Extracellular MRP8/14 is a regulator of β2 integrin-dependent neutrophil slow rolling and adhesion

Nat Commun. 2015 Apr 20:6:6915. doi: 10.1038/ncomms7915.

Abstract

Myeloid-related proteins (MRPs) 8 and 14 are cytosolic proteins secreted from myeloid cells as proinflammatory mediators. Currently, the functional role of circulating extracellular MRP8/14 is unclear. Our present study identifies extracellular MRP8/14 as an autocrine player in the leukocyte adhesion cascade. We show that E-selectin-PSGL-1 interaction during neutrophil rolling triggers Mrp8/14 secretion. Released MRP8/14 in turn activates a TLR4-mediated, Rap1-GTPase-dependent pathway of rapid β2 integrin activation in neutrophils. This extracellular activation loop reduces leukocyte rolling velocity and stimulates adhesion. Thus, we identify Mrp8/14 and TLR4 as important modulators of the leukocyte recruitment cascade during inflammation in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CD18 Antigens / genetics
  • CD18 Antigens / metabolism*
  • Calgranulin A / genetics
  • Calgranulin A / metabolism*
  • Calgranulin B / genetics
  • Calgranulin B / metabolism*
  • Cell Adhesion / physiology*
  • Gene Expression Regulation
  • Hyaluronan Receptors / genetics
  • Hyaluronan Receptors / metabolism
  • Inflammation / chemically induced
  • Inflammation / metabolism
  • Leukocyte Rolling / physiology*
  • Macrophages / physiology
  • Male
  • Mice
  • Mice, Knockout
  • Neutrophils / physiology*
  • Protein Binding

Substances

  • CD18 Antigens
  • Calgranulin A
  • Calgranulin B
  • Hyaluronan Receptors
  • S100A9 protein, mouse
  • S100a8 protein, mouse