Transmembrane proteins of the tight junctions at the blood-brain barrier: structural and functional aspects

Semin Cell Dev Biol. 2015 Feb:38:16-25. doi: 10.1016/j.semcdb.2014.11.004. Epub 2014 Nov 26.

Abstract

The blood-brain barrier (BBB) is formed by microvascular endothelial cells sealed by tetraspanning tight junction (TJ) proteins, such as claudins and TAMPs (TJ-associated marvel proteins, occludin and tricellulin). Claudins are the major components of the TJs. At the BBB, claudin-5 dominates the TJs by preventing the paracellular permeation of small molecules. On the other hand, TAMPs regulate the structure and function of the TJs; tricellulin may tighten the barrier for large molecules. This review aims at integrating and summarizing the most relevant and recent work on how the BBB is influenced by claudin-1, -3, -5, -12 and the TAMPs occludin and tricellulin, all of which are four-transmembrane TJ proteins. The exact functions of claudin-1, -3, -12 and TAMPs at this barrier still need to be elucidated.

Keywords: Blood–brain barrier; Claudin; Endothelial cells; Occludin; Tight junction; Tricellulin.

Publication types

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

MeSH terms

  • Animals
  • Biological Transport
  • Blood-Brain Barrier / cytology*
  • Blood-Brain Barrier / physiology*
  • Endothelial Cells / metabolism
  • Humans
  • Membrane Proteins / metabolism*
  • Tight Junctions / physiology*
  • Tight Junctions / ultrastructure

Substances

  • Membrane Proteins