Laminin 332 processing impacts cellular behavior

Cell Adh Migr. 2013 Jan-Feb;7(1):122-34. doi: 10.4161/cam.23132. Epub 2012 Dec 21.

Abstract

Laminin 332, composed of the α3, β3 and γ2 chains, is an epithelial-basement membrane specific laminin variant. Its main role in normal tissues is the maintenance of epithelial-mesenchymal cohesion in tissues exposed to external forces, including skin and stratified squamous mucosa. After being secreted and deposited in the extracellular matrix, laminin 332 undergoes physiological maturation processes consisting in the proteolytic processing of domains located within the α3 and the γ2 chains. These maturation events are essential for laminin 332 integration into the basement membrane where it plays an important function in the nucleation and maintenance of anchoring structures. Studies in normal and pathological situations have revealed that laminin 332 can trigger distinct cellular events depending on the level of its proteolytic cleavages. In this review, the biological and structural characteristics of laminin 332 domains are presented and we discuss whether they trigger specific functions.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Basement Membrane / metabolism*
  • Binding Sites
  • Cell Adhesion
  • Cell Adhesion Molecules / metabolism*
  • Cell Movement
  • Extracellular Matrix / metabolism*
  • Humans
  • Kalinin
  • Keratinocytes / cytology
  • Keratinocytes / metabolism
  • Laminin / metabolism*
  • Mice
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Proteolysis
  • Skin / cytology
  • Skin / metabolism
  • Syndecan-1 / metabolism
  • Wound Healing

Substances

  • Cell Adhesion Molecules
  • Laminin
  • Sdc1 protein, mouse
  • Syndecan-1