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Published: 4 June 2021

Last updated: 26 July 2024

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1

Qazi, Khaleda Rahman. "Heat shock proteins as vaccine adjuvants." Doctoral thesis, Stockholm : Department of Immunology, Wenner-Gren Institute, Stockholm University, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-441.

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2

Ragno, Silvia. "Heat shock proteins and experimental arthritis." Thesis, Queen Mary, University of London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.281712.

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3

Suzue, Kimiko 1968. "Heat shock proteins as immunological carriers." Thesis, Massachusetts Institute of Technology, 1998. http://hdl.handle.net/1721.1/50418.

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4

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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5

Stege, Gerardus Johannes Jozef. "Hyperthermia and protein aggregation role of heat shock proteins /." [S.l. : [Groningen] : s.n.] ; [University Library Groningen] [Host], 1995. http://irs.ub.rug.nl/ppn/138287325.

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6

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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7

Morris, Amie Michelle. "Structure and function of the mammalian small heat shock protein Hsp25." Access electronically Access electronically, 2007. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20080605.104334/index.html.

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8

Matambo, Tonderayi Sylvester. "Biochemical characterization of plasmodium falciparum heat shock protein 70." Thesis, Rhodes University, 2004. http://eprints.ru.ac.za/73/1/Matambo-MSc.pdf.

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Plamodium falciparum heat shock protein (PfHsp70) is believed to be involved in the cytoprotection of the malaria parasite through its action as a molecular chaperone. Bioinformatic analysis reveal that PfHsp70 consists of the three canonical Hsp70 domains; an ATPase domain of 45 kDa, Substrate binding domain of 15 kDa and a C-terminal domain of 10 kDa. At the C-terminus there is a GGMP repeat motif that is commonly found in Hsp70s of parasitic origins. Plasmodium falciparum genome is 80% A-T rich, making it difficult to recombinantly express its proteins in Escherhia coli (E. coli) as a result of rare codon usage. In this study we carried out experiments to improve expression in E. coli by inserting the PfHsp70 coding region into the pQE30 expression vector. However multiple bands were detected by Western analysis, probably due to the presence of rare codons. The RIG plasmid, which encodes tRNAs for rare codons in particular Arg (AGA/AGG), Ile (AUA) and Gly (GGA) was engineered into the E. coli strain resulting in production of full length PfHsp70. Purification was achieved through Ni^(2+) Chelating sepharose under denaturing conditions. PfHsp70 was found to have a very low basal ATPase activity of 0.262 ± 0.05 nmoles/min/mg of protein. In the presence of reduced and carboxymethylated lactalbumin (RCMLA) a 11-fold increase in ATPase activity was noted whereas in the presence of both RCMLA and Trypanosoma cruzi DnaJ (Tcj2) a 16-fold was achieved. For ATP hydrolysis kcat value of 0.003 min^(-1) was obtained whereas for ADP release a greater k_cat_ value of 0.8 min^(-1) was obtained. These results indicated that rate of ATP hydrolysis maybe the rate-determining step in the ATPase cycle of PfHsp70.

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9

Fang, Lin. "Mechanism of client protein binding by heat shock protein 90 /." view abstract or download file of text, 2006. http://proquest.umi.com/pqdweb?did=1251819301&sid=2&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2006.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 115-121). Also available for download via the World Wide Web; free to University of Oregon users.

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10

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.
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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11

Chan, Yiu-Che. "Vascular disease, immune status and heat shock proteins." Thesis, Imperial College London, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.410031.

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12

Dempsey, Nina Claire. "Localisation of heat shock proteins in haematological malignancies." Thesis, University of Chester, 2009. http://hdl.handle.net/10034/93233.

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Although a number of HSPs have been shown to be up-regulated in a wide range of human cancers, the full significance of this remains to be determined. The localisation of HSPs seems to be critical in determining their role in cancer cell survival; High intracellular levels (iHsp) appear to be advantageous to the tumour cell, inhibiting key steps in apoptosis, while in some circumstances, surface expression (sHsp) appears to be detrimental to the cell, aiding immune recognition by various effector cells. Consequently, clarifying the importance of HSP cellular location in the cancer setting may lead to the development of novel therapies based upon manipulation of HSP localisation. This thesis had two major aims; (1) to investigate the cellular localisation of HSPs in leukocytes from patients with both myelocytic and lymphocytic malignancies in order to establish relationships between apoptosis and stage of disease (2) to study the synergistic effect of four chemotherapeutic drugs with membrane fluidising agents, compounds which have the potential to modulate HSP localisation. Hsp90 and Hsp27 expression was shown to be restricted to the inside of peripheral blood leukocytes, while Hsp72 was localised both intracellularly and on the cell surface. In CLL, iHsp90 and iHsp27 levels were found to be significantly higher than in control subjects, while surface and intracellular Hsp72 was shown to be expressed either at very high levels or at very low levels. Furthermore, iHsp90 levels were found to be associated with stage of disease, while iHsp27 levels were shown to negatively correlate with levels of apoptosis. CLL patients with stable disease were found to express higher levels of iHsp72 than patients with progressive disease. However, in AML and MDS, levels of all HSPs in peripheral blood were found to be similar to those seen in control subjects, but disease patients showed a much wider range of expression. In AML, levels of sHsp72 positively correlated in all cell types, an observation not made in MDS patients or control subjects. HSP localisation was shown to be affected by membrane fluidising agents, with a movement of Hsp72 and Hsp60 to the cell surface. This effect was not due to proteotoxicity and supports data implicating the cell membrane in the regulation of HSP responses. This manipulation of HSP localisation and the increase in membrane fluidity resulted in increased sensitivity of CLL cells to three chemotherapeutic agents and points to the possibility that manipulation of membrane fluidity, may have significant value in the development of new treatment regimes.

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13

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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14

Hochberg, Georg. "Dynamics and function of small heat-shock proteins." Thesis, University of Oxford, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.711818.

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15

Walsh, David. "Heat shock proteins in whole rat embryo cultures." Thesis, The University of Sydney, 2006. https://hdl.handle.net/2123/26024.

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The effects of heat shock on 9.5 day pre-somite embryos have been studied cultured rat embryos. The results illustrate the sensitivity at gastrulation of the developing head and brain to hyperthermia. Embryos exposed to a heat shock at 43 °C for 7.5 min exibit neurectoderm cell death and reduction of the forebrain processes. After a further 48 hr severe craniofacial defects including microphthalmia, microcephaly, and gross reduction of the forebrain region are observed. The midbrain and hindbrain regions of the neural plate appeared unaffected by heat shock. The induction of heat shock shows a relationship between time and temperature implying that a specific quantum of heat needs to be delivered to result in teratogenesis. A heat shock of 3.5‘C elevation for 15 min appears to be the minimum threshold temperature elevation for teratogenesis. Heat shock at 42‘C for 10 min is not teratogenic and results in embryos acquiring thermotolerance and protection from cell death against a further heat shock at 43‘C for 7.5 min. Thermotolerance appears to be related to a minimum recovery period of 12 min at 38.5‘C and the enhanced induction of a specific set of heat shock proteins (HSPs, 71, 73 and 88 kD). Embryos with acquired thermotolerance appear effectively to suspend proliferation in the neural plate and reschedule normal growth. The molecular mechanisms and level of cellular control for acquired thermotolerance and protection against abnormal development are unknown.

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16

Edkins, Adrienne Lesley. "Over-expression, purification and biochemical characterisation of trypanosomal heat shock protein." Thesis, Rhodes University, 2003. http://hdl.handle.net/10962/d1011736.

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The molecular chaperone process of assisted protein folding, characteristic of members of the Heat Shock Protein 70 kDa (Hsp70) and Heat Shock Protein 40kDa (Hsp40) families, is essential for cytoprotection in stressful cellular conditions. Examples of such conditions are heat shock or invasion by pathogens. The Hsp70/Hsp40 process of assisted protein folding is dependent on ATP (governed by the intrinsic ATPase activity of Hsp70) and the ability of molecular chaperones to recognise and bind non-native protein conformations. Here, we analyse and attempt to characterise the molecular chaperone activity of an inducible, cytoplasmic Hsp70 (TcHsp70) from Trypanosoma cruzi and its interactions with its potential partner Hsp40s, Tcj 1, Tcj2, Tcj3 and Tcj4. A bioinformatic analyses of the primary sequences of the trypanosomal proteins revealed that they all contained the canonical domains that define other members of the Hsp70 and Hsp40 family. Tcj2 and Tcj4 showed deviations from the consensus sequence in their substrate binding regions, which may have implications for their substrate binding specificities. TcHsp70, Tcj 1, Tcj2, Tcj3 and Tcj4 were over-expressed recombinantly as 6xHis-tag fusion proteins in Escherichia coli. His-TcHsp70, Tcjl-His and His-Tcj2 were successfully purified by Nickel-affinity chromatography for functional analyses to assess the molecular chaperone activity of His-TcHsp70 in terms of its ATPase activity and substrate binding ability. The basal ATPase activity of His-TcHsp70 was determined as 40 nmol Pi/min/mg, significantly higher than that reported for other Hsp70s. This basal ATPase activity was stimulated to a maximal level of 60 nmol Pi/min/mg in the presence of His-Tcj2 and a model non-native substrate, reduced carboxymethylated αx-lactalbumin (RCMLA). Using native polyacrylamide gel electrophoresis and Western analysis, His-TcHsp70 was shown to form discrete complexes when in the presence of Tcj 1- His, His-Tcj2 and/or RCMLA. These complexes potentially represent His-TcHsp70 - RCMLA or His-TcHsp70 - Tcj interactions, that may be indicative of chaperone activity. In vivo complementation assays showed that Tcj2, but not Tcj3, was able to overcome the temperature sensitivity of the ydjJ mutant Saccharomyces cerevisiae strain JJ160, suggesting that Tcj2 may be functionally equivalent to the yeast Hsp40 Ydj1.

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17

Shonhai, Addmore. "Molecular characterisation of the chaperone properties of Plasmodium falciparum heat shock protein 70." Thesis, Rhodes University, 2007. http://eprints.ru.ac.za/886/.

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18

Chughtai, Zahoor. "Nuclear transport of heat shock proteins in stressed cells." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=37616.

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Nuclear import of proteins that are too large to passively enter the nucleus requires soluble factors, energy, and a nuclear localization signal (NLS). Nuclear protein transport can be regulated, and different forms of stress affect nucleocytoplasmic trafficking. As such, import of proteins containing a classical NLS is inhibited in starving yeast cells. In contrast, the heat shock protein hsp70 Ssa4p concentrates in nuclei upon starvation. Nuclear concentration of Ssa4p in starving cells is reversible, and transfer of nutrient-depleted cells to fresh medium induces Ssa4p nuclear export. This export reaction represents an active process that is sensitive to oxidative stress. Upon starvation, the N-terminal domain of Ssa4p mediates Ssa4p nuclear accumulation, and a short hydrophobic sequence, termed Star (for starvation), is sufficient to localize the reporter proteins green fluorescent protein or beta-galactosidase to nuclei. To determine whether nuclear accumulation of Star-beta-galactosidase depends on a specific nuclear carrier, I have analyzed its distribution in mutant yeast strains that carry a deletion of a single beta-importin gene. With this assay I have identified Nmd5p as a beta-importin required to concentrate Star-beta-galactosidase in nuclei of stationary phase cells.

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19

Davies, Emma Louise. "Heat shock proteins : interactions with bone and immune cells." Thesis, University of Chester, 2004. http://hdl.handle.net/10034/76182.

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Heat shock proteins (Hsps) are increasingly being seen as having roles other than those of intracellular molecular chaperones, particularly with regard to their potential to act as cytokines, and to stimulate the innate immune system. Hsps have also been found to promote bone resorption and osteoclast formation in vitro, although the mechanism has not been previously identified. The overall aims of this thesis were to determine whether Hsps could stimulate bone resorption by affecting the RANKL/OPG pathway, and to address the hypothesis that Hsps can act as a danger signal to the innate immune system. In order for Hsps to affect either the RANKL/OPG system of bone resorption or act as danger signals they would need to be actively released from cells, ideally in a controlled manner following exposure to the source of stress. Hsp60 and Hsp70 were found to be released from a range of immune cells including the cell lines Jurkat and U937, and also PBMCs, T-cells and B-cells. This release was not due to cell damage. The release of Hsp60 and Hsp70 were downregulated by inhibitors of protein secretion, in particular Hsp70 release was reduced by compounds that inhibited lysosomal pathways and Hsp60 release by classical secretion inhibitors. Hsp60, Hsp70, GroEL and LPS all affected the RANKL/OPG system of bone regulation; OPG production and release was down-regulated in the MG63 and GCT osteoblast-like cell lines following treatment with Hsp60, Hsp70 and LPS, and RANKL expression was upregulated following treatment with Hsp60, Hsp70, GroEL and LPS. This effect on the RANKL/OPG system was found to translate into an effect on osteoclast formation when conditioned media from treated osteoblasts was added to osteoclast precursors in the presence of M-CSF. A range of different factors that affected Hsp release were identified; PHA activation of PBMCs was found to upregulate Hsp60 release from PBMCs. GroEL and LPS caused an upregulation in Hsp70 release from PBMCs and GCT osteoblast like cells, and Hsp70 was found to stimulate Hsp60 release from PBMCs and GCT cells. These responses of Hsp release were used to form a theory of a cascade-like danger signal that may occur when cells are exposed to bacterial infection and which would result in activation of antigen presenting cells via previously identified receptors for Hsps such as CD14/TLR4 or by unidentified pathways. The elevated release of Hsps in response to GroEL and LPS was also identified as a mechanism that could stimulate bone loss during infection or autoimmuniry by affecting the RANKL/OPG system. hi conclusion, Hsp60 and Hsp70 can be released from immune cells under normal conditions, and from both immune and osteoblast-like cells following stimulation with LPS and other Hsps. The observed release responses provide a mechanism through which Hsps can act as danger signals to the innate immune system, and also as promoters of bone resorption via the RANKL/OPG system.

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Melville, Mark Wallace. "The interferon induced serine/threonine protein kinase, PKR, is regulated by the influenza virus activated protein, P58IPK, and the molecular chaperones, Hsp40 and Hsp70 /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/11489.

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21

Barratt, Elizabeth M. "Characterisation of the heat shock response in Streptomyces lividans." Thesis, University of Manchester, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389972.

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22

Wagner, John 1966. "Modular recognition and binding properties of human heat shock transcription factor." Thesis, McGill University, 1991. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=60480.

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A partially purified preparation of in vivo activated human heat shock transcription factor (HSF) has been obtained from HeLa cells and its interaction with the heat shock response element (HSE) in the human Hsp70 gene promoter was investigated. A variety of DNA-protein binding studies including DNAse I protection, hydroxyl radical protection, and diethylpyrocarbonate interference analysis were used to investigate recognition of the HSE by human HSF. Direct contacts to bases within the 5 basepair recognition motif were detected and the overall pattern of binding was compared with the Drosophila results. Analysis of the high resolution protection patterns to extended HSE mutants indicates that HSF binding coincides with the location of the additional element motifs. Moreover, examination of the protection patterns from these constructs indicate that a proposed model for HSF binding is consistent with a model depicting HSF as a trimer.

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Rahmani, Sadoh Danesi. "Immune responses to heat shock proteins in chronic periodontitis and coronary heart disease." Thesis, King's College London (University of London), 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.413239.

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24

Liu, Jing. "Roles of heat shock protein 70 and testosterone in delayed cardioprotection of preconditioning." Click to view the E-thesis via HKUTO, 2006. http://sunzi.lib.hku.hk/hkuto/record/B37190660.

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Longshaw, Victoria Mary. "The phosphorylation and nuclear localization of the co-chaperone murine stress-inducible protein 1." Thesis, Rhodes University, 2003. http://hdl.handle.net/10962/d1004038.

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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.

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Carter, Jack D. "Heat Shock Transcription Factor 1 (HSF1) is a Novel Supporter of NSCLC Anoikis Resistance Independent of Heat Shock Proteins." Thesis, University of the Sciences in Philadelphia, 2018. http://pqdtopen.proquest.com/#viewpdf?dispub=10692983.

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Metastasis is the most lethal step in the progression of cancer, and the five-year survival rate for metastatic lung cancer patients is less than 5%. An essential step for metastasis is resistance to anoikis, a cell death program physiologically induced by detachment of cells from the extracellular matrix. Heat shock transcription factor 1 (HSF1) is the master regulator of heat shock proteins (HSP), and HSF1 and HSP promote cell survival and protein homeostasis during stress. In cancer, HSF1 dynamically controls a network of genes beyond HSP, is a mediator of malignant transformation, and promotes metastasis. HSF1 has been linked to anchorage-independent growth, but whether it exerts its effect by supporting anoikis resistance is largely unknown. Using NSCLC cells, we identified HSF1 as a novel supporter of anoikis resistance. Knockdown of HSF1 sensitizes NSCLC cells to anoikis, yet HSF1 expression or activation does not confer anoikis resistance to normal bronchial epithelial cells, suggesting parallel oncogenic pathways may be required to inhibit anoikis. Consistent with the ability of HSF1 to regulate HSP, HSF1 knockdown partially inhibited HSP72, HSP40, and HSP27. However, targeted inhibition of each HSP did not induce anoikis, suggesting the mechanism of HSF1 is unrelated to these HSP. Intriguingly, HSF1 activation markers were increased in response to cell detachment in H460 cells. Except for HSP60 in A549 cells, cell detachment did not induce HSP, further suggesting an alternative mechanism for HSF1. Interestingly, knockdown of HSP60 sensitized A549 cells to anoikis, despite HSF1 knockdown having no effect on HSP60. This work provides novel evidence that HSF1 and HSP60 can promote anchorage independence by supporting anoikis resistance, and may be valuable targets for future efforts to therapeutically suppress metastasis.

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Treweek, Teresa Mary. "Structure/function studies of the alpha-crystallin small heat-shock chaperone proteins." Department of Chemistry and Department of Biological Sciences - Faculty of Science, 2003. http://ro.uow.edu.au/theses/532.

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Alpha-crystallin is a member of the small heat shock protein (sHsp) family which exists as a multimer of alphaA- and alphaB-crystallin subunits in the ratio of 3:1 in the lens, where it was first identified. It is an intracellular molecular chaperone, capable of interacting with a multitude of target proteins to prevent their aggregation and precipitation. Initially considered to be solely a lens protein, individual alphaA- and alphaB-crystallin proteins have since been found in other organs with alphaB-crystallin in particular appearing to play a role in many neurodegenerative disorders (e.g. Alzheimers, Parkinsons and Creutzfeldt-Jakob diseases). Due to the dynamic nature of alpha-crystallin oligomers and the propensity for subunit exchange, crystallisation of the protein has been impossible. As a result, the mechanisms by which alpha-crystallin functions remain elusive, as does a complete picture of the chaperones quaternary structure. In this study, recombinant human alphaA- and alphaB-crystallin were expressed and purified using conventional methods (Horwitz, J., Huang, Q-L., Ding, L. and Bova, M. P. (1998) Methods in Enzymology 290:363-383). A series of mutants of alphaA- and alphaB-crystallin were also constructed, with mutation sites concentrated in the C-terminal region of the protein and in particular the solvent-exposed and flexible C-terminal extension. This extension, which comprises 10 and 12 amino acids in human alphaA- and alphaB-crystallin, respectively, behaves in a similar manner to an unstructured peptide in solution. Previous NMR spectroscopic studies have indicated that it serves a crucial role in binding target proteins. C-Terminal extension mutants K175L, K174A/K175A, E164A/E165A, I159A/I161A and R163STOP (alphaB-crystallin) and S172L, T168L and R163STOP mutants (alphaA-crystallin) were produced and purified in the same manner as for the wildtype proteins. The expected masses of mutants were confirmed by electrospray mass spectrometry (ESI-MS). Complete purification, however, of S172L and R163STOP alphaA-crystallin was not achieved due to decreased aggregate size and excessive hydrophobicity, respectively. Purified wildtype and mutant proteins were structurally and functionally characterised using a variety of spectroscopic techniques. These included chaperone assays under both reduction and heat stress with insulin and beta(subscript L)-crystallin as target proteins, respectively, intrinsic tryptophan fluorescence spectroscopy, far- and near-UV circular dichroism (CD) spectroscopy, thermostability studies, size-exclusion high-performance liquid chromatography (HPLC), mass spectrometry and nuclear magnetic resonance (NMR) spectroscopy. Many of the alphaB-crystallin mutants purified successfully and provided insight into specific amino acid residues that are important for the chaperone action of the protein. These include the I-X-I motif at the C-terminal end of the protein which is highly conserved throughout sHsps and is thought to be critical for oligomeric assembly. Mutation of both isoleucine residues in the alphaB-crystallin I-X-I motif to alanine resulted in a protein which formed larger oligomeric complexes than the wildtype protein. Truncation of the C-terminal extension of alphaB-crystallin resulted in a protein with severely impaired chaperone ability, increased tendency to aggregate and disrupted secondary, tertiary and quaternary structures. These results suggest that the polar and flexible C-terminal extension is also necessary for uniform oligomeric assembly as well as for the solubility of ?-crystallin as a whole. Chaperone and thermostability studies on the double glutamic acid mutant (E164A/E165A) showed that these highly charged residues are critical to the solubility of alphaB-crystallin at higher temperature. Consistent with this, ion-pairs and the formation of salt bridges between charged amino acids on the surfaces of thermophilic proteins are thought to be responsible for their increased thermostability. Recombinant human alphaA- and alphaB-crystallin were uniformly (superscript 15)N-labelled for the purposes of 2D Nuclear Magnetic Resonance spectroscopy (NMR) studies. Measurement of (superscript 15)N relaxation time constants (T[subscript 1] and T[subscript 2]) and (superscript 15)N Nuclear Overhauser Effects (NOEs) for both wildtype proteins and the K175L and I159/I161A mutants of alphaB-crystallin have provided detailed information on the relative flexibilities of residues in the proteins C-terminal extension. Substitution of a leucine residue for the C-terminal lysine (K175) increased extreme C-terminal mobility and substitution of the isoleucine pair of the I-X-I motif with alanine residues led to a disruption of flexibility throughout the C-terminal extension. (superscript 15)N T(subscript 1) and T(subscript 2) and (superscript 15)N NOE values were also determined for (superscript 15)N-labelled alphaA-crystallin in the presence of reduced alpha-lactalbumin in order to gain information on changes in the flexibility of the C-terminal extension upon chaperone interaction with a stressed target protein. Upon formation of a chaperone-target protein complex, the flexibilities of C-terminal residues of alphaA-crystallin were equalised across the extension indicating that the entire extension was involved in interaction with the target protein to some extent. The R120G alphaB-crystallin mutant, which is associated with desmin-related myopathy and cataract in humans was also expressed and purified for the purposes of further structural characterisation. Previous studies on this mutant have provided some ambiguous results with regard to its chaperone ability and general structural stability. It was found that in addition to being intrinsically unstable and susceptible to unfolding, R120G alphaB-crystallin underwent C-terminal proteolysis with time. Furthermore, R120G alphaB-crystallin exhibited marked substrate specificity and in fact, acted as an anti-chaperone in the presence of reduced ?-lactalbumin. Under these conditions, R120G alphaB-crystallin promoted the aggregation of the molten globule state of alpha-lactalbumin and co-precipitated with it out of solution. This study, therefore provided several insights into structural and functional aspects of alpha-crystallin small heat shock chaperone proteins. [Note: this abstract contained scientific formulae that would not come across on this form. Please see the 01Front files abstract for the full details.]

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Studer, Sonja. "Chaperone activity and oligomerization of bacterial small heat shock proteins /." [S.l.] : [s.n.], 2002. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=14550.

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Vendrell, i. Flotats Meritxell. "Heat shock proteins: a strategy to improve bovine oocyte vitrification." Doctoral thesis, Universitat Autònoma de Barcelona, 2019. http://hdl.handle.net/10803/667864.

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La crioconservació de gàmetes s'ha convertit en una necessitat per a una producció eficient d'animals domèstics, permetent la modificació dels programes de cria d'animals i oferint un mitjà per a mantenir la diversitat genètica mitjançant l'emmagatzematge d'important germoplasma que podria revitalitzar les poblacions futures. Aconseguir un mètode robust de crioconservació garantiria la preservació del material genètic femení d'espècies en perill d'extinció i de gran importància econòmica. La vitificació és la tècnica més prometedora per a la crioconservació d'oòcits. Des dels primers intents de vitrificació d'oòcits bovins, el protocol de vitrificació i els dispositius de suport utilitzats han canviat considerablement. No obstant això, a causa de les peculiaritats de l'oòcit boví, la taxa de fecundació i la capacitat de desenvolupament dels oòcits crioconservats bovins encara han de millorar-se. Durant el procés de vitrificació, les cèl·lules sofreixen crio-dany i formació de gel, la qual cosa condueix a canvis ultraestructurals que provoquen fallades en la maduració i el desenvolupament. Per a aquest propòsit, en aquesta tesi hem investigat diferents estratègies per a millorar la capacitat de desenvolupament dels oòcits bovins després dels processos de vitrificació i escalfament. Les proteïnes de xoc tèrmic (HSPs) són proteïnes d'estrès cel·lular altament conservades que s'han identificat com un mecanisme de defensa cel·lular. La majoria d'elles s'expressen de forma constitutiva a nivells baixos, però algunes es poden regular positivament en resposta a factors estressants cel·lulars per a controlar el plegament de proteïnes i protegir contra l'agregació i desnaturalització de proteïnes. Entre les proteïnes induïbles, en aquesta tesi van ser analitzades la HSP70 (HSPA1A) i la HSP90 (HSP90AA1). En el capítol II, podem observar com un tractament de xoc tèrmic definit (1h, 41.5 °C) va augmentar la intensitat de la fluorescència per a la HSP70 quan es va aplicar a les 8h d'IVM. Quan aquest estrès per calor es va aplicar abans de la vitificació dels oòcits, no es van mitigar els efectes nocius de la crioconservació, com prèviament hi havia hipotetitzat. El líquid fol·licular és naturalment ric en factors de creixement i citocines. Se sap que la família de citocines interleuquina (IL) -6 té un paper predominant en la funció de reproducció. En el capítol III, avaluem com la IL-6, la IL-11 i el factor inhibidor de la leucèmia (LIF) induïen canvis en l'expressió de miR-21 i uns altres miRNAs claus en cèl·lules de cúmuls i oòcits bovins. No trobem dades prometedores per a IL-6 i IL-11, però LIF va augmentar l'expressió de miR-21tant en cèl·lules de cúmul com en oòcits. S'ha descrit el paper del LIF en l'activació de vies de senyalització clau per a la supervivència i el manteniment de les cèl·lules. En el capítol IV, avaluem com la suplementació amb LIF afectava el desenvolupament d'embrions i modulava l'expressió gènica en oòcits i embrions. LIF va augmentar l'expressió d'HSPA1A i HSP90AA1 en el moment de l'activació del genoma embrionari. En el moment en què es van desenvolupar els embrions, en l'etapa expandida i eclosionada, la HSPA1A es va reduir i també ho va fer el DNMT3A. LIF no va influir en la divisió i la taxa de blastocists. El major impacte exercit per LIF va ser durant la transició matern-embrionària. Imitant les condicions fisiològiques i guiats pels resultats obtinguts anteriorment, en el capítol V suplementaren els oòcits amb LIF durant la maduració per a millorar la vitrificació. La vitrificació va modificar clarament els nivells de ARNm i el LIF sembla precondicionar als oòcits perquè no sofreixin tant estrès, encara que no es van observar diferències en cap grup de tractament en termes de taxa de blastocists.
Gamete cryopreservation, as many other reproductive technologies, has become a necessity for an efficient production of domestic animals, allowing the modification of animal breeding programs and offering a mean to maintain genetic diversity by banking important germplasm that could reinvigorate future populations. Achieving a robust cryopreservation method would guarantee the preservation of feminine genetic material of endangered species and of those of a great economic importance. Vitification is the most promising technique for oocyte cryopreservation. From the first attempts of vitrifiying bovine oocytes the vitrification protocol and the support devices used have changed considerably. However, due to the peculiarities of the bovine oocyte, fertilization rate and developmental competence of bovine cryopreserved oocytes still need to be improved. During the vitrification process cells suffer cryodamage and ice formation, what leads to ultrastructural changes driving to maturation or development impairment. For this purpose, in this thesis we have investigated different strategies to ameliorate the developmental competence of bovine oocytes after vitrification and warming processes. Heat shock proteins (HSPs) are highly conserved cellular stress proteins that have been identified as a cell defense mechanism. Most of them are constitutively expressed at low levels but some can be upregulated in response to cellular stressors so to regulate protein folding, protect against protein aggregation and denaturation. Among the inducible ones, HSP70 (HSPA1A) and HSP90 (HSP90AA1) were those analyzed in this thesis. In chapter II, we can observe how a defined heat shock treatment (1h, 41.5ºC) increases fluorescence intensity for HSP70 when applied at 8h of IVM. When this heat stress was applied before oocyte vitification, it did not mitigate the harmful effects of cryopreservation how me hypothesized. Follicular fluid is naturally rich in growth factors and cytokines. Interleukin (IL)-6 family of cytokines is known to have a predominant role in reproduction function. In chapter III, we assessed how IL-6, IL-11 and leukemia inhibitory factor (LIF) induced changes in the expression of miR-21 and other key miRNAs in bovine cumulus cells and oocyte. We did not find promising data for IL-6 and IL-11, but LIF did enhance the expression of miR-21 in both cumulus cells and oocytes. LIF has been described to activate key signaling pathways for cell survival and maintenance. In chapter IV, we evaluated how LIF supplementation affected embryo development and modulated gene expression in oocytes and embryos. LIF increased expression of HSPA1A and HSP90AA1 at the time of embryonic genome activation. By the time embryos developed, at the expanded and hatched stage, HSPA1A was reduced and so did DNMT3A. LIF did not influence on cleavage and blastocyst rate. The greater impact exerted by LIF was during the maternal-to-embryonic transition. Mimicking physiological conditions, and guided for the results obtained previously, on chapter V we supplemented oocytes with LIF during maturation in order to improve vitrification. Vitrification modifies clearly mRNA levels and LIF seemed to precondition oocytes not to suffer so much stress, although no differences were observed in any treatment group in terms of blastocyst rate.

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30

Lubaretz, Olga. "Non-stress induced small heat shock proteins in higher plants." [S.l. : s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=962714305.

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31

Landsbury, Andrew. "The interactions of small heat shock proteins with intermediate filaments." Thesis, Durham University, 2012. http://etheses.dur.ac.uk/3606/.

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The interaction of small heat shock proteins (sHsps) and intermediate filaments (IFs) is essential to the cell. Mutations both in sHsps and IFs cause disease in humans, characterised by aggregates containing both sHsps and IFs, demonstrating the importance of this interaction. However, the molecular details of this interaction and the mechanisms which lead to disease are unknown. Investigations into the sHsp-IF interaction may allow future development of new therapeutic approaches to maintain the sHsp-IF interaction and therefore inhibit the formation of the pathological aggregates which cause disease. This thesis analyses the sHsp-IF interaction in vitro using the sHsp ‘aB crystallin’ and the IF ‘desmin’. I investigate the domains in both aB crystallin and desmin which are important for their interaction. I also analyse the effect of IF assembly conditions on filament properties and interaction with aB crystallin. In addition, I investigate the ‘beaded filament’ to gain insight into the factors affecting filament assembly, filament properties and filament interactions with aB crystallin. Furthermore, I investigate the effects of a disease causing aB crystallin mutation on activity in vitro. I also attempt to model the potential structural changes in aB crystallin resulting from mutation, using the sHsp, Hsp16.5. These studies provide important insight into the interaction between sHsps and IFs.

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32

Guedes, de Bacelar Maria Manuela Ferreira Vaz. "Heat shock proteins as danger signals to the immune system." Thesis, University of Liverpool, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.436253.

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33

Ishida, Kenji. "Identifying a role for heat shock proteins in Schistosoma mansoni." Case Western Reserve University School of Graduate Studies / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=case1496938244172559.

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34

Watson, Andrea. "Heat shock proteins in leukaemia cell differentiation and cell death." Thesis, Aston University, 1990. http://publications.aston.ac.uk/12533/.

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When HL60 cells were induced to differentiate to granulocyte-like cells with the agents N-methylformamide and tunicamycin an concentrations marginally below those which were cytotoxic, there was a decrease in the synthesis of the glucose- regulated proteins which preceded the expression of markers of a differentiated phenotype. There was a transient increase in the amount of hsp70 after 36 hours in NMF treated cells but in differentiated cells negligible amounts were detected. Inducers which were known to modulate hsp70 such as azetadine carboxylic acid did not induce differentiation suggesting early changes in the endoplasmic reticulum may be involved in the commitment to terminal differentiation of HL60 cells. These changes in group synthesis were not observed when K562 human chronic myelogenous leukemia cells were induced to differentiate to erythroid-like cells but there was a comparable increase in amounts of hsp70. When cells were treated with concentrations of drugs which brought about a loss in cell viability there was an early increase in the amount of hsp70 protein in the absence of any increase in synthesis. HL60 cells were treated with NMF (225mM), Adriamycin (1 jiM), or CB3717 (5iM) and there was an increase in the amounts of hsp70, in the absence of any new synthesis, which preceded any loss of membrane integrity and any significant changes in cell cycle but was concomitant with a later loss in viability of > 50% and a loss in proliferative potential. The amounts of hsp70 in the cell after treatment with any of the drugs was comprable to that obtained after a heat shock. Following a heat shock hsp70 was translocated from the cytoplasm to the nucleus, but treatment with toxic concentrations of drug caused hsp70 to remain localised in the cytoplasm. Changes in hsp70 turn-over was observed after a heat shock compared to NMF-treated cells. Morphological studies suggested that cells that had been treated with NMF and CB3717 were undergoing necrosis whereas the Adriamycin cells showed characteristics that were indicative of apoptosis. The data supports the hypothesis that an increase in amounts of hsp70 is an early marker of cell death.

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35

Martin, Jody L. "Small heat shock proteins and protection against cardiac ischemic damage /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1997. http://wwwlib.umi.com/cr/ucsd/fullcit?p9806511.

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36

Würstlin, Oliver Djun [Verfasser], and Christian [Akademischer Betreuer] Flotho. "Expression von Heat Shock Proteins bei der juvenilen myelomonozytären Leukämie." Freiburg : Universität, 2011. http://d-nb.info/1123463026/34.

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37

Crowgey, Erin Lynn. "Effects of protein malnourishment and corticosterone on thymocyte apoptosis." Connect to this document online, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1134141732.

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Thesis (M.S.)--Miami University, Dept. of Microbiology, 2005.
Title from first page of PDF document. Document formatted into pages; contains [1], iv, 44 p. : ill. Includes bibliographical references (p. 40-44).

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Liu, Jing, and 劉靜. "Roles of heat shock protein 70 and testosterone in delayed cardioprotection of preconditioning." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2006. http://hub.hku.hk/bib/B37190660.

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39

Lai, Chien-houng. "Heat shock protein expression in limpets on Hong Kong rocky shores." Click to view the E-thesis via HKUTO, 2005. http://sunzi.lib.hku.hk/hkuto/record/B36846144.

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40

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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41

Muchowski, Paul J. "Structural and functional characterization of human alphaB-crystallin, a small heat-shock protein and molecular chaperone /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/5676.

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42

Poon, Wai-hei. "The induction of cellular stress responses by specific Kappa-opioid receptor agonist." Click to view the E-thesis via HKUTO, 2004. http://sunzi.lib.hku.hk/hkuto/record/B31473921.

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43

Gould, Phillip Spencer. "Regulation and role of the three chaperonin operons of Rhizobium leguminosarum." Thesis, University of Birmingham, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.273921.

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44

Leoni, Francesca. "Hsp72 translocation and secretion in in vivo and in vitro models." Thesis, University of Chester, 2009. http://hdl.handle.net/10034/93835.

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Evidence suggesting that Hsp72 is actively participating in cellular signalling as well interacting with immune system dynamics has been increasing. This is true in healthy, stressed and diseased cells but to different degrees. Modulation of the plasma membrane association and secretion in the extracellular environment by different types of stressors is the key event that leads to different degrees of immune system activation. Hence a better understanding of the mechanisms of Hsp72 secretion and association with plasma membrane is crucial. This thesis investigated the tissue source and mechanism of Hsp72 surface presentation to plasma membrane structures and release in relation with different cellular and physiological stressors. In vivo models confirmed that different tissue types determine specific Hsp72 responses following the same stress and increase serum Hsp72 dependant on intensity and duration of the stress. Diseases models confirm that Hsp72 responses in specific cell populations is related to disease progression, while in vitro models clearly showed that there are multiple mechanisms of secretion and surface presentation, dependent on the nature of the stressor as well as the intensity and duration. This observations clearly change the view of extracellular Hsp72 as a danger signal and lead to a revision of the original danger model. It also suggests that manipulation of Hsp72 translocation through the different pathways involved may prove effective therapeutically.

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O'Farrell, Francis J. "An investigation of the response of lymphoid cells to oxidative stress." Thesis, University of Ulster, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.241678.

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Daturpalli, Soumya Srinivas. "Mechanistic studies of Hsp90 in neurodegenerative diseases and cancer." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648691.

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Wang, Ruihua. "Blockade of heat shock protein 90 (HSP90) for the treatment of hepatocellular carcinoma (HCC)." Click to view the E-thesis via HKUTO, 2008. http://sunzi.lib.hku.hk/hkuto/record/B41005776.

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48

Sienkiewicz, Natasha. "The heat-shock response in Serpula species at the cellular and molecular level." Thesis, Abertay University, 1999. https://rke.abertay.ac.uk/en/studentTheses/59c9a9f3-c2ec-4fcb-81f7-54a472faf8d5.

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The study focuses on the effects of heat stress on Serpula lacrymans and S. himantioides (which have been previously shown to be relatively thermosensitive and thermotolerant respectively) in relation to the heat shock response. A part of this response is the production of heat-shock proteins (hsps). Comparative studies of chick embryo fibroblasts and Saccharomyces cerevisiae (wine strain, L-2226) were used to demonstrate possible differences between these three very distinct eukaryotic systems. The aims of the project were to determine whether S. lacrymans and S. himantioides undergo the heatshock response with respect primarily to induced thermotolerance and the production of hsps. The approach taken to establish the above was by systematic analysis of the different pathways involved in this response. Firstly, overall heat induced changes in protein and mRNA synthesis were analysed, in conjunction with the identification of specific proteins related to the heat-shock response, namely hsp60, hsp70 which have been shown in other eukaryotic systems to play key roles in this response. Secondly, immunological studies were also used to detect changes in the pattern of protein ubiquitination, which resulted from heat stress. Thirdly, changes in hsp70 mRNA were monitored by RT-PCR. The cDNA and genomic amplimer products generated by RT-PCR and PCR respectively were cloned and sequenced to identify a putative of hsp70 gene sequence. Fourthly, the AMP-activated protein kinase (AMPK) cascade has been demonstrated to be activated in response to stress and steps were made to detect and identify AMPK activity in cellular extracts of both Serpula species. Finally, the effect of heat upon trehalose accumulation and mobilisation during the heat-shock response was studied as there is growing evidence to link increased thermotolerance to transient increase in trehalose levels, which is now considered to be a stress metabolite.

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Yunkun, Wu. "X-ray crystal structures of yeast heat shock proteins and mitochondrial outer membrane translocon member Tom70p." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2009r/wu.pdf.

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Miroshnichenko, Sergey. "Immunomodulation of cytosolic small heat shock proteins in transgenic tobacco plants." [S.l. : s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=967123127.

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