title: High-density lipoprotein loses its anti-inflammatory properties during acute influenza a infection.
abstract: BACKGROUND
  Viruses have been identified as one of a variety of potential agents that are implicated in atherogenesis.
  
  
  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.
authors.affiliation: Department of Medicine, UCLA School of Medicine, Los Angeles, California, USA. bvanlent@mednet.ucla.edu
authors.forename: B J
authors.initials: BJ
authors.lastname: Van Lenten
authors.forename: A C
authors.initials: AC
authors.lastname: Wagner
authors.forename: D P
authors.initials: DP
authors.lastname: Nayak
authors.forename: S
authors.initials: S
authors.lastname: Hama
authors.forename: M
authors.initials: M
authors.lastname: Navab
authors.forename: A M
authors.initials: AM
authors.lastname: Fogelman
mesh_terms: D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase; D000208:Acute Disease; D000210:Acute-Phase Reaction / Q000378:metabolism / Q000821:virology; D000818:Animals; D001053:Apolipoproteins / Q000097:blood; D001158:Arteries / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D043303:Aryldialkylphosphatase; D002478:Cells, Cultured; D002570:Ceruloplasmin / Q000032:analysis / Q000378:metabolism; D002633:Chemotaxis / Q000187:drug effects; D051152:Clusterin; D004195:Disease Models, Animal; D004950:Esterases / Q000032:analysis / Q000378:metabolism; D005260:Female; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism; D006801:Humans; D007249:Inflammation / Q000097:blood* / Q000821:virology*; D009980:Influenza A virus / Q000254:growth & development / Q000302:isolation & purification; D007251:Influenza, Human / Q000097:blood* / Q000821:virology; D015850:Interleukin-6 / Q000097:blood; D008075:Lipoproteins, HDL / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D008077:Lipoproteins, LDL / Q000097:blood / Q000494:pharmacology; D008264:Macrophages / Q000187:drug effects / Q000378:metabolism; D051379:Mice; D008810:Mice, Inbred C57BL; D018832:Molecular Chaperones / Q000032:analysis / Q000378:metabolism; D009000:Monocytes / Q000187:drug effects / Q000378:metabolism; D010741:Phospholipases A / Q000032:analysis / Q000378:metabolism; D000685:Serum Amyloid A Protein
chemical_list: D001053:Apolipoproteins; C495242:CLU protein, human; C495243:Clu protein, mouse; D051152:Clusterin; D006023:Glycoproteins; D015850:Interleukin-6; D008075:Lipoproteins, HDL; D008077:Lipoproteins, LDL; D018832:Molecular Chaperones; D000685:Serum Amyloid A Protein; D002570:Ceruloplasmin; D004950:Esterases; D010741:Phospholipases A; D043203:1-Alkyl-2-acetylglycerophosphocholine Esterase; D043303:Aryldialkylphosphatase