High-density lipoprotein loses its anti-inflammatory properties during acute influenza a infection

Circulation. 2001 May 8;103(18):2283-8. doi: 10.1161/01.cir.103.18.2283.

Abstract

Background: Viruses have been identified as one of a variety of potential agents that are implicated in atherogenesis.

Methods and results: C57BL/6J mice were killed before or 2, 3, 5, 7, or 9 days after intranasal infection with 10(5) plaque-forming units (pfu) of Influenza A strain WSN/33. Peak infectivity in lungs was reached by 72 hours, and it returned to baseline by 9 days. No viremia was observed at any time. The activities of paraoxonase and platelet-activating factor acetylhydrolase in HDL decreased after infection and reached their lowest levels 7 days after inoculation. The ability of HDL from infected mice to inhibit LDL oxidation and LDL-induced monocyte chemotactic activity in human artery wall cell cocultures decreased with time after inoculation. Moreover, as the infection progressed, LDL more readily induced monocyte chemotaxis. Peak interleukin-6 and serum amyloid A plasma levels were observed at 2 and 7 days after inoculation. HDL apoA-I levels did not change. ApoJ and ceruloplasmin levels in HDL peaked 3 days after infection. Ceruloplasmin remained elevated throughout the time course, whereas apoJ levels decreased toward baseline after the third day.

Conclusions: We conclude that alterations in the relative levels of paraoxonase, platelet-activating factor acetylhydrolase, ceruloplasmin, and apoJ in HDL occur during acute influenza infection, causing HDL to lose its anti-inflammatory properties.

Publication types

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

MeSH terms

  • 1-Alkyl-2-acetylglycerophosphocholine Esterase
  • Acute Disease
  • Acute-Phase Reaction / metabolism
  • Acute-Phase Reaction / virology
  • Animals
  • Apolipoproteins / blood
  • Arteries / cytology
  • Arteries / drug effects
  • Arteries / metabolism
  • Aryldialkylphosphatase
  • Cells, Cultured
  • Ceruloplasmin / analysis
  • Ceruloplasmin / metabolism
  • Chemotaxis / drug effects
  • Clusterin
  • Disease Models, Animal
  • Esterases / analysis
  • Esterases / metabolism
  • Female
  • Glycoproteins / analysis
  • Glycoproteins / metabolism
  • Humans
  • Inflammation / blood*
  • Inflammation / virology*
  • Influenza A virus / growth & development
  • Influenza A virus / isolation & purification
  • Influenza, Human / blood*
  • Influenza, Human / virology
  • Interleukin-6 / blood
  • Lipoproteins, HDL / chemistry
  • Lipoproteins, HDL / metabolism*
  • Lipoproteins, HDL / pharmacology
  • Lipoproteins, LDL / blood
  • Lipoproteins, LDL / pharmacology
  • Macrophages / drug effects
  • Macrophages / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Molecular Chaperones / analysis
  • Molecular Chaperones / metabolism
  • Monocytes / drug effects
  • Monocytes / metabolism
  • Phospholipases A / analysis
  • Phospholipases A / metabolism
  • Serum Amyloid A Protein

Substances

  • Apolipoproteins
  • CLU protein, human
  • Clu protein, mouse
  • Clusterin
  • Glycoproteins
  • Interleukin-6
  • Lipoproteins, HDL
  • Lipoproteins, LDL
  • Molecular Chaperones
  • Serum Amyloid A Protein
  • Ceruloplasmin
  • Esterases
  • Phospholipases A
  • 1-Alkyl-2-acetylglycerophosphocholine Esterase
  • Aryldialkylphosphatase