Academic literature on the topic 'Heat shock proteins – Physiological effect'
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Journal articles on the topic "Heat shock proteins – Physiological effect"
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Sun, Xiaonan, Sharadhi Siri, Amirah Hurst, and Hongyu Qiu. "Heat Shock Protein 22 in Physiological and Pathological Hearts: Small Molecule, Large Potentials." Cells 11, no. 1 (2021): 114. http://dx.doi.org/10.3390/cells11010114.
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Small heat shock protein 22 (HSP22) belongs to the superfamily of heat shock proteins and is predominantly expressed in the heart, brain, skeletal muscle, and different types of cancers. It has been found that HSP22 is involved in variant cellular functions in cardiomyocytes and plays a vital role in cardiac protection against cardiomyocyte injury under diverse stress. This review summarizes the multiple functions of HSP22 in the heart and the underlying molecular mechanisms through modulating gene transcription, post-translational modification, subcellular translocation of its interacting proteins, and protein degradation, facilitating mitochondrial function, cardiac metabolism, autophagy, and ROS production and antiapoptotic effect. We also discuss the association of HSP22 in cardiac pathologies, including human dilated cardiomyopathy, pressure overload-induced heart failure, ischemic heart diseases, and aging-related cardiac metabolism disorder. The collected information would provide insights into the understanding of the HSP22 in heart diseases and lead to discovering the therapeutic targets.
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Paull, Robert E., and Chris B. Watkins. "Are the Effects of Heat on Physiology Due to Heat Shock Proteins?" HortScience 31, no. 4 (1996): 691c—691. http://dx.doi.org/10.21273/hortsci.31.4.691c.
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Production of heat shock proteins (HSP) in response to high temperatures are a highly recognizable feature of plant and animal systems. It is thought that such proteins play a critical role in survival under supraoptimal temperature conditions. The use of heat treatments has been examined extensively, especially for disinfestation of fruit and disease control. Heat treatments can affect physiological responses, such as ethylene production, softening, and other ripening factors, as well as reducing physiological disorders, including chilling injury. HSPs have been implicated in a number of stress responses, but the extent that they are involved, especially in amelioration of chilling injury, is a subject of debate. In a number of cases, heat shock proteins do not appear to be involved, and HSPs do not explain long-term adaptation to heat; other systems for which we do not have models may be at work. Resolution of these issues may require the use of transgenic plants with modified heat shock responses.
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Nannapaneni, Sreeja, Gnana Sri Deepika Vusthepalli, Pavan Santhosh Guptha Vusthepalli, Kusuma Naredla, Kavya Gowd Aitha, and Suryanarayana Veeravilli. "CLINICAL AND THERAPEUTIC SIGNIFICANCE OF HEAT SHOCK PROTEINS." International Journal of Advanced Research 9, no. 02 (2021): 961–64. http://dx.doi.org/10.21474/ijar01/12539.
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Multiple experimental investigations have been successful in suggesting the role of heat shock protein as a clinical biomarker and therapeutic target in several diseases. All living cells, from the simplest prokaryote to the most complex multicellular organism, contain heat shock proteins-molecular chaperones that are responsible for management of unfolded polypeptides within the cell. In view of the fundamental role of heat shock proteins in maintenance of protein homeostasis, it seems likely that malfunctions associated with members of heat shock protein families would have pathological effects. Such effects might be minimal under normal physiological conditions, but could be exacerbated at times. This review provides an overview of the cell biology and immunology of heat shock proteins focusing predominantly on immunological responses to heat shock proteins in a range of immune-mediated diseases and in infectious diseases.
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Bernstein, Harris D., and Janine B. Hyndman. "Physiological Basis for Conservation of the Signal Recognition Particle Targeting Pathway in Escherichia coli." Journal of Bacteriology 183, no. 7 (2001): 2187–97. http://dx.doi.org/10.1128/jb.183.7.2187-2197.2001.
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ABSTRACT The Escherichia coli signal recognition particle (SRP) is a ribonucleoprotein complex that targets nascent inner membrane proteins (IMPs) to transport sites in the inner membrane (IM). Since SRP depletion only partially inhibits IMP insertion under some growth conditions, however, it is not clear why the particle is absolutely essential for viability. Insights into this question emerged from experiments in which we analyzed the physiological consequences of reducing the intracellular concentration of SRP below the wild-type level. We found that even moderate SRP deficiencies that have little effect on cell growth led to the induction of a heat shock response. Genetic manipulations that suppress the heat shock response were lethal in SRP-deficient cells, indicating that the elevated synthesis of heat shock proteins plays an important role in maintaining cell viability. Although it is conceivable that the heat shock response serves to increase the capacity of cells to target IMPs via chaperone-based mechanisms, SRP-deficient cells did not show an increased dependence on either GroEL or DnaK. By contrast, the heat shock-regulated proteases Lon and ClpQ became essential for viability when SRP levels were reduced. These results suggest that the heat shock response protects SRP-deficient cells by increasing their capacity to degrade mislocalized IMPs. Consistent with this notion, a model IMP that was mislocalized in the cytoplasm as the result of SRP depletion appeared to be more stable in a Δlon ΔclpQ strain than in control cells. Taken together, the data provide direct evidence that SRP is essential in E. coli and possibly conserved throughout prokaryotic evolution as well partly because efficient IMP targeting prevents a toxic accumulation of aggregated proteins in the cytoplasm.
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Russell, A. D. "Lethal Effects of Heat on Bacterial Physiology and Structure." Science Progress 86, no. 1-2 (2003): 115–37. http://dx.doi.org/10.3184/003685003783238699.
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High temperatures have profound effects on the structural and physiological properties of sporulating and non-sporulating bacteria, with membranes, RNA, DNA, ribosomes, protein and enzymes all affected. Nevertheless, it is apparent that no one single event is responsible for cell death. The induction of intracellular heat-shock proteins and the activation of extracellular alarmones in vegetative cells exposed to mildly lethal temperatures are important cell responses. In bacterial spores, several factors contribute to the overall resistance to moist (wet) and dry heat; the latter, but not the former, induces mutations. Heat resistance develops during sporulation, when spore-specific heat-shock proteins are also produced. Heat sensitivity is regained during germination of spores.
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Neuer, A., S. D. Spandorfer, P. Giraldo, et al. "Heat Shock Protein Expression During Gametogenesis and Embryogenesis." Infectious Diseases in Obstetrics and Gynecology 7, no. 1-2 (1999): 10–16. http://dx.doi.org/10.1155/s1064744999000034.
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When cells are subjected to various stress factors, they increase the production of a group of proteins called heat shock proteins (hsp). Heat shock proteins are highly conserved proteins present in organisms ranging from bacteria to man. Heat shock proteins enable cells to survive adverse environmental conditions by preventing protein denaturation. Thus the physiological and pathological potential of hsps is enormous and has been studied widely over the past two decades. The presence or absence of hsps influences almost every aspect of reproduction. They are among the first proteins produced during mammalian embryo development. In this report, the production of hsps in gametogenesis and early embryo development is described. It has been suggested that prolonged and asymptomatic infections trigger immunity to microbial hsp epitopes that are also expressed in man. This may be relevant for human reproduction, since many couples with fertility problems have had a previous genital tract infection. Antibodies to bacterial and human hsps are present at high titers in sera of many patients undergoing in vitro fertilization. In a mouse embryo culture model, these antibodies impaired the mouse embryo development at unique developmental stages. The gross morphology of these embryos resembled cells undergoing apoptosis. The TUNEL (terminal deoxynucleotidyl transferase-mediated X-dUTP nick end labeling) staining pattern, which is a common marker of apoptosis, revealed that embryos cultured in the presence of hsp antibodies stained TUNEL-positive more often than unexposed embryos. These data extend preexisting findings showing the detrimental effect of immune sensitization to hsps on embryo development. Infect. Dis. Obstet. Gynecol. 7:10–16, 1999.
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Jolly, Emmitt R. "HSP70, HSP90A, and HSP90B are Differentially Regulated in Response to Thermal, Osmotic and Hypoxic Stressors." Annals of Experimental and Molecular Biology 1, no. 1 (2018): 1–9. http://dx.doi.org/10.23880/aemb-16000101.
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The Heat shock proteins, Hsp70 and Hsp90 are highly conserved and play a significant role in cellular response to a variety of stressors. In response to stressors, cellular expression levels of these heat shock proteins are increased to stabilize degrading proteins and to initiate thermotolerance among other complex functions. Maintenance of physiological temperature in all organisms is imperative to ensure that biological systems function normally. This is especially critical for cold-blooded organisms whose internal temperature is subject to their environmental conditions. High temperatures and other stressors can deleteriously affect animal motility, its ability to avoid predators, neuronal activity and affect neuropeptide populations. However, the effect of stressors on muscle and on neuronal activity are not always equal. Here we use the important commercially important Jonah crab, Cancer borealis as a model to assess the effect of different stressors on transcript levels of the major heat shock proteins, HSP70, HSP90A and HSP90B. Since these genes have not been identified or sequenced in C borealis, we cloned each gene and we demonstrate that a) these genes have different expression profiles in thermal, osmotic and hypoxic stresses and that b) these genes are differentially expressed in muscle and brain cells.
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Yang, S. H., A. Nussenzweig, L. Li, et al. "Modulation of thermal induction of hsp70 expression by Ku autoantigen or its individual subunits." Molecular and Cellular Biology 16, no. 7 (1996): 3799–806. http://dx.doi.org/10.1128/mcb.16.7.3799.
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Previously, we proposed a dual control mechanism for the regulation of the heat shock response in mammalian cells: a positive control mediated by the heat shock transcription factor HSF1 and a negative control mediated by the constitutive heat shock element-binding factor (CHBF). To study the physiological role of CHBF in the regulation of heat shock response, we purified CHBF to apparent homogeneity and showed it to be identical to the Ku autoantigen, a heterodimer consisting of 70-kDa (Ku-70) and 86-kDa (Ku-80) polypeptides. To study further the functional significance of Ku/CHBF in the cellular response to heat shock, we established rodent cell lines that stably and constitutively overexpressed one or both subunits of the human Ku protein, and examined the thermal induction of hsp70 and other heat shock proteins in these Ku-overexpressing ing cells. We show that expression of the human Ku-70 and Ku-80 subunits jointly or of the Ku-70 subunit alone specifically inhibits heat-induced hsp70 expression. Conversely, expression of human Ku-80 alone does not have this effect. Thermal induction of other heat shock proteins in all of the Ku-overexpressing cell lines appears not to be significantly affected, nor is the state of phosphorylation or the DNA-binding ability of HSF1 affected. These findings support a model in which hsp70 expression is controlled by a second regulatory factor in addition to the positive activation of HSF1. The Ku protein, specifically the Ku-70 subunit, is involved in the regulation of hsp70 gene expression.
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Arvans, Donna L., Stephan R. Vavricka, Hongyu Ren, et al. "Luminal bacterial flora determines physiological expression of intestinal epithelial cytoprotective heat shock proteins 25 and 72." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 4 (2005): G696—G704. http://dx.doi.org/10.1152/ajpgi.00206.2004.
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Heat shock proteins (HSP) 25 and 72 are expressed normally by surface colonocytes but not by small intestinal enterocytes. We hypothesized that luminal commensal microflora maintain the observed colonocyte HSP expression. The ability of the small intestine to respond to bacteria and their products and modulate HSPs has not been determined. The effects of luminal bacterial flora in surgically created midjejunal self-filling (SFL) vs. self-emptying (SEL) small-bowel blind loops on epithelial HSP expression were studied. HSP25 and HSP72 expression were assessed by immunoblot and immunohistochemistry. SFL were chronically colonized, whereas SEL contained levels of bacteria normal for the proximal small intestine. SFL creation significantly increased HSP25 and HSP72 expression relative to corresponding sections from SEL. Metronidazole treatment, which primarily affects anaerobic bacteria as well as a diet lacking fermentable fiber, significantly decreased SFL HSP expression. Small bowel incubation with butyrate ex vivo induced a sustained and significant upregulation of HSP25 and altered HSP72 expression, confirming the role of short-chain fatty acids. To determine whether HSPs induction altered responses to an injury, effects of the oxidant, monochloramine, on epithelial resistance and short-circuit current ( Isc) responses to carbachol and glucose were compared. Increased SFL HSP expression was associated with protection against oxidant-induced decreases in transmural resistance and Iscresponses to glucose, but not secretory responses to carbachol. In conclusion, luminal microflora and their metabolic byproducts direct expression of HSPs in gut epithelial cells, an effect that contributes to preservation of epithelial cell viability under conditions of stress.
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Santos, Bento C., Alejandro Chevaile, Ryoji Kojima, and Steven R. Gullans. "Characterization of the Hsp110/SSE gene family response to hyperosmolality and other stresses." American Journal of Physiology-Renal Physiology 274, no. 6 (1998): F1054—F1061. http://dx.doi.org/10.1152/ajprenal.1998.274.6.f1054.
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Hsp110, Osp94, and Hsp70RY are members of the recently described Hsp110/SSE subfamily of (heat and osmotic) stress proteins whose members are structurally related to the Hsp70/BiP gene superfamily. To date, little is known about the response of this gene family to stresses in vitro or in vivo. In this study, an analysis of mRNA expression showed that Hsp110 and Osp94, like Hsp70, are induced in renal murine inner medullary collecting duct (mIMCD3) epithelial cells by heat shock, hyperosmotic NaCl, and cadmium, whereas low pH had a suppressive effect on Osp94. H2O2decreased expression of Osp94 while inducing levels of Hsp110 and Hsp70 message. Tunicamycin, hypertonic urea, and tumor necrosis factor-α had no effects. Hsp70RY was responsive exclusively to cadmium chloride. Moreover, enhanced expression of Hsp110 and Osp94 was subsequent to induction of Hsp70 and was suppressed by inhibition of protein synthesis by cycloheximide. RT-PCR analysis showed Hsp110, Osp94, and Hsp70RY are ubiquitously expressed in mouse tissues. In murine kidney, there was a corticomedullary gradient of expression of Hsp110, Osp94, Hsp70RY, and Hsp70 but not Hsc70 or BiP. Furthermore, dehydration increased inner medullary expression of Hsp110 and Osp94. An analysis of stress tolerance in mIMCD3 cells showed that heat shock and hyperosmotic NaCl stress are cross-tolerant stresses, suggesting hyperosmolality is a physiological correlate of heat shock in mammalian kidney. Thus Hsp110 and Osp94 behave as heat shock proteins, although they are regulated differently than Hsp70.
Dissertations / Theses on the topic "Heat shock proteins – Physiological effect"
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WIDELITZ, RANDALL BRUCE. "HEAT SHOCK PROTEIN SYNTHESIS AND THERMOTOLERANCE EXPRESSION IN RAT EMBRYONIC FIBROBLASTS (HYPERTHERMIA, GENE REGULATION)." Diss., The University of Arizona, 1986. http://hdl.handle.net/10150/183851.
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In response to a variety of hyperthermic treatments, rat embryonic fibroblasts synthesize heat shock proteins (hsps), including those with molecular weights of 68,000 (hsp 68), 70,000 (hsp 70) and 89,000 (hsp 89). Hyperthermic stresses, which produce the hsps, also cause expression of thermotolerance. The dependence of thermotolerance expression on hsp synthesis was investigated in this mammalian cell line under different heating conditions. Temperature shift experiments showed that hsp synthesis and thermotolerance expression were dependent not only on the absolute hyperthermic temperature, but also on the difference between the initial incubation temperature and the hyperthermic temperature. Small temperature differences which produced no cell killing did not cause detectable synthesis of hsp 68. Increasing the difference of the initial and hyperthermic temperatures reduced cell survival and increased the synthesis of hsp 68. Thermotolerance could be expressed by surviving cells following an initial heat stress even when both heat shock and general protein synthesis were inhibited. Cells exposed to cycloheximide were heated, incubated at their initial temperature for six hours and reheated in the presence of the drug. The inhibitor was then removed and the cells plated for colony formation. The hsps were expressed during this latter incubation period. The regulation of hsp 70 in rat fibroblasts was investigated next. Hsp 70 synthesis rates correlated with the amount of hsp 70 encoding mRNA. The time course of heat shock synthesis and general protein synthesis recovery were each dependent on the duration of the heat stress. Inhibiting protein synthesis with cycloheximide resulted initially in the accumulation of the RNA encoding hsp 70 but did not effect the normal turnover of this RNA species. The conclusions based on these findings are that thermal survival adaptation can be expressed in the absence of hsp 68 synthesis. Hsp 68 is expressed by cells that will ultimately die (see Chapter 2). The hsps do not appear to protect cells against subsequent heat stress. They may function in a repair capacity (see Chapter 3). Hsp 70 expression is primarily regulated by transcription in Rat-1 cells. Hsp 70 does not act to regulate its own turnover (see Chapter 4).
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Ott-Reeves, Ellen (Ellen Theresa). "In Situ Hybridization of 70 kD Heat Shock Protein mRNA in a Rat Model of Ethanol Self-Administration." Thesis, University of North Texas, 1994. https://digital.library.unt.edu/ark:/67531/metadc332564/.
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Sucrose fading was used to initiate self-administration of ethanol on an FR4 schedule in male Fischer 344 rats. Rats showed low response rates for ethanol alone. After administration of liquid diet containing ethanol, ethanol intake increased over levels prior to administration of the liquid diet. In situ hybridization compared mRNA for the inducible or constitutive 70 kD heat shock proteins in ethanol and nonethanol rats. Both inducible and constitutive mRNAs were found in nonethanol and ethanol tissues. In peripheral organs, radiolableling was higher in ethanol tissue. In brain regions, nonethanol tissues showed higher radiolabeling.
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O'Sullivan, Joseph C. "The effect of diazoxide upon heat shock protein expression and physiological response to hemorrhagic shock and cerebral stroke." Download the dissertation in PDF, 2006. http://www.lrc.usuhs.mil/dissertations/pdf/O'Sullivan2006.pdf.
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Blood, Alan Physics Faculty of Science UNSW. "Biological effects of GSM mobile phone microwave radiation: an investigation of gene expression." Awarded by:University of New South Wales. School of Physics, 2005. http://handle.unsw.edu.au/1959.4/22071.
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There is evidence that athermal radiofrequency radiation can alter Heat Shock Protein (HSP) expression or protein phosphorylation, or alter MAP kinase signalling. Effects of long-term exposure in brain tissue due to repeated HSP perturbation (eg an inhibition of apoptosis) have been hypothesised (French et al, 2001). This study aimed to investigate the RNA expression profile (12,000 genes) and HSP family protein expression levels after either acute 1-hour or chronic 4-day intermittent exposures to simulated GSM radiation in a human primary fibroblast model. The results found minimal or no effects of GSM. Flasks were exposed to 900 MHz (217 Hz modulation) at 0.18 W/kg SAR within a Transverse Electromagnetic Mode chamber (TEM cell). Cultures rested for 2 hours before exposures. Affymetrix U95A microarray analysis of a single pilot set of experiments showed that about 40 genes were reported as upregulated >=2.5 fold in each condition. There was no evidence of altered expression of any MAPK-associated genes. Target genes reported in both conditions (CBFA2T1, ZNF148, ITGA1), and genes altered in one condition (CCS, PLEC1, BIRC5), and marginally altered HSP72 were selected for PCR analysis. No other members of the HSP family were altered. In three replicate experiments assayed by real-time PCR, six genes were either unchanged or showed randomly variable expression. However HSP72 RNA showed possible consistent slight upregulation of 1.37 +/- 0.21 in the chronic condition. Western immunoblots of HSP-60, -70, -72 and -V90 proteins showed no significant changes 5 hours after exposure. In preliminary studies using a serum starvation protocol, ERK-1 phosphorylation was unaltered after 5 or 30 minutes GSM (single experiments). When flasks were transiently cooled, ERK-1 phosphorylation was increased 20 minutes later, indicating a source of artefact in some protocols. An inflammatory challenge experiment with a low-dose of the cytokine IL-1???? found that acute GSM exposure post-challenge inhibited NF????B-mediated GRO???? induction by 1.5 fold (2 experiments). Preconditioning with mild heat induces transient inhibition of both NF????B signalling and apoptosis. Other studies indicate that EMF exposures similarly evoke cytoprotection. It is suggested that GSM evoked cytoprotective signalling in this inflammatory model.
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Chao, Sheng-Hao. "Heat Shock Proteins in Ascaris suum." Thesis, University of North Texas, 1995. https://digital.library.unt.edu/ark:/67531/metadc279311/.
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Ascaris suum were exposed to a number of stressors, including heavy metals and both high (40°C) and low (18°C) temperatures. The 70kD and 90kD heat shock proteins (HSPs) in the different A. suum tissues were analyzed by Western blot and quantitated by Macintosh Image Program.
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Wagstaff, Marcus James Dermot. "The neuroprotective effect of the heat shock proteins." Thesis, University College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267150.
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Promisel, Carol Juanita. "Heat shock proteins in Mojave Desert dragonflies." CSUSB ScholarWorks, 1994. https://scholarworks.lib.csusb.edu/etd-project/910.
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Heydari, Ahmad R. Richardson Arlan. "The effect of age and caloric-restriction on the expression of heat shock proteins in rat hepatocytes." Normal, Ill. Illinois State University, 1990. http://wwwlib.umi.com/cr/ilstu/fullcit?p9115227.
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Thesis (Ph. D.)--Illinois State University, 1990.<br>Title from title page screen, viewed November 29, 2005. Dissertation Committee: Arlan Richardson (chair), Marjorie A. Jones, Lynne A. Lucher, Anthony J. Otsuka, Brian J. Wilkinson. Includes bibliographical references (leaves 168-187) and abstract. Also available in print.
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Fredriksson, Åsa. "On the role of protein oxidation and heat shock proteins in senescence and fitness /." Göteborg : Göteborg University, 2006. http://www.loc.gov/catdir/toc/fy0708/2006421399.html.
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Delaney, John Michael. "Regulation and function of the heat shock response in Escherichia coli." Diss., The University of Arizona, 1989. http://hdl.handle.net/10150/184776.
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The heat shock response is a highly conserved genetic mechanism which is induced by a wide range of environmental stimuli. Although intensively studied in both prokaryotes and eukaryotes, no regulatory mechanism has been identified by which the environmental stimuli affect expression of the heat shock genes. In addition, although many inducers of the heat shock response are known to cause DNA damage, the role of heat shock in repair of DNA damage remains unclear. Mutants of Escherichia coli defective in the recA, uvrA, and xthA genes are more sensitive to heat than wild type. However, these mutants are able to develop thermotolerance, suggesting that thermotolerance is an inducible response capable of repairing heat-induced DNA damage independent of recA, uvrA, and xthA. Thermotolerance itself is shown to depend on the dnaK gene, directly linking the E. coli heat shock response to thermotolerance. In addition, the dnaK mutant is sensitive to heat and H₂O₂, but not to UV suggesting that the DnaK protein may function to protect cells from the specific DNA damage caused by heat and H₂O₂. An E. coli grpE mutant was found to be substantially more resistant to 50°C heat treatment than wild type. However, grpE⁻ cells have the same H₂O₂ and UV sensitivity as wild type. This implies that the conditions, for which a grpE mutation is beneficial, are unique to heat exposure and are not caused by H₂O₂ or UV exposure. Furthermore, heat shock protein synthesis occurs sooner in the grpE mutant than in wild type, indicating that the grpE gene product of E. coli may act as a negative regulator of the heat shock response. An adenyl cyclase deletion mutant of E. coli (cya) failed to exhibit a heat shock response even after 30 min. at 42°C. Furthermore, a presumptive cyclic AMP receptor protein (CRP) binding site exists within the promoter region of the E. coli htpR gene. Together, these results suggest that the cya gene may regulate the heat shock response, through cyclic AMP, by directly affecting the level of expression of the heat shock sigma factor.
Books on the topic "Heat shock proteins – Physiological effect"
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1956-, Pedersen Bente Klarlund, and SpringerLink (Online service), eds. Heat Shock Proteins and Whole Body Physiology. Springer Science+Business Media B.V., 2010.
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Kabakov, Alexander E. Heat shock proteins and cytoprotection: ATP-deprived mammalian cells. Springer, 1997.
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1959-, Gabai Vladimir L., ed. Heat shock proteins and cytoprotection: ATP-deprived mammalian cells. R.G.Landes, 1996.
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Heat shock response and organ preservation: Models of stress conditioning. Springer, 1997.
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Locke, Marius, and Earl G. Noble. Exercise and stress response: The role of stress proteins. CRC Press, 2002.
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Fredriksson, Åsa. On the role of protein oxidation and heat shock proteins in senescence and fitness. Göteborg University, 2006.
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Kolesnichenko, A. V., та V. K. Voĭnikov. Stressovyĭ belok BKhSh 310: Kharakteristika i funkt︠s︡ii v rastitelʹnoĭ kletke. In-t geografii SO RAN, 2004.
Find full textBook chapters on the topic "Heat shock proteins – Physiological effect"
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Multhoff, G., E. A. Repasky, and Peter Vaupel. "Mild Hyperthermia Induced by Water-Filtered Infrared A Irradiation: A Potent Strategy to Foster Immune Recognition and Anti-Tumor Immune Responses in Superficial Cancers?" In Water-filtered Infrared A (wIRA) Irradiation. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-92880-3_10.
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AbstractApart from a number of positive “physiological” effects such as an increase in local blood flow which results in an improved oxygen supply and a reversal of tumor hypoxia, a key hallmark of cancer growth which greatly impairs anti-tumor immune responses, hyperthermia (HT) also exerts beneficial effects on anti-cancer immunity. The water-filtered infrared A (wIRA) irradiation technique achieves tissue temperatures in the fever-range (tT = 39–41 °C) or mild hyperthermia levels (tT = 39–43 °C) up to tissue depths of ≈25 mm in tissues. At tissue temperatures of 39–43 °C, by fostering the reactivity of the “immunological” TME [e.g., the activity of CD8+ cytotoxic T cells, CD4+ helper T cells, dendritic cells (DC), M1 macrophages, natural killer (NK) cells, and NK-like T (NK-T) cells], while compromising immunosuppressive cells [e.g., tumor-associated M2 macrophages (TAMs), myeloid-derived suppressor cells (MDSCs), regulatory T (Treg) cells]. Moreover, elevated temperatures resulting in mild hyperthermia induce the synthesis and release of heat-shock proteins (HSPs), and thereby augment tumor antigenicity.
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Sen, Shib Sankar, and Sib Sankr Giri. "Physiological Role of Heat Shock Proteins, Molecular Function and Stress Removal in Fishes." In Heat Shock Proteins. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-73377-7_8.
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Cohen, Irun R., Francisco J. Quintana, Gabriel Nussbaum, Michal Cohen, Alexandra ZaninZhorov, and Ofer Lider. "HSP60 and the regulation of inflammation: Physiological and pathological." In Heat Shock Proteins and Inflammation. Birkhäuser Basel, 2003. http://dx.doi.org/10.1007/978-3-0348-8028-2_1.
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Orejuela, Diana, Anne Bergeron, Geneviève Morrow, and Robert M. Tanguay. "Small Heat Shock Proteins in Physiological and Stress-Related Processes." In Cell Stress Proteins. Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-39717-7_7.
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Lehner, Thomas, Yufei Wang, and Charles Kelly. "Heat shock protein receptors, functions and their effect on monocytes and dendritic cells." In Heat Shock Proteins and Inflammation. Birkhäuser Basel, 2003. http://dx.doi.org/10.1007/978-3-0348-8028-2_13.
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Mertoğlu, Elif, Aslıhan Şengelen, Ezgi Kıyga, and Evren Önay-Uçar. "Therapeutic Drugs and Natural Products: The Effect of Suppressing Heat Shock Proteins (Hsp) in Brain Tumors." In Heat Shock Proteins in Neuroscience. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-24285-5_12.
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Panossian, Alexander, Georg Wikman, Punit Kaur, and Alexzander Asea. "Molecular Chaperones as Mediators of Stress Protective Effect of Plant Adaptogens." In Heat Shock Proteins and Whole Body Physiology. Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3381-9_20.
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Hoffmann, Frank, and Ursula Rinas. "Roles of Heat-Shock Chaperones in the Production of Recombinant Proteins in Escherichia coli." In Physiological Stress Responses in Bioprocesses. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/b93996.
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Padmini, Ekambaram. "Physiological Adaptations of Stressed Fish to Polluted Environments: Role of Heat Shock Proteins." In Reviews of Environmental Contamination and Toxicology. Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6260-7_1.
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Knack, Gaby, Beate Otto, Peter Ottersbach, Roland Alexander, Zhonglai Liu, and Klaus Kloppstech. "Structure and Possible Function of Chloroplast Heat-Shock Proteins and the Effect of Cyclic Heat-Shock on Plant Morphogenesis and Circadian Rhythmicity." In Current Research in Photosynthesis. Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0511-5_758.
Full textConference papers on the topic "Heat shock proteins – Physiological effect"
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Chung, Eunna, and Marissa Nichole Rylander. "Multi-Stress Conditioning Can Synergisticly Enhance Production of Osteogenic Markers and Heat Shock Proteins." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19511.
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Tissue regeneration can be enhanced by introduction of biochemical and mechanical cues. We investigated the effect of thermal and mechanical stress alone or in combination with growth factors (GFs) (BMP-2 and TGF-β1) on cell proliferation and induction of heat shock proteins and bone-related proteins by MC3T3-E1mouse preosteoblasts. Thermal and mechanical stress conditioning alone induced bone-related proteins such as osteocalcin (OCN), vascular endothelial growth factor (VEGF), osteoprotegerin (OPG), and osteopontin (OPN) and heat shock proteins (HSP27, HSP47, HSP70). Cell proliferation was increased by cyclic tension in combination with growth factors. Combined thermal and mechanical stress induced synergistic expression of HSPs and VEGF. Therefore, utilization of thermal and tensile stress conditioning can stimulate bone healing or regeneration.
Reports on the topic "Heat shock proteins – Physiological effect"
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O'Sullivan, Joseph C. The Effect of Diazoxide Upon Heat Shock Protein and Physiological Response to Hemorrhagic Shock and Cerebral Stroke. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ad1014226.
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Yahav, Shlomo, John McMurtry, and Isaac Plavnik. Thermotolerance Acquisition in Broiler Chickens by Temperature Conditioning Early in Life. United States Department of Agriculture, 1998. http://dx.doi.org/10.32747/1998.7580676.bard.
Full textAbstract:
The research on thermotolerance acquisition in broiler chickens by temperature conditioning early in life was focused on the following objectives: a. To determine the optimal timing and temperature for inducing the thermotolerance, conditioning processes and to define its duration during the first week of life in the broiler chick. b. To investigate the response of skeletal muscle tissue and the gastrointestinal tract to thermal conditioning. This objective was added during the research, to understand the mechanisms related to compensatory growth. c. To evaluate the effect of early thermo conditioning on thermoregulation (heat production and heat dissipation) during 3 phases: (1) conditioning, (2) compensatory growth, (3) heat challenge. d. To investigate how induction of improved thermotolerance impacts on metabolic fuel and the hormones regulating growth and metabolism. Recent decades have seen significant development in the genetic selection of the meat-type fowl (i.e., broiler chickens); leading to rapid growth and increased feed efficiency, providing the poultry industry with heavy chickens in relatively short growth periods. Such development necessitates parallel increases in the size of visceral systems such as the cardiovascular and the respiratory ones. However, inferior development of such major systems has led to a relatively low capability to balance energy expenditure under extreme conditions. Thus, acute exposure of chickens to extreme conditions (i.e., heat spells) has resulted in major economic losses. Birds are homeotherms, and as such, they are able to maintain their body temperature within a narrow range. To sustain thermal tolerance and avoid the deleterious consequences of thermal stresses, a direct response is elicited: the rapid thermal shock response - thermal conditioning. This technique of temperature conditioning takes advantage of the immaturity of the temperature regulation mechanism in young chicks during their first week of life. Development of this mechanism involves sympathetic neural activity, integration of thermal infom1ation in the hypothalamus, and buildup of the body-to-brain temperature difference, so that the potential for thermotolerance can be incorporated into the developing thermoregulation mechanisms. Thermal conditioning is a unique management tool, which most likely involves hypothalamic them1oregulatory threshold changes that enable chickens, within certain limits, to cope with acute exposure to unexpected hot spells. Short-tem1 exposure to heat stress during the first week of life (37.5+1°C; 70-80% rh; for 24 h at 3 days of age) resulted in growth retardation followed immediately by compensatory growth" which resulted in complete compensation for the loss of weight gain, so that the conditioned chickens achieved higher body weight than that of the controls at 42 days of age. The compensatory growth was partially explained by its dramatic positive effect on the proliferation of muscle satellite cells which are necessary for further muscle hypertrophy. By its significant effect of the morphology and functioning of the gastrointestinal tract during and after using thermal conditioning. The significant effect of thermal conditioning on the chicken thermoregulation was found to be associated with a reduction in heat production and evaporative heat loss, and with an increase in sensible heat loss. It was further accompanied by changes in hormones regulating growth and metabolism These physiological responses may result from possible alterations in PO/AH gene expression patterns (14-3-3e), suggesting a more efficient mechanism to cope with heat stress. Understanding the physiological mechanisms behind thermal conditioning step us forward to elucidate the molecular mechanism behind the PO/AH response, and response of other major organs. The thermal conditioning technique is used now in many countries including Israel, South Korea, Australia, France" Ecuador, China and some places in the USA. The improvement in growth perfom1ance (50-190 g/chicken) and thermotolerance as a result of postnatal thermal conditioning, may initiate a dramatic improvement in the economy of broiler's production.
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Fromm, Hillel, and Joe Poovaiah. Calcium- and Calmodulin-Mediated Regulation of Plant Responses to Stress. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568096.bard.
Full textAbstract:
We have taken a molecular approach to clone cellular targets of calcium/calmodulin (Ca2+/CaM). A 35S-labeled recombinant CaM was used as a probe to screen various cDNA expression libraries. One of the isolated clones from petunia codes for the enzyme glutamate decarboxylase (GAD) which catalyzes the conversion of glutamate to g-aminobutyric acid (GABA). The activity of plant GAD has been shown to be dramatically enhanced in response to cold and heat shock, anoxia, drought, mechanical manipulations and by exogenous application of the stress phytohormone ABA in wheat roots. We have purified the recombinant GAD by CaM-affinity chromatography and studied its regulation by Ca2+/CaM. At a physiological pH range (7.0-7.5), the purified enzyme was inactive in the absence of Ca2+ and CaM but could be stimulated to high levels of activity by the addition of exogenous CaM (K0.5 = 15 nM) in the presence of Ca2+ (K 0.5 = 0.8 mM). Neither Ca2+ nor CaM alone had any effect on GAD activity. Transgenic tobacco plants expressing a mutant petunia GAD lacking the CaM-binding domain, or transgenic plants expressing the intact GAD were prepared and studied in detail. We have shown that the CaM-binding domain is necessary for the regulation of glutamate and GABA metabolism and for normal plant development. Moreover, we found that CaM is tightly associated with a 500 kDa GAD complex. The tight association of CaM with its target may be important for the rapid modulation of GAD activity by Ca2+ signaling in response to stresses.
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Chen, Junping, Zach Adam, and Arie Admon. The Role of FtsH11 Protease in Chloroplast Biogenesis and Maintenance at Elevated Temperatures in Model and Crop Plants. United States Department of Agriculture, 2013. http://dx.doi.org/10.32747/2013.7699845.bard.
Full textAbstract:
specific objectives of this proposal were to: 1) determine the location, topology, and oligomerization of FtsH11 protease; 2) identify the substrate/s of FtsH11 and the downstream components involved in maintaining thermostability of chloroplasts; 3) identify new elements involved in FtsH11 protease regulatory network related to HT adaptation processes in chloroplast; 4) Study the role of FtsH11 homologs from crop species in HT tolerance. Background to the topic: HT-tolerant varieties that maintain high photosynthetic efficiency at HT, and cope better with daily and seasonal temperature fluctuations are in great need to alleviate the effect of global warming on food production. Photosynthesis is a very complex process requiring accurate coordination of many complex systems and constant adjustments to the changing environments. Proteolytic activities mediated by various proteases in chloroplast are essential part of this process and critical for maintaining normal chloroplast functions under HT. However, little is known about mechanisms that contribute to adaptation of photosynthetic processes to HT. Our study has shown that a chloroplast-targeted Arabidopsis FtsH11 protease plays an essential and specific role in maintaining thermostability of thylakoids and normal photosynthesis at moderate HT. We hypothesized that FtsH11 homologs recently identified in other plant species might have roles similarly to that of AtFtsH1. Thus, dissecting the underlying mechanisms of FtsH11 in the adaptation mechanisms in chloroplasts to HT stress and other elements involved will aid our effort to produce more agricultural products in less favorable environments. Major conclusions, solutions, achievements - Identified the chloroplast inner envelope membrane localization of FtsH11. - Revealed a specific association of FtsH11 with the a and b subunits of CPN60. - Identified the involvement of ARC6, a protein coordinates chloroplast division machineries in plants, in FtsH11 mediated HT adaptation process in chloroplast. -Reveal possible association of a polyribonucleotide nucleotidyltransferase (cpPNPase), coded by At3G03710, with FtsH11 mediated HT adaptation process in chloroplast. - Mapped 4 additional loci in FtsH11 mediated HT adaptation network in chloroplast. - Demonstrated importance of the proteolytic activity of FtsH11 for thermotolerance, in addition to the ATPase activity. - Demonstrated a conserved role of plant FtsH11 proteases in chloroplast biogenesis and in maintaining structural and functional thermostability of chloroplast at elevated temperatures. Implications, both scientific and agricultural:Three different components interacting with FtsH11 were identified during the course of this study. At present, it is not known whether these proteins are directly involved in FtsH11mediated thermotolerance network in chloroplast and/or how these elements are interrelated. Studies aiming to connect the dot among biological functions of these networks are underway in both labs. Nevertheless, in bacteria where it was first studied, FtsH functions in heat shock response by regulating transcription level of σ32, a heat chock factor regulates HSPsexpression. FtsH also involves in control of biosynthesis of membrane components and quality control of membrane proteins etc. In plants, both Arc 6 and CPN60 identified in this study are essential in chloroplast division and developments as mutation of either one impairs chloroplast division in Arabidopsis. The facts that we have found the specific association of both α and β CPN60 with FtsH11 protein biochemically, the suppression/ enhancement of ftsh11 thermosensitive phenotype by arc6 /pnp allele genetically, implicate inter-connection of these networks via FtsH11 mediated network(s) in regulating the dynamic adaptation processes of chloroplast to temperature increases at transcriptional, translational and post-translational levels. The conserved role of FtsH11 proteases in maintaining thermostability of chloroplast at HT demonstrated here provides a foundation for improving crop photosynthetic performance at high temperatures.
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Cohen, Roni, Kevin Crosby, Menahem Edelstein, et al. Grafting as a strategy for disease and stress management in muskmelon production. United States Department of Agriculture, 2004. http://dx.doi.org/10.32747/2004.7613874.bard.
Full textAbstract:
The overall objective of this research was to elucidate the horticultural, pathological, physiological and molecular factors impacting melon varieties (scion) grafted onto M. cannonballus resistant melon and squash rootstocks. Specific objectives were- to compare the performance of resistant melon germplasm (grafted and non-grafted) when exposed to M. cannoballus in the Lower Rio Grande valley and the Wintergarden, Texas, and in the Arava valley, Israel; to address inter-species relationships between a Monosporascus resistant melon rootstock and susceptible melon scions in terms of fruit-set, fruit quality and yield; to study the factors which determine the compatibility between the rootstock and the scion in melon; to compare the responses of graft unions of differing compatibilities under disease stress, high temperatures, deficit irrigation, and salinity stress; and to investigate the effect of rootstock on stress related gene expression in the scion. Some revisions were- to include watermelon in the Texas investigations since it is much more economically important to the state, and also to evaluate additional vine decline pathogens Didymella bryoniae and Macrophomina phaseolina. Current strategies for managing vine decline rely heavily on soil fumigation with methyl bromide, but restrictions on its use have increased the need for alternative management strategies. Grafting of commercial melon varieties onto resistant rootstocks with vigorous root systems is an alternative to methyl bromide for Monosporascus root rot/vine decline (MRR/VD) management in melon production. Extensive selection and breeding has already produced potential melon rootstock lines with vigorous root systems and disease resistance. Melons can also be grafted onto Cucurbita spp., providing nonspecific but efficient protection from a wide range of soil-borne diseases and against some abiotic stresses, but compatibility between the scion and the rootstock can be problematic. During the first year experiments to evaluate resistance to the vine decline pathogens Monosporascus cannonballus, Didymella bryoniae, and Macrophomina phaseolina in melon and squash rootstocks proved the efficacy of these grafted plants in improving yield and quality. Sugars and fruit size were better in grafted versus non-grafted plants in both Texas and Israel. Two melons (1207 and 124104) and one pumpkin, Tetsukabuto, were identified as the best candidate rootstocks in Texas field trials, while in Israel, the pumpkin rootstock RS59 performed best. Additionally, three hybrid melon rootstocks demonstrated excellent resistance to both M. cannonballus and D. bryoniae in inoculated tests, suggesting that further screening for fruit quality and yield should be conducted. Experiments with ABA in Uvalde demonstrated a significant increase in drought stress tolerance and concurrent reduction in transplant shock due to reduced transpiration for ‘Caravelle’ plants. In Israel, auxin was implicated in reducing root development and contributing to increased hydrogen peroxide, which may explain incompatibility reactions with some squash rootstocks. However, trellised plants responded favorably to auxin (NAA) application at the time of fruit development. Gene expression analyses in Israel identified several cDNAs which may code for phloem related proteins, cyclins or other factors which impact the graft compatibility. Manipulation of these genes by transformation or traditional breeding may lead to improved rootstock cultivars. Commercial applications of the new melon rootstocks as well as the ABA and TIBA growth regulators have potential to improve the success of grafted melons in both Israel and Texas. The disease resistance, fruit quality and yield data generated by the field trials will help producers in both locations to decide what rootstock/scion combinations will be best.
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Droby, Samir, Michael Wisniewski, Ron Porat, and Dumitru Macarisin. Role of Reactive Oxygen Species (ROS) in Tritrophic Interactions in Postharvest Biocontrol Systems. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7594390.bard.
Full textAbstract:
To elucidate the role of ROS in the tri-trophic interactions in postharvest biocontrol systems a detailed molecular and biochemical investigation was undertaken. The application of the yeast biocontrol agent Metschnikowia fructicola, microarray analysis was performed on grapefruit surface wounds using an Affymetrix Citrus GeneChip. the data indicated that 1007 putative unigenes showed significant expression changes following wounding and yeast application relative to wounded controls. The expression of the genes encoding Respiratory burst oxidase (Rbo), mitogen-activated protein kinase (MAPK) and mitogen-activated protein kinase kinase (MAPKK), G-proteins, chitinase (CHI), phenylalanine ammonia-lyase (PAL), chalcone synthase (CHS) and 4-coumarate-CoA ligase (4CL). In contrast, three genes, peroxidase (POD), superoxide dismutase (SOD) and catalase (CAT), were down-regulated in grapefruit peel tissue treated with yeast cells. The yeast antagonists, Metschnikowia fructicola (strain 277) and Candida oleophila (strain 182) generate relatively high levels of super oxide anion (O2−) following its interaction with wounded fruit surface. Using laser scanning confocal microscopy we observed that the application of M. fructicola and C. oleophila into citrus and apple fruit wounds correlated with an increase in H2O2 accumulation in host tissue. The present data, together with our earlier discovery of the importance of H₂O₂ production in the defense response of citrus flavedo to postharvest pathogens, indicate that the yeast-induced oxidative response in fruit exocarp may be associated with the ability of specific yeast species to serve as biocontrol agents for the management of postharvest diseases. Effect of ROS on yeast cells was also studied. Pretreatment of the yeast, Candida oleophila, with 5 mM H₂O₂ for 30 min (sublethal) increased yeast tolerance to subsequent lethal levels of oxidative stress (50 mM H₂O₂), high temperature (40 °C), and low pH (pH 4). Suppression subtractive hybridization analysis was used to identify genes expressed in yeast in response to sublethal oxidative stress. Transcript levels were confirmed using semi quantitative reverse transcription-PCR. Seven antioxidant genes were up regulated. Pretreatment of the yeast antagonist Candida oleophila with glycine betaine (GB) increases oxidative stress tolerance in the microenvironment of apple wounds. ROS production is greater when yeast antagonists used as biocontrol agents are applied in the wounds. Compared to untreated control yeast cells, GB-treated cells recovered from the oxidative stress environment of apple wounds exhibited less accumulation of ROS and lower levels of oxidative damage to cellular proteins and lipids. Additionally, GB-treated yeast exhibited greater biocontrol activity against Penicillium expansum and Botrytis cinerea, and faster growth in wounds of apple fruits compared to untreated yeast. The expression of major antioxidant genes, including peroxisomal catalase, peroxiredoxin TSA1, and glutathione peroxidase was elevated in the yeast by GB treatment. A mild heat shock (HS) pretreatment (30 min at 40 1C) improved the tolerance of M. fructicola to subsequent high temperature (45 1C, 20–30 min) and oxidative stress (0.4 mol-¹) hydrogen peroxide, 20–60 min). HS-treated yeast cells showed less accumulation of reactive oxygen species (ROS) than non-treated cells in response to both stresses. Additionally, HS-treated yeast exhibited significantly greater (P≥0.0001) biocontrol activity against Penicillium expansum and a significantly faster (Po0.0001) growth rate in wounds of apple fruits stored at 25 1C compared with the performance of untreated yeast cells. Transcription of a trehalose-6-phosphate synthase gene (TPS1) was up regulated in response to HS and trehalose content also increased.