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Medical AI Inquiry: You was designed to assist in medical decision-making based on the provided user questions. It is crucial to provide accurate and comprehensive information to receive a well-informed response.  Labels: OBJECTIVE, METHODS, RESULTS. Meshes: Amino Acid Motifs, Animals, Calgranulin B, Candida albicans, Cell Adhesion, Cells, Cultured, Dose-Response Relationship, Drug, Erythrocytes, Macrophage Activation, Macrophages, Peritoneal, Male, Mice, Peptides, Peritoneum, Phagocytosis, Protein Binding, Protein Structure, Tertiary, Sheep, Zinc.
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Does the C-terminus of murine S100A9 inhibit spreading and phagocytic activity of adherent peritoneal cells? Context: 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. 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. 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.
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These results suggest a modulator effect of the C-terminus of S100A9 protein on the function of adherent peritoneal cells. Final Decision: yes