Polyunsaturated fatty acids enhance the heat induced stress response in rainbow trout (Oncorhynchus mykiss) leukocytes

Samples, B.; Pool, Gary L.; Lumb, Roger H.

doi:10.1016/s0305-0491(99)00083-8

Cited by 29 publications

(19 citation statements)

References 37 publications

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“…This model also implies that the wide variations of membrane lipids in cells and tissues may provide cell-specific response to combinations of intraand extracellular stress signals. Close correlations between changes in composition and physical order of membranes and cellular stress response have been widely documented (8,9,29,30). Combining these observations with our results, we conclude that BM and its derivatives may partially elicit their effect by interacting with specific lipid components in the cellular membranes and may activate membrane-associated signaling cascade(s) linked to the heat shock response.…”

Section: Discussionsupporting

confidence: 85%

“…Protein function influenced by membrane fluidity and͞or heterogeneity has been suggested for phospholipase A 2 , the enzymatic activity of which is known to be stimulated by heat shock (30). Elevated activity of membrane-bound phospholipases and the resultant release of lipid mediators could also enhance the subsequent membrane association and activation of protein kinase C, found to drive the phosphorylation of HSFs (32).…”

Section: Discussionmentioning

confidence: 99%

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

Török

Tsvetkova

Balogh

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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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.

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Section: Discussionsupporting

confidence: 85%

Section: Discussionmentioning

confidence: 99%

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

Török

Tsvetkova

Balogh

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…Perturbation of the organization and phase state of acidic glycerophospholipids, the major determinants of the activity of membrane proteins ( van Klompenburg et al ., 1997 ), by nontoxic drugs like bimoclomol may influence the structure/activity of membrane‐bound proteins without direct drug–protein interaction. Protein function influenced by membrane fluidity and/or microheterogeneity has been suggested for phospholipase A 2 , which is stimulated by heat shock, resulting in arachidonic acid release ( Honger et al ., 1996 ; Samples et al ., 1999 ). Arachidonic acid stimulates HSF–DNA binding, increases phosphorylation of HSF‐1 and upregulates transcription of the Hsp70 gene in HeLa cells ( Jurivich et al ., 1994 ).…”

Section: Cellular Membranes Act As Alternative Thermosensors To Regulmentioning

confidence: 99%

Heat shock proteins as emerging therapeutic targets

Sőti

Nagy

Giricz

et al. 2005

British J Pharmacology

345

251

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Chaperones (stress proteins) are essential proteins to help the formation and maintenance of the proper conformation of other proteins and to promote cell survival after a large variety of environmental stresses. Therefore, normal chaperone function is a key factor for endogenous stress adaptation of several tissues. However, altered chaperone function has been associated with the development of several diseases; therefore, modulators of chaperone activities became a new and emerging field of drug development. Inhibition of the 90 kDa heat shock protein (Hsp)90 recently emerged as a very promising tool to combat various forms of cancer. On the other hand, the induction of the 70 kDa Hsp70 has been proved to be an efficient help in the recovery from a large number of diseases, such as, for example, ischemic heart disease, diabetes and neurodegeneration. Development of membrane-interacting drugs to modify specific membrane domains, thereby modulating heat shock response, may be of considerable therapeutic benefit as well. In this review, we give an overview of the therapeutic approaches and list some of the key questions of drug development in this novel and promising therapeutic approach.

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“…Physical strains in membrane microenvironments may make certain phospholipids available to phospholipases associated with the membrane, causing their activity to increase, resulting in release of lipid mediators. These in turn could interact with known domains of HSF, driving their activation, DNA binding and subsequent hsp synthesis (Samples et al 1999).…”

Section: Discussionmentioning

confidence: 99%

Analysis of Stress-Induced Gene Expression in Trout Red Blood cells following Tributyltinchloride Exposure

Tiano

Davies²,

Craft

et al. 2004

Fish Physiol Biochem

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Submicromolar concentrations of tributyltinchloride (TBTC), an organotin compound, is able to impair mitochondrial activity in trout erythrocytes, as detected by ultrastructural transmission electron microscopy investigations and exhibits pro apoptotic activity in a variety of cells including nucleated red blood cells. Here we show that TBTC is able to induce the expression of hsp70 in rainbow trout (Onchorynchus mykiss) erythrocytes in a time-and dose-dependent manner. This induction was demonstrated by quantification of the relative abundance of mRNA, and the synthesis of hsp70 was detected by means of an immunological test. This study could provide a practical assay of environmental stress at sublethal toxicant concentrations.

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Polyunsaturated fatty acids enhance the heat induced stress response in rainbow trout (Oncorhynchus mykiss) leukocytes

Cited by 29 publications

References 37 publications

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

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

Heat shock proteins as emerging therapeutic targets

Analysis of Stress-Induced Gene Expression in Trout Red Blood cells following Tributyltinchloride Exposure

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