title: Can the stress protein response be controlled by 'membrane-lipid therapy'?
abstract: In addition to high temperature, other stresses and clinical conditions such as cancer and diabetes can lead to the alteration of heat-shock protein (HSP) levels in cells. Moreover, HSPs can associate with either specific lipids or with areas of special membrane topology (such as lipid rafts), and changes in the physical state of cellular membranes can alter hsp gene expression. We propose that membrane microheterogeneity is important for regulating the HSP response. In support of this hypothesis, when particular membrane intercalating compounds are used to alter membrane properties, the simultaneous normalization of dysregulated expression of HSPs causes beneficial responses to disease states. Therefore, these compounds (such as hydroxylamine derivatives) have the potential to become a new class of pharmaceuticals for use in 'membrane-lipid therapy'.
authors.affiliation: Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, H-6726 Szeged, Hungary.
authors.forename: László
authors.initials: L
authors.lastname: Vigh
authors.forename: Ibolya
authors.initials: I
authors.lastname: Horváth
authors.forename: Bruno
authors.initials: B
authors.lastname: Maresca
authors.forename: John L
authors.initials: JL
authors.lastname: Harwood
mesh_terms: D000818:Animals; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D007328:Insulin / Q000378:metabolism; D008055:Lipids / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry*; D021962:Membrane Microdomains / Q000737:chemistry / Q000502:physiology*; D008954:Models, Biological; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D013696:Temperature
chemical_list: D006360:Heat-Shock Proteins; D007328:Insulin; D008055:Lipids; D008563:Membrane Lipids