Zoekopdracht:
faculteit: "ACTA" en publicatiejaar: "2009"
| Auteurs | E.M. Molhoek, A.L. den Hertog, A.M.B.C. de Vries, K. Nazmi, E.C.I. Veerman, F.C. Hartgers, M. Yazdanbakhsh, F.J. Bikker, D. van der Kleij | | Titel | Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses |
| Tijdschrift | Biological chemistry |
| Jaargang | 390 |
| Jaar | 2009 |
| Nummer | 3 |
| Pagina's | 295-303 |
| ISSN | 14316730 |
| Faculteit | ACTA |
| Samenvatting | Cathelicidins are effector molecules of the innate host defense system that establish an antimicrobial barrier at epithelial interfaces. The human cathelicidin LL-37, in addition to its antimicrobial activity, also exhibits immunomodulatory effects, such as inhibition of pro-inflammatory responses to bacterial LPS in human monocytic cells. In this report, we demonstrate that LL-37 almost completely prevents the pro-inflammatory cytokine release by human peripheral blood mononuclear cells (PBMCs) following stimulation with Toll-like receptor (TLR)4 and TLR2/1 agonists while leaving TLR2/6, TLR5, TLR7 and TLR8 responses unchanged. Modulation of the TLR response by LL-37 occurred at least partly through the MAP kinase pathway via inhibition of p38 phosphorylation. By using an LL-37 library with overlapping sequences, we identified the mid-region of LL-37, comprising amino acids 13–31, as the active domain for the modulation of TLR responses. The mechanism of immunomodulation of LL-37 and LL-37 fragments is lipopoly-saccharide binding. Correlations between the capacity of LL-37 fragments to modulate TLR responses and their physico-chemical properties revealed that cationicity and hydrophobicity are essential for the modulation of LL-37-mediated TLR responses. |
| Soort document | Artikel |
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