Dynamics and plasticity of Weibel-Palade bodies in endothelial cells

Arterioscler Thromb Vasc Biol. 2006 May;26(5):1002-7. doi: 10.1161/01.ATV.0000209501.56852.6c. Epub 2006 Feb 9.

Abstract

Agonist-induced release of endothelial cell specific storage granules, designated Weibel-Palade bodies (WPBs), provides the endothelium with the ability to rapidly respond to changes in its micro-environment. Originally being defined as an intracellular storage pool for von Willebrand factor (VWF), it has recently been shown that an increasing number of other components, including P-selectin, interleukin (IL)-8, eotaxin-3, endothelin-1, and angiopoietin-2, is present within this subcellular organelle, implicating a role for WPB exocytosis in inflammation, hemostasis, regulation of vascular tone and angiogenesis. Recent studies emphasize that WPBs provide a dynamic storage compartment whose contents can be regulated depending on the presence of inflammatory mediators in the vascular micro-environment. Additionally, release of WPBs is tightly regulated and feedback mechanisms have been identified that prevent excessive release of bioactive components from this subcellular organelle. The ability to regulate both contents and exocytosis of WPBs endows these endothelial cell specific organelles with a remarkable plasticity. This is most likely needed to allow for controlled delivery of bioactive components into the circulation on vascular perturbation.

Publication types

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

MeSH terms

  • Animals
  • Calcium / metabolism
  • Chemokine CCL26
  • Chemokines, CC / metabolism
  • Endothelial Cells / physiology
  • Endothelial Cells / ultrastructure*
  • Exocytosis
  • Humans
  • Interleukin-8 / metabolism
  • P-Selectin / metabolism
  • Weibel-Palade Bodies / physiology*
  • rab GTP-Binding Proteins / physiology
  • rab27 GTP-Binding Proteins
  • von Willebrand Factor / analysis

Substances

  • CCL26 protein, human
  • Chemokine CCL26
  • Chemokines, CC
  • Interleukin-8
  • P-Selectin
  • rab27 GTP-Binding Proteins
  • von Willebrand Factor
  • RAB27A protein, human
  • rab GTP-Binding Proteins
  • Calcium