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Enhancement of complement-induced cell lysis: a novel mechanism for the anticancer effects of Hsp90 inhibitors.

Abstract：

:Molecular chaperones (heat shock proteins, Hsp-s) play a pleiotropic role in immunological functions. Hsp-s participate in the presentation of peptide antigens, folding of several immunologically important proteins, such as the MHC, and in the maintenance of the activation-competent conformation of key signaling molecules (mostly serine/threonine and tyrosine kinases) of B and T cells activation. The most abundant cytoplasmic chaperone, Hsp90, is in the center of these processes. In recent years Hsp90 inhibitors emerged as very promising anticancer agents. Not surprisingly, Hsp90 inhibitors behave as immunosuppressants, and also cause an induction of superoxide production. Here we extend our previous data by showing the enhancement of complement-induced lysis of several types of tumor cells after Hsp90 inhibition. This novel mechanism may significantly contribute to the anticancer effects of Hsp90 inhibitors in vivo.

journal_name

Immunol Lett

journal_title

Immunology letters

authors

Sreedhar AS,Nardai G,Csermely P

doi

10.1016/j.imlet.2003.11.025

subject

Has Abstract

pub_date

2004-03-29 00:00:00

pages

157-61

issue

1-2

eissn

0165-2478

issn

1879-0542

pii

S0165247803003134

journal_volume

92

pub_type

杂志文章,评审

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