The C-terminus of murine S100A9 inhibits spreading and phagocytic activity of adherent peritoneal cells

Inflamm Res. 2005 May;54(5):204-10. doi: 10.1007/s00011-005-1344-y.

Abstract

Objective and design: In the present study, the effect of a synthetic peptide (H(92)-G(102)) identical to the C-terminus of murine S100A9 (mS100A9p) was investigated on adherent peritoneal cell function.

Materials and methods: For in vitro assays, peritoneal cells were obtained from the abdominal cavity of mice and incubated, with the different concentrations of mS100A9p, for 1 h, and then their spreading and phagocytosis activities were evaluated. For ex-vivo assays, cells obtained from animals treated for 1 h with the peptide were submitted to the mannose-receptor phagocytosis assay. Shorter homologue peptides to the C-terminus of mS100A9p were also evaluated on in vitro phagocytosis assays of Candida albicans particles.

Results: mS100A9p reduced both the spreading index and phagocytic activity, in vitro and ex-vivo, independent of the receptor evaluated. The homologue peptide corresponding to the H(92)-E(97) region of mS100A9p, the zinc-binding motif, was responsible for such an effect.

Conclusion: These results suggest a modulator effect of the C-terminus of S100A9 protein on the function of adherent peritoneal cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Calgranulin B / chemistry*
  • Calgranulin B / metabolism
  • Candida albicans / metabolism
  • Cell Adhesion
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Erythrocytes / cytology
  • Erythrocytes / microbiology
  • Macrophage Activation*
  • Macrophages, Peritoneal / cytology
  • Male
  • Mice
  • Peptides / chemistry
  • Peritoneum / cytology*
  • Phagocytosis
  • Protein Binding
  • Protein Structure, Tertiary
  • Sheep
  • Zinc / chemistry

Substances

  • Calgranulin B
  • Peptides
  • Zinc