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

被引：36

作者：

Habich, C

Kempe, K

van der Zee, R

Burkart, V

Kolb, H

机构：

[1] Univ Dusseldorf, German Diabet Res Inst, D-40225 Dusseldorf, Germany

[2] Univ Utrecht, Fac Vet Med, Dept Immunol & Infect Dis, NL-3508 TD Utrecht, Netherlands

来源：

FEBS LETTERS | 2003年 / 533卷 / 1-3期

关键词：

heat shock protein 60; innate immunity; macrophage receptor; tumor necrosis factor alpha;

D O I：

10.1016/S0014-5793(02)03772-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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, TNFalpha production was induced by 0.1 muM 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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：105 / 109

页数：5

共 29 条

[1] T cell proliferative responses of type 1 diabetes patients and healthy individuals to human hsp60 and its peptides [J].