NDLI: Heat shock protein coinducers with no effect on protein denaturation specifically modulate the membrane lipid phase

Content Provider	PubMed Central
Author	Török, Zsolt Tsvetkova, Nelly M. Balogh, Gábor Horváth, Ibolya Nagy, Enikő Pénzes, Zoltán Hargitai, Judit Bensaude, Olivier Csermely, Péter Crowe, John H. Maresca, Bruno László, Vígh
Copyright Year	2003
Abstract	The hydroxylamine derivative bimoclomol (BM) has been shown to activate natural cytoprotective homeostatic responses by enhancing the capability of cells to cope with various pathophysiological conditions. It exerts its effect in synergy with low levels of stress to induce the synthesis of members of major stress protein families. We show here that the presence of BM does not influence protein denaturation in the cells. BM and its derivatives selectively interact with acidic lipids and modulate their thermal and dynamic properties. BM acts as a membrane fluidizer at normal temperature, but it is a highly efficient membrane stabilizer, inhibiting the bilayer–nonbilayer phase transitions during severe heat shock. We suggest that BM and the related compounds modify those domains of membrane lipids where the thermally or chemically induced perturbation of lipid phase is sensed and transduced into a cellular signal, leading to enhanced activation of heat shock genes. BM may be a prototype for clinically safe membrane-interacting drug candidates that rebalance the level and composition of heat shock proteins.
Related Links	http://dx.doi.org/10.1073/pnas.0438003100
Ending Page	3136
Page Count	6
Starting Page	3131
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	100
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2003-03-18
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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