Limited contribution of claudin-5-dependent tight junction strands to endothelial barrier function

Eur J Cell Biol. 2006 Nov;85(11):1131-44. doi: 10.1016/j.ejcb.2006.07.005. Epub 2006 Sep 7.

Abstract

Members of the claudin family are involved in formation of barriers that control access to the paracellular space of epithelia. Likewise, endothelium-specific claudin-5 is involved in the function of the blood-brain barrier (BBB). Here, we assessed the role of claudin-5 in non-BBB endothelial barriers using lentiviral-driven overexpression and silencing of claudin-5 in its native environment of primary vascular endothelial cells. Effects were monitored using macromolecular tracers between 342Da and 40kDa. Measurements were made both in absence and presence of transmigrating leukocytes. Freeze-fracture preparations were analyzed for effects at the ultrastructural level. We show that overexpression of claudin-5 leads to formation of elaborate networks of junction strands, which are absent in untransduced endothelial cells. Concomitantly, a modest, non-size-selective enhancement of the barrier function was observed. In contrast, silencing of endogenous claudin-5 does not influence barrier function. The efficient sealing of the endothelium during diapedesis of monocytes or granulocytes is also claudin-5 independent. Collectively, these data provide evidence for a limited contribution of claudin-5 to the barrier function of human umbilical vein endothelial cells (HUVEC), implying that, unlike selective barriers in epithelia, the barrier of non-BBB endothelium seems largely independent of claudin-directed tight junction structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane Permeability
  • Cells, Cultured
  • Claudin-5
  • Endothelial Cells / metabolism*
  • Endothelial Cells / ultrastructure
  • Endothelium, Vascular / metabolism*
  • Fluorescent Antibody Technique
  • Freeze Fracturing
  • Gene Silencing
  • Humans
  • Lentivirus / genetics
  • Lentivirus / metabolism
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • RNA Interference
  • Tight Junctions / metabolism*

Substances

  • CLDN5 protein, human
  • Claudin-5
  • Membrane Proteins