Iron primes hepatic macrophages for NF-kappaB activation in alcoholic liver injury

Am J Physiol. 1999 Dec;277(6):G1240-50. doi: 10.1152/ajpgi.1999.277.6.G1240.

Abstract

NF-kappaB activation induced by lipopolysaccharide (LPS) in cultured hepatic macrophages (HM) may be abrogated by pretreatment of cells with a lipophilic iron chelator, 1,2-dimethyl-3-hydroxypyrid-4-one (L1, deferiprone), suggesting a role for iron in this molecular event [M. Lin, M., R. A. Rippe, O. Niemelä, G. Brittenham, and H. Tsukamoto, Am. J. Physiol. 272 (Gastrointest. Liver Physiol. 35): G1355-G1364, 1997]. To ascertain the relevance in vivo of this hypothesis, HM from an experimental model of alcoholic liver injury were examined for the relationship between nuclear factor (NF)-kappaB activation and iron storage. HM showed a significant increase in nonheme iron concentration (+70%), accompanied by enhanced generation of electron paramagnetic resonance-detected radicals (+200%), NF-kappaB activation (+100%), and tumor necrosis factor-alpha (+150%) and macrophage inflammatory protein-1 (+280%) mRNA induction. Treatment of the cells ex vivo with L1 normalized all these parameters. HM content of ferritin protein, ferritin L chain mRNA, and hemeoxygenase-1 mRNA and splenic content of nonheme iron were increased, suggesting enhanced heme turnover as a cause of the increased iron storage and NF-kappaB activation. To test this possibility, increased iron content in HM was reproduced in vitro by phagocytosis of heat-treated red blood cells. Treatment caused a 40% increase in nonheme iron concentration and accentuated LPS-induced NF-kappaB activation twofold. Both effects could be abolished by pretreatment of cells with zinc protoporphyrin, a hemeoxygenase inhibitor. To extend this observation, animals were splenectomized before 9-wk alcohol feeding. Splenectomy resulted in further increments in HM nonheme iron storage (+60%) and NF-kappaB activation (+90%) and mononuclear cell infiltration (+450%), particularly around the iron-loaded HM in alcohol-fed animals. These results support the pivotal role of heme-derived iron in priming HM for NF-kappaB activation and expression of proinflammatory genes in alcoholic liver injury.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoferritins
  • Calcium-Binding Proteins / pharmacology
  • Central Nervous System Depressants / pharmacology
  • Chemokine CCL4
  • Disease Models, Animal
  • Erythrocytes
  • Ethanol / pharmacology
  • Ferritins / genetics
  • Gene Expression / physiology
  • Heme Oxygenase (Decyclizing) / genetics
  • Hepatitis, Alcoholic / drug therapy
  • Hepatitis, Alcoholic / immunology
  • Hepatitis, Alcoholic / metabolism*
  • Iron / metabolism*
  • Kupffer Cells / drug effects
  • Kupffer Cells / enzymology*
  • Kupffer Cells / immunology
  • Leukocyte L1 Antigen Complex
  • Lipopolysaccharides / pharmacology
  • Liver / cytology
  • Liver / drug effects*
  • Liver / immunology
  • Macrophage Inflammatory Proteins / genetics
  • Male
  • Membrane Glycoproteins / pharmacology
  • NF-kappa B / immunology
  • NF-kappa B / metabolism*
  • Neural Cell Adhesion Molecules / pharmacology
  • Phagocytosis / immunology
  • Picolines / metabolism
  • Proto-Oncogene Proteins / metabolism
  • RNA, Messenger / analysis
  • Rats
  • Rats, Wistar
  • Splenectomy
  • Tumor Necrosis Factor-alpha / genetics
  • Wnt2 Protein

Substances

  • Calcium-Binding Proteins
  • Central Nervous System Depressants
  • Chemokine CCL4
  • Leukocyte L1 Antigen Complex
  • Lipopolysaccharides
  • Macrophage Inflammatory Proteins
  • Membrane Glycoproteins
  • NF-kappa B
  • Neural Cell Adhesion Molecules
  • Picolines
  • Proto-Oncogene Proteins
  • RNA, Messenger
  • Tumor Necrosis Factor-alpha
  • Wnt2 Protein
  • Ethanol
  • 2-tert-butyl-6-methyl-3-hydroxypyridine
  • Ferritins
  • Apoferritins
  • Iron
  • Heme Oxygenase (Decyclizing)