articleThe Journal of ImmunologyMar 1, 2003BRONZE OA

Proinflammatory Activities of S100: Proteins S100A8, S100A9, and S100A8/A9 Induce Neutrophil Chemotaxis and Adhesion

Université Laval

PubMed
Indexed incrossrefpubmed

Abstract

S100A8 and S100A9 are small calcium-binding proteins that are highly expressed in neutrophil and monocyte cytosol and are found at high levels in the extracellular milieu during inflammatory conditions. Although reports have proposed a proinflammatory role for these proteins, their extracellular activity remains controversial. In this study, we report that S100A8, S100A9, and S100A8/A9 caused neutrophil chemotaxis at concentrations of 10(-12)-10(-9) M. S100A8, S100A9, and S100A8/A9 stimulated shedding of L-selectin, up-regulated and activated Mac-1, and induced neutrophil adhesion to fibrinogen in vitro. Neutralization with Ab showed that this adhesion was mediated by Mac-1. Neutrophil adhesion was also…

Citation impact

857
total citations
FWCI
7.79
Percentile
100%
References
56
Citations per year

Authors

5

Topics & keywords

Keywords
  • S100A8
  • S100A9
  • Neutrophil extracellular traps
  • Proinflammatory cytokine
  • Chemotaxis
  • Extracellular
  • Inflammation
  • Cell biology
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