Different heat shock protein 60 species share pro‐inflammatory activity but not binding sites on macrophages

FEBS Letters

Burkart, Volker²  Kempe, Karina²  Habich, Christiane²  Kolb, Hubert²  van der Zee, Ruurd¹ 

[1] Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80 165, 3508 TD Utrecht, The Netherlands;German Diabetes Research Institute at the Heinrich-Heine-University of Düsseldorf, Auf'm Hennekamp 65, 40225 Düsseldorf, Germany

关键词: Heat shock protein 60;    Innate immunity;    Macrophage receptor;    Tumor necrosis factor α;    hsp60;    heat shock protein 60;    LPS;    lipopolysaccharide;    BSA;    bovine serum albumin;    OVA;    ovalbumin;    TLR;    toll-like receptor;   

DOI  :  10.1016/S0014-5793(02)03772-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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, TNFα production was induced by 0.1 μM 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.

【 授权许可】

Unknown