Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages.
In a study of seven different hsp60 species, we found that all mammalian and microbial proteins shared the property of eliciting an inflammatory response in mouse macrophages. In all cases, TNFalpha production was induced by 0.1 microM concentrations of hsp60. However, the different hsp60 preparations did not compete for the same binding site. The binding of fluorescence-labeled human hsp60 was inhibited by excess unlabeled human, rat or mouse hsp60, but not hamster, Escherichia coli, Chlamydia pneumoniae or Mycobacterium bovis hsp60. We conclude that phylogenetically separate hsp60 species interact with innate immune cells via different recognition pathways.
Habich
Christiane
C
German Diabetes Research Institute at the Heinrich-Heine-University of Düsseldorf, Auf'm Hennekamp 65, 40225, Düsseldorf, Germany. christiane.habich@ddfi.uni-duesseldorf.de
Kempe
Karina
K
van der Zee
Ruurd
R
Burkart
Volker
V
Kolb
Hubert
H
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D002460:Cell Line; D018834:Chaperonin 60 / Q000378:metabolism* / Q000494:pharmacology*; D016993:Chlamydophila pneumoniae / Q000378:metabolism; D006224:Cricetinae; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D018836:Inflammation Mediators / Q000378:metabolism* / Q000494:pharmacology*; D008264:Macrophages / Q000187:drug effects* / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D008809:Mice, Inbred C3H; D008817:Mice, Mutant Strains; D009163:Mycobacterium bovis / Q000378:metabolism; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D013045:Species Specificity; D014409:Tumor Necrosis Factor-alpha / Q000096:biosynthesis
D001426:Bacterial Proteins; D018834:Chaperonin 60; D018836:Inflammation Mediators; D011994:Recombinant Proteins; D014409:Tumor Necrosis Factor-alpha