive proteins are large in size, multi-domainal in composition, and are capable of self-association. A general property of the adhesive proteins is their susceptibility to structural modulation, and conformational change provides a mechanism for regulation of their adhesive functions. To illustrate this concept, conformational alterations of thrombospondin, fibrinogen and fibronectin are shown to modulate their adhesive potential. Thus, conformational status of the adhesive proteins contributes to the regulation of cell adhesion.

Publication types

  • Review

MeSH terms

  • Cell Adhesion
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / physiology
  • Fibrinogen / chemistry
  • Fibrinogen / physiology
  • Fibronectins / chemistry
  • Fibronectins / physiology
  • Humans
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / physiology
  • Protein Conformation
  • Thrombospondins

Substances

  • Cell Adhesion Molecules
  • Fibronectins
  • Membrane Glycoproteins
  • Thrombospondins
  • Fibrinogen