Bikunin suppresses lipopolysaccharide-induced lethality through down-regulation of tumor necrosis factor- alpha and interleukin-1 beta in macrophages

J Infect Dis. 2005 Mar 15;191(6):930-8. doi: 10.1086/428134. Epub 2005 Feb 11.

Abstract

Background: Lipopolysaccharide (LPS) is the primary mediator of gram-negative sepsis; it induces the production of macrophage-derived cytokines. It has been shown that bikunin, a Kunitz-type protease inhibitor, inhibits LPS-induced cytokine expression.

Methods: To explore the role of bikunin, bikunin knockout (Bik(-/-)) mice were used for in vitro cytokine experiments and in vivo animal models.

Results: We show that a higher level of LPS-mediated death was induced in Bik(-/-), compared with wild-type (wt), mice; the administration of bikunin caused a significant reduction in LPS-induced lethality; LPS significantly increased tumor necrosis factor (TNF)- alpha and interleukin-1 beta levels in Bik(-/-), relative to wt, mice after LPS challenge; concomitant administration of bikunin inhibited the LPS-induced plasma levels of these cytokines; bikunin suppressed the LPS-induced up-regulation of cytokine expression through the suppression of the phosphorylation of ERK1/2, JNK, and p38 in macrophages; and LPS-induced up-regulation of TNF- alpha expression was not enhanced in Bik(-/-) macrophages without endogenous bikunin.

Conclusions: These data allow us to speculate that the increased sensitivity of Bik(-/-) mice to LPS-induced death in vivo is due to a lack of circulating bikunin in plasma. Bikunin may play a role as a potent anti-inflammatory agent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Down-Regulation*
  • Inflammation / drug therapy
  • Inflammation / mortality*
  • Interleukin-1 / metabolism*
  • Lipopolysaccharides / pharmacology
  • Macrophage Activation
  • Macrophages, Peritoneal / immunology*
  • Macrophages, Peritoneal / metabolism
  • Membrane Glycoproteins / administration & dosage
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / pharmacology
  • Membrane Glycoproteins / physiology*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Serine Proteinase Inhibitors / administration & dosage
  • Serine Proteinase Inhibitors / genetics
  • Serine Proteinase Inhibitors / pharmacology
  • Trypsin Inhibitor, Kunitz Soybean / administration & dosage
  • Trypsin Inhibitor, Kunitz Soybean / genetics
  • Trypsin Inhibitor, Kunitz Soybean / pharmacology
  • Tumor Necrosis Factor-alpha / metabolism*

Substances

  • Interleukin-1
  • Lipopolysaccharides
  • Membrane Glycoproteins
  • SPINT2 protein, human
  • Serine Proteinase Inhibitors
  • Tumor Necrosis Factor-alpha
  • Trypsin Inhibitor, Kunitz Soybean