Suppressive effects of lysozyme on polyphosphate-mediated vascular inflammatory responses

Biochem Biophys Res Commun. 2016 Jun 10;474(4):715-721. doi: 10.1016/j.bbrc.2016.05.016. Epub 2016 May 4.

Abstract

Lysozyme, found in relatively high concentration in blood, saliva, tears, and milk, protects us from the ever-present danger of bacterial infection. Previous studies have reported proinflammatory responses of endothelial cells to the release of polyphosphate(PolyP). In this study, we examined the anti-inflammatory responses and mechanisms of lysozyme and its effects on PolyP-induced septic activities in human umbilical vein endothelial cells (HUVECs) and mice. The survival rates, septic biomarker levels, behavior of human neutrophils, and vascular permeability were determined in PolyP-activated HUVECs and mice. Lysozyme suppressed the PolyP-mediated vascular barrier permeability, upregulation of inflammatory biomarkers, adhesion/migration of leukocytes, and activation and/or production of nuclear factor-κB, tumor necrosis factor-α, and interleukin-6. Furthermore, lysozyme demonstrated protective effects on PolyP-mediated lethal death and the levels of the related septic biomarkers. Therefore, these results indicated the therapeutic potential of lysozyme on various systemic inflammatory diseases, such as sepsis or septic shock.

Keywords: Barrier integrity; Inflammation; Lysozyme; Polyphosphate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Inflammatory Agents / administration & dosage
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Endothelial Cells / drug effects
  • Endothelial Cells / immunology*
  • Humans
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Muramidase / administration & dosage*
  • Polyphosphates / immunology*
  • Sepsis / drug therapy*
  • Sepsis / immunology
  • Treatment Outcome
  • Umbilical Veins / drug effects
  • Vasculitis / drug therapy*
  • Vasculitis / immunology*

Substances

  • Anti-Inflammatory Agents
  • Polyphosphates
  • Muramidase