Autophagy regulates endothelial cell processing, maturation and secretion of von Willebrand factor

Nat Med. 2013 Oct;19(10):1281-7. doi: 10.1038/nm.3288. Epub 2013 Sep 22.

Abstract

Endothelial secretion of von Willebrand factor (VWF) from intracellular organelles known as Weibel-Palade bodies (WPBs) is required for platelet adhesion to the injured vessel wall. Here we demonstrate that WPBs are often found near or within autophagosomes and that endothelial autophagosomes contain abundant VWF protein. Pharmacological inhibitors of autophagy or knockdown of the essential autophagy genes Atg5 or Atg7 inhibits the in vitro secretion of VWF. Furthermore, although mice with endothelial-specific deletion of Atg7 have normal vessel architecture and capillary density, they exhibit impaired epinephrine-stimulated VWF release, reduced levels of high-molecular weight VWF multimers and a corresponding prolongation of bleeding times. Endothelial-specific deletion of Atg5 or pharmacological inhibition of autophagic flux results in a similar in vivo alteration of hemostasis. Thus, autophagy regulates endothelial VWF secretion, and transient pharmacological inhibition of autophagic flux may be a useful strategy to prevent thrombotic events.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagy*
  • Autophagy-Related Protein 5
  • Autophagy-Related Protein 7
  • Endothelial Cells / metabolism*
  • Exocytosis
  • Hemostasis
  • Humans
  • Microtubule-Associated Proteins / genetics
  • Ubiquitin-Activating Enzymes / genetics
  • Weibel-Palade Bodies / metabolism
  • von Willebrand Factor / metabolism*

Substances

  • ATG5 protein, human
  • Autophagy-Related Protein 5
  • Microtubule-Associated Proteins
  • von Willebrand Factor
  • ATG7 protein, human
  • Autophagy-Related Protein 7
  • Ubiquitin-Activating Enzymes