DAMPs and NETs in Sepsis

Front Immunol. 2019 Oct 30:10:2536. doi: 10.3389/fimmu.2019.02536. eCollection 2019.

Abstract

Sepsis is a deadly inflammatory syndrome caused by an exaggerated immune response to infection. Much has been focused on host response to pathogens mediated through the interaction of pathogen-associated molecular patterns (PAMPs) and pattern recognition receptors (PRRs). PRRs are also activated by host nuclear, mitochondrial, and cytosolic proteins, known as damage-associated molecular patterns (DAMPs) that are released from cells during sepsis. Some well described members of the DAMP family are extracellular cold-inducible RNA-binding protein (eCIRP), high mobility group box 1 (HMGB1), histones, and adenosine triphosphate (ATP). DAMPs are released from the cell through inflammasome activation or passively following cell death. Similarly, neutrophil extracellular traps (NETs) are released from neutrophils during inflammation. NETs are webs of extracellular DNA decorated with histones, myeloperoxidase, and elastase. Although NETs contribute to pathogen clearance, excessive NET formation promotes inflammation and tissue damage in sepsis. Here, we review DAMPs and NETs and their crosstalk in sepsis with respect to their sources, activation, release, and function. A clear grasp of DAMPs, NETs and their interaction is crucial for the understanding of the pathophysiology of sepsis and for the development of novel sepsis therapeutics.

Keywords: CIRP; DAMPs (damage-associated molecular patterns); HMGB1 (high-mobility group box 1); NETs (neutrophil extracellular traps); cold-inducible RNA-binding protein; histone; neutrophils; sepsis.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Adenosine Triphosphate
  • Alarmins / genetics*
  • Alarmins / metabolism
  • Animals
  • Disease Susceptibility
  • Extracellular Traps
  • HMGB1 Protein / genetics
  • HMGB1 Protein / metabolism
  • Histones / metabolism
  • Humans
  • Neutrophils / immunology*
  • Neutrophils / metabolism*
  • Neutrophils / pathology
  • Protein Binding
  • Sepsis / etiology*
  • Sepsis / metabolism*
  • Sepsis / pathology
  • Signal Transduction

Substances

  • Alarmins
  • HMGB1 Protein
  • Histones
  • Adenosine Triphosphate