Cathelicidin LL-37 peptide regulates endothelial cell stiffness and endothelial barrier permeability

Am J Physiol Cell Physiol. 2011 Jan;300(1):C105-12. doi: 10.1152/ajpcell.00158.2010. Epub 2010 Oct 13.

Abstract

LL-37 peptide is a multifunctional host defense molecule essential for normal immune responses to infection or tissue injury. In this study we assess the impact of LL-37 on endothelial stiffness and barrier permeability. Fluorescence microscopy reveals membrane localization of LL-37 after its incubation with human umbilical vein endothelial cells (HUVECs). A concentration-dependent increase in stiffness was observed in HUVECs, bovine aortic endothelial cells (BAECs), human pulmonary microvascular endothelial cells, and mouse aorta upon LL-37 (0.5-5 μM) addition. Stiffening of BAECs by LL-37 was blocked by P2X7 receptor antagonists and by the intracellular Ca²(+) chelator BAPTA-AM. Increased cellular stiffness correlated with a decrease in permeability of HUVEC cell monolayers after LL-37 addition compared with nontreated cells, which was similar to the effect observed upon treatment with sphingosine 1-phosphate, and both treatments increased F-actin content in the cortical region of the cells. These results suggest that the antiinflammatory effect of LL-37 at the site of infection or injury involves an LL-37-mediated increase in cell stiffening that prevents increased pericellular permeability. Such a mechanism may help to maintain tissue fluid homeostasis.

Publication types

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

MeSH terms

  • Actins / physiology
  • Adherens Junctions / physiology
  • Animals
  • Antimicrobial Cationic Peptides / metabolism*
  • Antimicrobial Cationic Peptides / pharmacology*
  • Aorta / drug effects
  • Cathelicidins
  • Cattle
  • Cell Membrane
  • Cells, Cultured
  • Cytoskeleton / physiology
  • Endothelial Cells / cytology*
  • Endothelial Cells / physiology*
  • Humans
  • Mice
  • Permeability / drug effects

Substances

  • Actins
  • Antimicrobial Cationic Peptides
  • Cathelicidins