The structure and function of claudins, cell adhesion molecules at tight junctions

Ann N Y Acad Sci. 2000;915:129-35. doi: 10.1111/j.1749-6632.2000.tb05235.x.

Abstract

Tight junctions (TJs) play a pivotal role in compartmentalization in multicellular organisms by sealing the paracellular pathway in epithelial and endothelial cell sheets. Recently, novel integral membrane proteins, claudins, have been identified as major cell adhesion molecules working at TJs. Claudins comprise a multigene family, and each member of approximately 23 kDa bears four transmembrane domains. To date, 15 members of this gene family have been identified. When expression vectors of each species of claudins were transfected into fibroblasts lacking endogenous claudins or TJs, well-developed TJs were observed between adjacent transfectants. Furthermore, claudins were shown to be directly involved in the barrier function of TJs by experiments using Clostridium perfringens enterotoxin. Now that claudins have been identified, the structure and functions of TJs should be determined in detail in molecular terms.

Publication types

  • Review

MeSH terms

  • Animals
  • Biological Transport / physiology
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism
  • Claudin-1
  • Claudins
  • Epithelial Cells / chemistry
  • Epithelial Cells / metabolism*
  • Epithelial Cells / ultrastructure
  • Gene Expression / physiology
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Protein Structure, Tertiary
  • Tight Junctions / chemistry*
  • Tight Junctions / metabolism*
  • Tight Junctions / ultrastructure

Substances

  • CLDN1 protein, human
  • CLDN2 protein, human
  • Cell Adhesion Molecules
  • Claudin-1
  • Claudins
  • Membrane Proteins