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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
21

The application of a transgenic strain of the nematode Caenorhabditis elegans to the biomonitoring of metal polluted soil

Power, Rowena Suzanne January 2000 (has links)
No description available.
22

Hsp72 modulation of inflammatory immune responses

Ireland, H. Elyse January 2009 (has links)
The body initiates an immune response to danger signals. The Danger model of the immune system postulates that danger signals are produced by exogenous molecules from foreign invaders, such as bacteria, and endogenous molecules released from damaged or injured cells. The response involves antigen recognition leading to up-regulation of cytokines and cell surface markers, followed by the recruitment of antigen presenting cells and T-helper cells which determine how the immune system responds. Endogenous danger signals include Hsp72 and HMGB-1. This thesis describes the development of specific antibodies and ELISAs for use in the quantification and detection of intra-cellular Hsp72 from cell extracts, and released Hsp72 from cell cultures which enabled the confirmation of physiological levels of Hsp72 from model systems. The ability of endogenous Hsp72 to stimulate an immune response was demonstrated and this response was not solely due to LPS contamination of recombinant protein preparations. Hsp72 was able to augment the response to LPS. In the presence of another endogenous danger signal, HMGB-1, relative amounts of Hsp72 were shown to augment a pro-inflammatory response whilst being able to maintain an anti-inflammatory response demonstrating Hsp72 has the ability to modulate the immune response. Hsp72 was also shown to be able to stimulate an immune response by binding to cell surface receptors, which could be blocked by specific peptides corresponding to known receptors. These include some receptors not utilised by LPS. The proportion of these different danger signals has consequences for the progression and outcome of an immune response and this may well be modulated by imposition of a supplemental or future stress at different points. In the most severe case, this can lead to death through sepsis following trauma.
23

Interactions between extracellular Hsp72 and blood cells

Williams, Helen January 2010 (has links)
In recent years, compelling evidence has accumulated suggesting heat shock proteins (HSPs) which are generally believed to be localised and functioning mainly within eukaryotic cells as cyto-protective molecular chaperones, are also localised in the extracellular milieu. Depending on their localisation, on the cell surface (membrance-bound or embedded), or in the peripheral circulation, extracellular HSPs may induce apoptotic cell death, or in contrast protect cells from cell damage and/or cell death when exposed to cellular stress, or may even elicit a stimulatory effect on the innate immune response including cell activiation and cytokine secretion. Hence, the localisation of intracellular and extracellular HSPs appears to be critical in determining their roles in terms of stimulating cell death, cyto-protection, or immune activiation under normal physiological conditions and following exposure to stress stimuli. This thesis describes the intracellular expression, up-regulation, and cell surface localisation of endogenous HSPs: HSP27, Hsp60, Hsp72 and Hsp90 by flow cytometry, florescence microscopy and Western blotting, under control conditions and in response to environmental stress using in vitro and ex vivo models with the intention of determining their physiological roles. The ability of extracellularly administered HSPs (Hsp70 and Hsp72) to protect cultured U937 cells in vitro or peripheral primary human leukogytes or erythrocytes ex vivo from various stress stimuli was demonstrated and was found to be dependent on surface binding and/or internalisation via scavenger receptors (SRs) or phosphatidylserine (PS), which could be blocked by receptor specific ligands. Extracellular HSPs were also shown to be able to stimulate an immune response through the induction of U937 monocyte differentiation into macrophages as evidenced through the up-regulation of the surface receptors: CD36, SR-A1 and CD91 analysed by flow cytometry. These proteins were able to stimulate TNF-x and IL-10 production and secretion by U937 macrophages, shown by ELISA, and chemotatic properties were demonstrated using Boyden chambers. The cyto-protective and immune regulatory effects of extracellular HSPs have potential therapeutic value as treatments in a wide variety of clinical situations.
24

Kinetics study of heat shock protein 70 expression

Wang, Sihong 25 July 2011 (has links)
Not available / text
25

Novel anti-oxidant properties of cobalamin

Altaie, Ala January 2009 (has links)
Oxidative stress has been associated with a wide range of diseases, including cardiovascular diseases, Alzheimer's disease, atherosclerosis, Parkinson's disease and cancer. It also plays a role in the ageing process. Hyperhomocysteimia is commonly found to be associated with these diseases. The hyperhomocysteimia is a result of a deficiency in both folate and cobalamin Folate is known to reduce Hey and protect cells from apoptosis, but there are no studies investigating the impact of cobalamin on apoptosis induced by oxidative stress or the mechanism(s) of the protection. The aims of the research are to investigate the protective role of cobalamin and the possible mechanism(s) for this protection. It also examines the protective role of novel cobalamin and investigates their superior protection. The methods used in this research for apoptosis detection we used caspase-3 and the annexin-V, while for necrosis we used PI staining, where cell viability were detected using MTS assay. We also measured the generation of superoxide by Lucigenin-enhanced chemiluminescence and reactive oxygene species by using the redox active prob DCFH-DA. Moreover, the intracellular proteins were measured via staining with specific fluorescent-conjugated antibodies were detected using flowcytometry. Our result demonstrated that 25|iM of cobalamin protects cells from apoptosis. The protection by cobalamin was associated with induction of iHsp72 and iHO-1, and these are shown to be essential for the protection. Furthermore, our research demonstrated a novel mechanism of cobalamin-apoptosis protection involving induction of NfkB, ERK1/2 and AKT signal transduction pathways. In order to protect cells from apoptosis induced by oxidative stress, cobalamin induces the pNfkB which in turn regulate the iNOS and HO-1 induction. Cobalamin also induces thepERK1/2 which regulates the induction of Hps72 and Nrf2. And finally, pAKT induced by cobalamin which regulate the Nrf2 and HO-1 induction. The inhibition of any of theses pathways leads to loss the protection. The GSCbl and NACCbl provide a superior protection against oxidative stress, this protection involved induction of the signal transduction pathways and Hsps. To conclude; cobalamin provides protection against cells death induced by oxidative stress. Cobalamin achieves this by multiple pathways which include direct antioxidant stimulation and induction of signal transduction pathways. Different cobalamin derivatives have superior protections. These finding are a useful pharmaceutical tool in the treatment of the oxidative stress related diseases.
26

Isolation and characterization of calmodulin-binding heat shock proteins and cDNAs encoding calmodulin-binding proteins in cultured tobacco cells

Lu, Yingtang January 1991 (has links)
Typescript. / Thesis (Ph. D.)--University of Hawaii at Manoa, 1991. / Includes bibliographical references (leaves 103-130) / Microfiche. / x, 130 leaves, bound ill. 29 cm
27

Design of hyperthermia protocols for inducing cardiac protection and tumor destruction by controlling heat shock protein expression

Rylander, Marissa Nichole, Diller, K. R. January 2005 (has links) (PDF)
Thesis (Ph. D.)--University of Texas at Austin, 2005. / Supervisor: Kenneth R. Diller. Vita. Includes bibliographical references.
28

Increasing ethanol tolerance through the heterologous expression of the geobacillus thermoglucosiadius heat-shock proteins (GroEL/GroES) in an escherichia coli host

Charewa, Wellington January 2012 (has links)
>Magister Scientiae - MSc / Due to economic and environmental concerns associated with use of fossil fuels, humanity is seeking alternative fuels. Ethanol is one of the alternative fuels produced commercially. Current ethanol production technologies using first generation ethanol processes is criticised for depleting the food supply and escalating food prices. Biomass is a target feedstock for use in bioethanol production and would resolve the criticism associated with the current bioethanol industry. Bacterial strains such as Geobacillus thermoglucosidasius NCIMB 11955 can be used to produce ethanol from biomass because they assimilate hexose and pentose sugars, a property that is lacking in first generation ethanol producing microbes (Saccharomyces cerevisiae and Zymomonas mobilis) (Riyanti and Rogers, 2009). Due to the low ethanol tolerance (4 % v/v (maximum)) of G. thermoglucosidasius, use of this species for bioethanol production is not economically viable. GroES and GroEL genes are involved in stress tolerance in bacteria: activation of these genes has been observed in stress induced bacteria (Rasouly and Ron, 2009). In this study the ethanol tolerance of G. thermoglucosidasius NCIMB 11955 was characterised by culturing at 45 ºC and 55 ºC in the presence of ethanol. A greater ethanol tolerance was observed at the sub-optimal growth temperature of 45 ºC. Escherichia coli metabolic systems are well understood. Aiming to improve the ethanol tolerance G. thermoglucosidasius NCIMB 11955, the GroES and GroEL genes of the organism were cloned in an expression vector and expressed in E.coli before testing their ability to confer an increased tolerance to ethanol. Proteomic analysis of the recombinant E. coli strain showed that GroES was over-expressed while GroEL was not. After over expression of GroES, the optical density of cultures was periodically measured. Over-expression of the G. thermoglucosidasius NCIMB 11955 GroES gene improved the ethanol tolerance of E. coli Rosetta pLySs growing in 4% (v/v) ethanol.
29

The phosphorylation and nuclear localization of the co-chaperone murine stress-inducible protein 1

Longshaw, Victoria Mary January 2003 (has links)
The co-chaperone murine stress-inducible protein 1 (mSTI1), a heat shock protein 70 (Hsp70)/ heat shock protein 90 (Hsp90) organizing protein (Hop) homologue, mediates the assembly of the Hsp70/Hsp90 chaperone heterocomplex. mSTI1 is phosphorylated in vitro by cell cycle kinases, proximal to a putative nuclear localization signal (NLS), substantiating a predicted CKII-cdc2-NLS (CcN) motif at position 189-239. Stable transfectants of NIH 3T3 fibroblasts that expressed mSTI1-EGFP, NLSmSTI1-EGFP and EGFP, were prepared. Fluorescence microscopy revealed mSTI1 was cytoplasmically localized, and that this localization was not affected by the fusion of mSTI1 with the EGFP moiety. NLSmSTI1-EGFP was targeted to the nucleus compared to EGFP, suggesting that the NLSmSTI1 was a functional NLS. The localization of mSTI1 was determined under normal and heat shock conditions, inhibition of nuclear export (leptomycin B), inhibition of CKII 5,6-dichlorobenzimidazole riboside, DRB), inhibition of cdc2 kinase (olomoucine), and G1/S phase arrest (hydroxyurea). mSTI1-EGFP and mSTI1 were excluded from the nucleus in the majority of resting cells, but accumulated in the nucleus following leptomycin B treatment, implying that mSTI1 possibly undergoes a functional import process, and export via the chromosomal region maintenance 1 (CRM-1)-mediated export pathway. Hydroxyurea and olomoucine (but not DRB or heat shock) treatment increased the proportion of cells in which mSTI1-EGFP exhibited cytoplasmic and nuclear localization. 2D gel electrophoresis detected three endogenous mSTI1 isoforms, which changed following hydroxyurea treatment. Furthermore, point inactivation and mimicking of phosphorylatable residues in mSTI1 altered the translocation of the protein and the isoform composition. Modification of mSTI1 at S189 and T198 decreased the number of isoforms of mSTI1-EGFP, suggesting that the protein is modified at these sites in vivo. The removal of the in vitro cdc2 kinase site at T198 promoted a nuclear localization during G1/S phase arrest. Therefore active cdc2 kinase, but not CKII, may be required for cytoplasmic localization of mSTI1. The CKII site appears to have no regulatory role under heat shock conditions or during the cell cycle. In vitro phosphorylation studies on untagged mSTI1 further supported the prediction that S189 is the only site recognised by CKII. The cdc2 kinase site at T198, however, although the major site, was not the only site phosphorylated in vitro. However, mSTI1 and cdc2 kinase did not interact in a detectable stable complex. Bioinformatic analysis of mSTI1 revealed NLS residues were conserved in STI1 proteins, and the NLS and TPR2A motifs were in close proximity. This may have mechanistic implications for the formation of the Hsp90-mSTI1 heterocomplex. The cytoplasmic or nuclear localization of mSTI1 is predicted to be the result of a dynamic equilibrium between nuclear import and nuclear export, the fulcrum of which may be shifted under different cell cycle conditions. These data provide the first evidence of regulated nuclear import/export of a major Hsp70/Hsp90 co-chaperone, and the regulation of this nuclear import by cell cycle status and cell cycle kinases.
30

Investigating the role of heat shock proteins (Hsps) 40, 70 and 90 in the life cycle of Theiler's murine encephalomyelitis virus (TMEV) / Investigating the role of heat shock proteins 40, 70 and 90 in the life cycle of a picornavirus, Theiler's murine encephalomyelitis virus

Mutsvunguma, Lorraine Zvichapera January 2011 (has links)
Introduction: Picornaviruses are a family of RNA viruses which are economically and clinically significant. Like many other viruses, picornaviruses utilise host cell machinery to facilitate their replication and assembly, including heat shock proteins (Hsps). The aim of this research was to investigate the role of Hsp40, Hsp70 and Hsp90 during picornavirus infection using the cardiovirus, Theiler’s murine encephalomyelitis virus (TMEV), as a study model. Methodology: Picornavirus VP1 capsid proteins were analysed by multiple sequence alignment and multiple structural comparisons. Protein domain architecture was used to analyse Hsp90 cellular and viral client proteins. Effects of Hsp90 inhibitors, novobiocin and geldanamycin, on TMEV growth in BHK-21 cells was observed over a 48hr period. Localisation of Hsp40, Hsp90 and Hsp70 in TMEV-infected BHK-21 cells was investigated by indirect immunofluorescence and confocal microscopy. Results and Discussion: VP1 proteins of picornaviruses are highly divergent within the family at the amino acid level, which might be linked to the protein’s function in determining virus tropism and antibody neutralisation. An eight-stranded anti-parallel beta-barrel structure was found conserved in the VP1 protein structures which might be linked to the highly conserved picornavirus capsid assembly process. Absence of a common protein domain between Hsp90 viral and cellular client proteins that might be functionally connected to Hsp90, suggests that Hsp90 most likely recognises surface features rather than sequence motifs/patterns. The Hsp90 inhibitors, novobiocin and geldanamycin, had a negative effect on virus growth as virus-induced cytopathic effect was not observed in treated cell after 48hrs. TMEV 2C protein was detected by Western analysis in infected cell lysates treated with geldanamycin but not novobiocin, suggesting novobiocin affects the translation or processing of TMEV 2C. Immunofluorescence analysis of TMEV-infected cells showed a relocalisation of Hsp40 into the nucleus during infection. Overlap of Hsp40 and TMEV P1 was observed in the perinuclear region, suggesting colocalisation between these proteins. Hsp70 converged around the replication complex during infection but did not overlap with TMEV 2C. Hsp90 concentrated in the region of the replication complex where it overlapped with TMEV 2C and this redistribution was found to be dependent on the stage of infection. The overlap between Hsp90 and TMEV 2C signals observed, suggested colocalisation between the two proteins. Conclusion: This study identified Hsp90, Hsp70 and Hsp40 as possible host factors required in TMEV replication.

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