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標題: The antimicrobial peptide, tilapia hepcidin 2-3, and PMA differentially regulate the protein kinase C isoforms, TNF-alpha and COX-2, in mouse RAW264.7 macrophages
作者: Rajanbabu, V.
Chen, J.Y.
關鍵字: Antimicrobial peptide;Tilapia hepcidin 2-3;PMA;PKC;TNF-alpha;COX-2;dendritic-like cells;lipopolysaccharide-induced differentiation;activation;phenotype;binding;sepsis;line;lps
Project: Peptides
期刊/報告no:: Peptides, Volume 32, Issue 2, Page(s) 333-341.
The antimicrobial and immunomodulatory functions of the antimicrobial peptide, tilapia hepcidin (TH)2-3, were previously studied. Herein, we report the differential modulation of protein kinase C (PKC)-associated proteins by TH2-3, and the PKC activator, phorbol 12-myristate 13-acetate (PMA), in RAW264.7 macrophages. Treatment with TH2-3 at 40 or 80 mu g/ml did not affect the cell morphology, but TH2-3 at 120 mu g/ml produced morphological changes similar to those after treatment with PMA in RAW264.7 cells. The coexistence of the PKC inhibitor, Ro-31-8220, prevented morphological changes induced by either PMA or 120 mu g/ml TH2-3 in RAW264.7 cells. Since PMA is known to induce expression of the proinflammatory cytokine, tumor necrosis factor (TNF)-alpha, activation of the TNF-alpha promoter in response to TH2-3 and PMA treatments in lipopolysaccharide (LPS)-stimulated cells was compared. In LPS-stimulated RAW264.7 cells, TNF-alpha promoter activity was significantly suppressed by TH2-3, but not by PMA. In addition, PMA activated prostaglandin synthase-associated cyclooxygenase (COX)-2 proteins on the cell surface, while the presence of TH2-3 inhibited its expression. Western blotting demonstrated that the expressions of PKC-mu, phosphorylated (p)-PKC mu at serine (S)-744, and p-PKC delta were activated by PMA, but were suppressed by TH2-3. In addition, p-PKC at S-916 was activated by TH2-3 and inhibited by PMA. In conclusion, the differential regulation of PKC isoforms by PMA and TH2-3 may influence morphological changes and regulation of TNF-alpha in RAW264.7 cells. (C) 2010 Elsevier Inc. All rights reserved.
ISSN: 0196-9781
DOI: 10.1016/j.peptides.2010.11.004
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