Antibacterial cathelicidin peptide CAP11 inhibits the lipopolysaccharide (LPS)-induced suppression of neutrophil apoptosis by blocking the binding of LPS to target cells

Inflamm Res. 2004 Nov;53(11):609-22. doi: 10.1007/s00011-004-1300-2.

Abstract

Objective: The action of antibacterial cathelicidin CAP11 (cationic antibacterial polypeptide of 11 kDa) on the lipopolysaccharide (LPS)-induced suppression of neutrophil apoptosis was evaluated in vitro.

Methods: Human neutrophils (10(6) cells/ml) were incubated alone or with mononuclear cells (6 x 10(5) cells/ml) in the presence of LPS (10 ng/ml) and CAP 11 (0.1 approximately 10 microg/ml), and neutrophil apoptosis was determined.

Results: LPS suppressed neutrophil apoptosis, accompanied with the activation of NF-kappaB, phosphorylation of extracellular signal-related protein kinase (ERK), expression of Bcl-XL (an anti-apoptotic protein) and inhibition of caspase 3 activity. Interestingly, CAP11 (> 1 microg/ml) reversed the actions of LPS to trigger these changes, and induced neutrophil apoptosis (p < 0.0001). Moreover, neutralizing antibodies against Mac-1 (CD11b/CD18) and Toll-like receptor (TLR) 4 completely blocked the LPS-induced suppression of neutrophil apoptosis (p < 0.0001), suggesting a major role of Mac-1 and TLR4 in the LPS-mediated neutrophil activation. In addition, LPS activated monocytes to produce proinflammatory cytokines (IL-1beta, TNF-alpha and IL-8) and inhibited neutrophil apoptosis. Importantly, CAP11 (> 1 microg/ml) reduced the cytokine production, thereby inducing neutrophil apoptosis (p < 0.0001). Finally, CAP11 (> 1 microg/ml) strongly suppressed the LPS-binding to neutrophils and monocytes (p < 0.01).

Conclusions: CAP11 is able to block the LPS-induced survival of neutrophils via the suppression of anti-apoptotic signaling in neutrophils and cytokine production from monocytes by inhibiting the binding of LPS to target cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimicrobial Cationic Peptides / pharmacology*
  • Apoptosis / drug effects*
  • Cells, Cultured
  • Coculture Techniques
  • Humans
  • Interleukin-1 / biosynthesis
  • Interleukin-8 / biosynthesis
  • Lipopolysaccharides / antagonists & inhibitors*
  • Lipopolysaccharides / immunology
  • Mitogen-Activated Protein Kinase 1 / metabolism
  • Mitogen-Activated Protein Kinase 3 / metabolism
  • Monocytes / drug effects*
  • Monocytes / immunology
  • Monocytes / metabolism
  • NF-kappa B / metabolism
  • Neutrophil Activation / drug effects
  • Neutrophils / drug effects*
  • Neutrophils / immunology
  • Neutrophils / metabolism
  • Phosphorylation / drug effects
  • Proto-Oncogene Proteins c-bcl-2 / biosynthesis
  • Tumor Necrosis Factor-alpha / biosynthesis
  • bcl-X Protein

Substances

  • Antimicrobial Cationic Peptides
  • BCL2L1 protein, human
  • CAP11 protein, Cavia
  • Interleukin-1
  • Interleukin-8
  • Lipopolysaccharides
  • NF-kappa B
  • Proto-Oncogene Proteins c-bcl-2
  • Tumor Necrosis Factor-alpha
  • bcl-X Protein
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3