Claudin-based permeability barriers in taste buds

J Comp Neurol. 2007 Jun 20;502(6):1003-11. doi: 10.1002/cne.21354.


Tight junctions operate as semipermeable barriers in epithelial tissue, separating the apical from the basolateral sides of the cells. Membrane proteins of the claudin family represent the major tight junction constituents, and some reinforce permeability barriers, whereas others create pores based on solute size and ion selectivity. To outline paracellular permeability pathways in gustatory tissue, all claudins expressed in mouse taste buds and in human fungiform papillae have been characterized. Twelve claudins are expressed in murine taste-papillae-enriched tissue, and five of those are expressed in human fungiform papillae. A subset of the claudins expressed in mouse papillae is uniquely found in taste buds. By immunohistochemistry, claudin 4 has been found in mouse taste epithelium, with high abundance around the taste pore. Claudin 6 is explicitly detected inside the pore, claudin 7 was found at the basolateral side of taste cells, and claudin 8 was found around the pore. With the ion permeability features of the different claudins, a highly specific permeability pattern for paracellular diffusion is apparent, which indicates a peripheral mechanism for taste coding.

MeSH terms

  • Animals
  • Cell Communication / physiology
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Cell Membrane Permeability / physiology*
  • Claudin-4
  • Claudins
  • Diffusion
  • Humans
  • Immunohistochemistry
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Taste / physiology*
  • Taste Buds / metabolism*
  • Taste Buds / ultrastructure
  • Tight Junctions / metabolism*
  • Tight Junctions / ultrastructure


  • CLDN4 protein, human
  • Claudin-4
  • Claudins
  • Cldn4 protein, mouse
  • Cldn7 protein, mouse
  • Membrane Proteins
  • claudin 8
  • claudin 6