Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide

被引:169
作者
Byrd, CA
Bornmann, W
Erdjument-Bromage, H
Tempst, P
Pavletich, N
Rosen, N
Nathan, CF
Ding, A
机构
[1] Cornell Univ, Weill Med Coll, Dept Microbiol & Immunol, New York, NY 10021 USA
[2] Cornell Univ, Weill Med Coll, Dept Med, New York, NY 10021 USA
[3] Mem Sloan Kettering Canc Ctr, Program Mol Biol, New York, NY 10021 USA
[4] Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA
[5] Mem Sloan Kettering Canc Ctr, Dept Med & Cell Biol, New York, NY 10021 USA
关键词
D O I
10.1073/pnas.96.10.5645
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Taxol, a plant-derived antitumor agent, stabilizes microtubules. Tasol also elicits cell signals in a manner indistinguishable from bacterial lipopolysaccharide (LPS), LPS-like actions of Taxol are controlled by the Ips gene and are independent of binding to the known Taxol target, beta-tubulin. Using biotin-labeled Taxol, avidin-agarose affinity chromatography, and peptide mass fingerprinting, we identified two Tasol targets from mouse macrophages and brain as heat shock proteins (Hsps) of the 70- and 90-kDa families. Geldanamycin, a specific inhibitor of the Hsp 90 family, blocked the nuclear translocation of NF-kappa B and expression of tumor necrosis factor in macrophages treated with Taxol or with LPS, Geldanamycin did not block microtubule bundling by Tasol or macrophage activation by tumor necrosis factor. Thus, Taxol binds Hsps, and Hsp 90 helps mediate the activation of macrophages by Taxol and by LPS.
引用
收藏
页码:5645 / 5650
页数:6
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