Relevant bibliographies by topics / Heat shock proteins

Academic literature on the topic 'Heat shock proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2024

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Heat shock proteins.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Heat shock proteins"

1

&NA;. "Heat Shock Proteins." Clinical Pulmonary Medicine 1, no. 6 (November 1994): 386. http://dx.doi.org/10.1097/00045413-199411000-00009.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Villar, Jesus, Sergio Ribeiro, and Arthur S. Slutsky. "HEAT SHOCK PROTEINS." Shock 4, Supplement (December 1995): 9. http://dx.doi.org/10.1097/00024382-199512001-00036.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Kaufmann, Stefan H. E. "Heat-shock proteins." Current Opinion in Rheumatology 2, no. 3 (June 1990): 430–35. http://dx.doi.org/10.1097/00002281-199002030-00003.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Schlesinger, M. J. "Heat shock proteins." Journal of Biological Chemistry 265, no. 21 (July 1990): 12111–14. http://dx.doi.org/10.1016/s0021-9258(19)38314-0.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Latchman, DavidS. "Heat-shock proteins." Lancet 337, no. 8738 (February 1991): 424. http://dx.doi.org/10.1016/0140-6736(91)91196-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Burdon, R. H. "Heat shock and the heat shock proteins." Biochemical Journal 240, no. 2 (December 1, 1986): 313–24. http://dx.doi.org/10.1042/bj2400313.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Ünver, Ramazan, Figen Deveci, Gamze Kırkıl, Selda Telo, Dilara Kaman, and Mutlu Kuluöztürk. "Serum Heat Shock Protein Levels and the Relationship of Heat Shock Proteins with Various Parameters in Chronic Obstructive Pulmonary Disease Patients." Turkish Thoracic Journal 17, no. 4 (October 10, 2016): 153–59. http://dx.doi.org/10.5578/ttj.30518.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

AL-Taee, Anwaar F., and Jamella H. Rasheed. "Expression of Heat Shock Protein HSP90 in Genomic-DNA of Chickpea (Cicer arietinum L.) Callus by Heat Shock Treatment." Academic Journal of Research and Scientific Publishing 3, no. 33 (January 5, 2022): 121–39. http://dx.doi.org/10.52132/ajrsp.e.2022.33.6.

Full text
Abstract:
This study was able to detect of the expression activity of heat shock proteins HSP90 and heat transcription factors HSFs for the first time in callus cultures of chickpea, Cicer arietinum L., that exposed to abiotic shocks, grown on MS medium supplemented with 1.0 mg L-1 naphthalene acetic acid (NAA) and 2.0 mg L-1 benzyl adenine (BA). Heat shock proteins HSPs were constructed for increase of withstand long-term physical shocks, and production of resistant to heat chickpeas plants, this shock was enhancement of tolerance of chickpea callus to abiotic stresses (high - temperatures). Results enhanced the ability of chickpea callus to abiotic stresses bearing and induce of HSF genes to heat shock proteins HSP90 production quickly to removing denatured proteins, avoid apoptosis, thus, supporting tolerance to the sudden action of these shocks. Expression activity of heat shock genes and transcription factors by determined based on polymerase chain reaction qPCR, that explained the gene activity increasing at shocks intensity increased
APA, Harvard, Vancouver, ISO, and other styles
9

Kuibida, V. V., P. P. Kokhanets, and V. V. Lopatynska. "Heat shock proteins in adaptation to physical activity." Ukrainian Biochemical Journal 94, no. 2 (July 11, 2022): 5–14. http://dx.doi.org/10.15407/ubj94.02.005.

Full text
Abstract:
The review article presents the author’s model of one of the blocks of the integrated adaptation mechanism to physical activity and the accompanying moderate heat effects. The participation of heat shock proteins in the stabilization of the tertiary structure and in the restoration of the function of proteins damaged by temperature and physical stressors but performing catalytic, transport, reception or protective role and being involved in the processes of contraction- relaxation and muscle and bone tissue remodeling is discussed.
APA, Harvard, Vancouver, ISO, and other styles
10

McCallum, Kirk L., John J. Heikkila, and William E. Inniss. "Temperature-dependent pattern of heat shock protein synthesis in psychrophilic and psychrotrophic microorganisms." Canadian Journal of Microbiology 32, no. 6 (June 1, 1986): 516–21. http://dx.doi.org/10.1139/m86-094.

Full text
Abstract:
The patterns of proteins synthesized by the arctic psychrophilic bacterium Res-10 and the psychrotroph Bacillus psychrophilus during various heat shocks up to 32 °C were examined. Both microorganisms were found to display temperature-dependent patterns of heat shock protein synthesis. Elevation of the incubation temperature of the arctic psychrophile from 0 to 15, 20, 25, or 32 °C induced the synthesis of at least 19 heat shock proteins. Imposing similar heat shock upon cells of the psychrotroph resulted in the induction of at least 25 heat shock proteins. Examination of the effect of the transcriptional inhibitor rifampicin on the synthesis of heat shock proteins revealed that the primary control of heat shock protein synthesis lies at the transcriptional level in both microorganisms.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Heat shock proteins"

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

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

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Chao, Sheng-Hao. "Heat Shock Proteins in Ascaris suum." Thesis, University of North Texas, 1995. https://digital.library.unt.edu/ark:/67531/metadc279311/.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Promisel, Carol Juanita. "Heat shock proteins in Mojave Desert dragonflies." CSUSB ScholarWorks, 1994. https://scholarworks.lib.csusb.edu/etd-project/910.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Heat shock proteins"

1

E, Kaufmann S. H., ed. Heat shock proteins. New York: Springer International, 1991.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Emma, Morel, and Vincent Camille 1960-, eds. Heat shock proteins: New research. New York: Nova Science Publishers, 2008.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Gaitanaris, George Anastasios. The role of heat shock proteins in protein folding. [New York]: [Columbia University], 1993.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Calderwood, Stuart K. Heat Shock Proteins in Cancer. Dordrecht: Springer, 2007.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Shonhai, Addmore, Didier Picard, and Gregory L. Blatch, eds. Heat Shock Proteins of Malaria. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-78397-6.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Asea, Alexzander A. A., and Punit Kaur, eds. Heat Shock Proteins and Stress. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-90725-3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Shonhai, Addmore, and Gregory L. Blatch, eds. Heat Shock Proteins of Malaria. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-007-7438-4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

van Eden, Willem, ed. Heat Shock Proteins and Inflammation. Basel: Birkhäuser Basel, 2003. http://dx.doi.org/10.1007/978-3-0348-8028-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Calderwood, Stuart K., Michael Y. Sherman, and Daniel R. Ciocca, eds. Heat Shock Proteins in Cancer. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6401-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Asea, Alexzander A. A., Punit Kaur, and Stuart K. Calderwood, eds. Heat Shock Proteins and Plants. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-46340-7.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Heat shock proteins"

1

Pfanner, N. "Role of Heat Shock Proteins in Mitochondrial Protein Import." In Heat Shock, 175–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76679-4_19.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Harr, Jeffrey N., Philip F. Stahel, Phillip D. Levy, Antoine Vieillard-Baron, Yang Xue, Muhammad N. Iqbal, Jeffrey Chan, et al. "Heat Shock Proteins." In Encyclopedia of Intensive Care Medicine, 1029–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-00418-6_749.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Blatch, Gregory L. "Heat Shock Proteins." In Encyclopedia of Malaria, 1–9. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-8757-9_24-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

van Eden, Willem, Femke Broere, and Ruurd van der Zee. "Heat Shock Proteins." In Inflammation - From Molecular and Cellular Mechanisms to the Clinic, 813–30. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2017. http://dx.doi.org/10.1002/9783527692156.ch31.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Richter-Landsberg, Christiane. "Heat Shock Proteins." In Heat Shock Proteins in Neural Cells, 1–12. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-39954-6_1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

van Eden, Willem, and Ruurd van der Zee. "Heat Shock Proteins." In Compendium of Inflammatory Diseases, 569–75. Basel: Springer Basel, 2016. http://dx.doi.org/10.1007/978-3-7643-8550-7_94.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Giovanella, Beppino C. "Heat Shock Proteins." In Advances in Experimental Medicine and Biology, 95–98. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5766-7_8.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Sainburg, Robert L., Andrew L. Clark, George E. Billman, Zachary J. Schlader, Toby Mündel, Kevin Milne, Earl G. Noble, et al. "Heat Shock Proteins." In Encyclopedia of Exercise Medicine in Health and Disease, 394–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_96.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Gooch, Jan W. "Heat-Shock Proteins." In Encyclopedic Dictionary of Polymers, 897. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13884.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

van Eden, Willem, and Ruurd van der Zee. "Heat Shock Proteins." In Encyclopedia of Inflammatory Diseases, 1–8. Basel: Springer Basel, 2014. http://dx.doi.org/10.1007/978-3-0348-0620-6_94-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Heat shock proteins"

1

Song, Alfred S., and Kenneth R. Diller. "Modeling Heat Shock Protein Expression While Wearing a Therapeutic Heat Wrap." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192823.

Full text
Abstract:
Hyperthermia mediated repair of injured tissues is attributed to increased blood perfusion and mass transport. A complimentary mechanism of healing may exist where heat shock proteins (HSPs) are over expressed due to local hyperthermia. HSPs are able to stabilize the tertiary structure of nascent proteins and to help re-fold denatured proteins. In this report, we created a temperature model that characterizes the temperature distribution in the dermis, subcutaneous fat, and muscle tissues due to the application a heat source as a commercially marketed heat wrap. The temperature evolution due to the heat wrap was calculated by applying the finite difference version of Pennes’ bioheat equation to the back of a subject consisting of a composite, semi-infinite system geometry. The temperature model included the factors of metabolic heat generation and blood perfusion. The HSP expression was modeled via interpolation of experimental constitutive data. The results show that the over expression of HSPs in the target tissue area likely contribute to the efficacy of the heat wrap.
APA, Harvard, Vancouver, ISO, and other styles
2

Tutar, Yusuf, and Aykut Özgür. "Heat Shock Proteins in Targeted  Cancer Chemotherapy." In 2nd International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2016. http://dx.doi.org/10.3390/ecmc-2-a030.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

"Comparative genomics of heat shock proteins system in extremophile nonbiting midges." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-137.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
5

Sajjadi, Amir Y., Kunal Mitra, and Michael S. Grace. "Visualization of Heat Shock Proteins for Quantifying Laser-Induced Thermal Ablation of Biological Tissues." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53483.

Full text
Abstract:
In laser-based therapeutics, it is important to ablate target tissue with minimal damage to surrounding healthy tissue. Unique properties of lasers allow precise and controlled ablation of tissue. Tightly focusing a short-pulse laser at the desired tissue region and controlling the exposure time by scanning the beam at the target can minimize corresponding collateral damage [1]. Even so, design of effective laser-based ablation procedures requires an understanding of the extent of laser-induced damage for given laser parameters (power, intensity, duration, etc.). Therefore, the instantaneous and effects over time of laser irradiation in live tissue should be studied. Instantaneous effects can be quantified by measuring thermal effects of laser irradiation on tissue. Depending on the application, threshold temperature is necessary to make permanent or temporary changes in tissue structure [1]. The temperature profile around the laser-irradiated region gives insight into radial energy spread and the extent of damage in tissue surrounding the ablation zone. In order to investigate the effects over time of laser irradiation of tissue, we studied the temporal expression patterns heat shock proteins (HSP), members of a class of proteins whose expression patterns change when cells are exposed to elevated temperature or other stressors [2]. We conducted experiments on live anesthetized mice to determine the spatiotemporal expression patterns of heat shock proteins in skin tissue after laser stimulation, both to understand the roles of heat shock proteins in laser-induced tissue damage and repair, and to develop heat shock proteins as tools to illustrate the extent of laser-induced damage and wound healing following irradiation.
APA, Harvard, Vancouver, ISO, and other styles
6

Adelaiye, Remi M., Leigh Ellis, and Roberto Pili. "Abstract 2766: Targeting heat shock proteins: Novel strategies for treating prostate cancer." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2766.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

De Silvestre Perrucio, Ligia, and Jaime Amaya-Farfan. "EFEITO DO CONSUMO DE AMINOÁCIDOS NAS HEAT SHOCK PROTEINS (HSPS) EM RATOS." In XXIV Congresso de Iniciação Científica da UNICAMP - 2016. Campinas - SP, Brazil: Galoa, 2016. http://dx.doi.org/10.19146/pibic-2016-51284.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Chung, Eunna, and Marissa Nichole Rylander. "Effects of Growth Factors and Stress Conditioning on the Induction of Heat Shock Proteins and Osteogenesis." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206662.

Full text
Abstract:
Tissue engineering is an emerging field that focuses on development of methods for repairing and regenerating damaged or diseased tissue. Successful development of engineered tissues is often limited by insufficient cellular proliferation and insufficient formation of extracellular matrix. To induce effective bone regeneration, many research groups have investigated the cellular response and capability for tissue regeneration associated with bioreactor conditions and addition of growth factors [1]. Bioreactors in tissue engineering have been developed to expose cells to a similar stress environment as found within the body or induce elevated stress levels for potential induction of specific cellular responses associated with tissue regeneration. Native bone encounters a diverse array of dynamic stresses such as shear, tensile, and compression daily. Stress conditioning protocols in the form of thermal or tensile stress have been shown to induce up-regulation of molecular chaperones called heat shock proteins (HSPs) and bone-related proteins like MMP13 (matrix metallopeptidase 13) [2] and OPG (osteoprotegerin) [3, 4]. HSPs have important roles in enhancing cell proliferation and collagen synthesis. Osteogenic growth factors such as TGF-β1 (transforming growth factor beta 1) and BMP-2 (bone morphogenetic protein 2) are related to bone remodeling and osteogenesis as well as HSP induction [5]. Therefore, identification of effective preconditioning using growth factors and stress protocols that enhance HSP expression could substantially advance development of bone regeneration. The purpose of this research was to identify preconditioning protocols using osteogenic growth factors and tensile stress applied through a bioreactor system to enhance expression of HSPs and bone-related proteins while minimizing cellular injury for ultimate use for bone regeneration.
APA, Harvard, Vancouver, ISO, and other styles
9

Petrović, Miloš, Radojica Đoković, Vladimir Kurćubić, Snežana Bogosavljević-Bošković, Simeon Rakonjac, and Milun Petrović. "Intracellular and extracellular Hsp70 in cows: Similarities and differences in physiological and pathophysiology conditions." In Zbornik radova 26. medunarodni kongres Mediteranske federacije za zdravlje i produkciju preživara - FeMeSPRum. Poljoprivredni fakultet Novi Sad, 2024. http://dx.doi.org/10.5937/femesprumns24025p.

Full text
Abstract:
Heat shock proteins (Hsp), also called chaperones, are proteins that are indispensable for the proper formation of the polypeptide chain; and have a role in its translocation within the cell. Hsp70 in cells helps to re-establish the native conformation of proteins that have denatured under the influence of various stressogens, by preventing their aggregation, which results in protecting the cell from apoptosis and having an anti-inflammatory effect. These proteins are classified on the basis of molecular mass, and the most significant is heat shock protein 70 (Hsp70) with a molecular mass of about 70 kDa, which is designated as "a master player in protein homeostasis". The concentration of Hsp increases significantly when exposed to a stressor originating from the cell itself or from the external environment. Many chaperones are induced under the influence of high ambient temperatures, when the universal heat shock response (HSR) develops, which is why the name heat shock proteins was defined. Intracellular Hsp70 (iHsp70) shows its protective and anti-inflammatory effects. Induced iHsp70 protects the cell from apoptosis by reducing or blocking the activation of caspases, binding to apoptosis-inducing factor (AIF) and inhibiting AIF-induced chromatin condensation or preventing mitochondrial damage and nuclear fragmentation. It blocks cell morphological changes caused by tumor necrosis factor-induced apoptosis, and has been found to aid in cell repair of damage caused by inflammation. The anti-inflammatory effect of iHsp70 is reflected in the fact that it inhibits the response to lipopolysaccharides and blocks the production of inflammatory mediators such as tumor necrosis factor Alpha (TNF-a), and other mechanisms have been described. he expression of the gene for the production of Hsp70 has been well studied in ruminants or their cell cultures exposed to high ambient temperatures, and the multiple increase of iHsp70 in the cells results in a better adaptation to heat stress. The study of eHsp70 has become relevant due to the availability of diagnostic kits for determining its concentration, and the latest results show that it is a very useful predictor of mortality in patients with septic shock. Hsp70 moves to the extracellular space in several ways: after leaving necrotic cells, under the action of various stress factors and inflammation in undamaged cells, it can be produced in the liver as an acute phase protein, and transport by exosomes and direct contact with the lipid membrane of cells have also been described. The pro-inflammatory effect of eHsp70 is realized by inducing immune cells, which further induces the secretion of inflammatory cytokines (TNF-a, IL-1b, IL-6), inducible nitric oxide synthase (iNOS) expression and nuclear translocation of nuclear factor-cB (NF-cB). According to the chaperone balance theory, the higher the value of eHsp70 compared to iHsp70, the more pronounced its proinflammatory effects. This hypothesis was also confirmed in dairy cows in the periparturient period.
APA, Harvard, Vancouver, ISO, and other styles
10

Alimova, Alexandra, Alvin Katz, Misu Paul, Elizabeth Rudolph, Paul Gottlieb, J. C. Steiner, and Robert R. Alfano. "Fluorescence detection of proteins released by Bacillus subtilis spores during heat shock germination." In Biomedical Optics 2005, edited by Tuan Vo-Dinh, Warren S. Grundfest, David A. Benaron, and Gerald E. Cohn. SPIE, 2005. http://dx.doi.org/10.1117/12.588592.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Heat shock proteins"

1

Blum, Abraham, Henry T. Nguyen, and N. Y. Klueva. The Genetics of Heat Shock Proteins in Wheat in Relation to Heat Tolerance and Yield. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568105.bard.

Full text
Abstract:
Fifty six diverse spring wheat cultivars were evaluated for genetic variation and heritability for thermotolerance in terms of cell-membrane stability (CMS) and triphenyl tetrazolium chloride (TTC) reduction. The most divergent cultivars for thermotolerance (Danbata-tolerant and Nacozari-susceptible) were crossed to develop an F8 random onbred line (RIL) population. This population was evaluated for co-segragation in CMS, yield under heat stress and HSP accumulation. Further studies of thermotolerance in relations to HSP and the expression of heterosis for growth under heat stress were performed with F1 hybrids of wheat and their parental cultivars. CMS in 95 RILs ranged from 76.5% to 22.4% with 71.5% and 31.3% in Danbata and Nacozari, respectively. The population segregated with a normal distribution across the full range of the parental values. Yield and biomass under non-stress conditions during the normal winter season at Bet Dagan dit not differ between the two parental cultivar, but the range of segregation for these traits in 138 RILs was very high and distinctly transgressive with a CV of 35.3% and 42.4% among lines for biomass and yield, respectively. Mean biomass and yield of the population was reduced about twofold when grown under the hot summer conditions (irrigated) at Bet Dagan. Segregation for biomass and yield was decreased relative to the normal winter conditions with CV of 20.2% and 23.3% among lines for biomass and yield, respectively. However, contrary to non-stress conditions, the parental cultivars differed about twofold in biomass and yield under heat stress and the population segregated with normal distribution across the full range of this difference. CMS was highly and positively correlated across 79 RILs with biomass (r=0.62**) and yield (r=0.58**) under heat stress. No such correlation was obtained under the normal winter conditions. All RILs expressed a set of HSPs under heat shock (37oC for 2 h). No variation was detected among RILs in high molecular weight HSP isoforms and they were similar to the patterns of the parental cultivars. There was a surprisingly low variability in low molecular weight HSP isoforms. Only one low molecular weight and Nacozari-specific HSP isoform (belonging to HSP 16.9 family) appeared to segregate among all RILs, but it was not quantitatively correlated with any parameter of plant production under heat stress or with CMS in this population. It is concluded that this Danbata/Nacozari F8 RIL population co-segregated well for thermotolerance and yield under heat stress and that CMS could predict the relative productivity of lines under chronic heat stress. Regretfully this population did not express meaningful variability for HSP accumulation under heat shock and therefore no role could be seen for HSP in the heat tolerance of this population. In the study of seven F1 hybrids and their parent cultivars it was found that heterosis (superiority of the F1 over the best parent) for CMs was generally lower than that for growth under heat stress. Hybrids varied in the rate of heterosis for growth at normal (15o/25o) and at high (25o/35o) temperatures. In certain hybrids heterosis for growth significantly increased at high temperature as compared with normal temperature, suggesting temperature-dependent heterosis. Generally, under normal temperature, only limited qualitative variation was detected in the patterns of protein synthesis in four wheat hybrids and their parents. However, a singular protein (C47/5.88) was specifically expressed only in the most heterotic hybrid at normal temperature but not in its parent cultivars. Parental cultivars were significantly different in the sets of synthesized HSP at 37o. No qualitative changes in the patterns of protein expression under heat stress were correlated with heterosis. However, a quantitative increase in certain low molecular weight HSP (mainly H14/5.5 and H14.5.6, belonging to the HSP16.9 family) was positively associated with greater heterosis for growth at high temperature. None of these proteins were correlated with CMS across hybrids. These results support the concept of temperature-dependent heterosis for growth and a possible role for HSP 16.9 family in this respect. Finally, when all experiments are viewed together, it is encouraging to find that genetic variation in wheat yield under chronic heat stress is associated with and well predicted by CMS as an assay of thermotolerance. On the other hand the results for HSP are elusive. While very low genetic variation was expressed for HSP in the RIL population, a unique low molecular weight HSP (of the HSP 16.9 family) could be associated with temperature dependant heterosis for growth.
APA, Harvard, Vancouver, ISO, and other styles
2

Nechushtai, Rachel, and Parag Chitnis. Role of the HSP70 Homologue from Chloroplasts in the Assembly of the Photosynthetic Apparatus. United States Department of Agriculture, July 1993. http://dx.doi.org/10.32747/1993.7568743.bard.

Full text
Abstract:
The major goal of the proposed research was to study the role of a 70-kDa heat shock cognate protein from chloroplasts (ct-HSP70) in the assembly of chlorophyll-protein complexes. The latters are mostly important in allowing photosynthesis to occur. Photosynthesis is at the heart of crop productivity and the knowledge of the biogenesis of the photosynthetic apparatus is essential to manipulate the efficiency of photosynthesis. The characterization of the function of the ct-HSP70 was planned to be studied in vitro by assaying its capability to physically interact with the thylakoid proteins and to assist their assembly into thylakoid membranes. We planned to identify regions in the light-harvesting complex protein (LHCP) that interact with the ct-HSP70 and characterize the interaction between them. We also intended to isolate cDNA clones encoding ct-HSP70, sequence them, express one of them in E. coli and use the purified protein for functional assays. The research in this BARD proposal aimed at providing insights and aid in understanding the mechanism by which plants may respond to the heat stress. Since plants often experience increased temperatures.
APA, Harvard, Vancouver, ISO, and other styles
3

Lurie, Susan, David R. Dilley, Joshua D. Klein, and Ian D. Wilson. Prestorage Heat Treatment to Inhibit Chilling Injury and Delay Ripening in Tomato Fruits. United States Department of Agriculture, June 1993. http://dx.doi.org/10.32747/1993.7568108.bard.

Full text
Abstract:
The research had two specific goals; (1) to develop and optimize a postharvest heat treatment and characterize the response of tomato to the heat and subsequent cold storage, and (2) to investigate the involvement of heat shock proteins (HSP) in resistance to chilling injury. For the first goal we have investigated many time-temperature treatments using dry heat and found that 48 h at 38oC is optimum for Israeli cultivars, while 48 h at 42oC worked better for American cultivars in preventing chilling injury. We have also compared hot water to hot air and found hot water to be effective, but less so than hot air. Membrane lipid composition in relation to chilling injury was investigated after hot water and hot air treatments. Investigation of fruit ripening found that mRNAs of ripening-related genes were inhibited by high temperature, but recovered during the subsequent storage period and allowed normal ripening to proceed. Sensory studies showed no difference in the taste of heated or nonheated fruit. Following the production of HSP in heated and stored fruit allowed us to determine that during low temperature storage the HSP remained present in the fruit tissue, and their presence was correlated with resistance to chilling injury. HSP clones have been isolated by both differential screening of a cDNA library of heated and chilled tomatoes (Israel) and by mRNA differential display (United States). These clones are being characterized.
APA, Harvard, Vancouver, ISO, and other styles
4

Locy, Robert D., Hillel Fromm, Joe H. Cherry, and Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress: Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, January 2001. http://dx.doi.org/10.32747/2001.7575288.bard.

Full text
Abstract:
Most plants accumulate the nonprotein amino acid, g-aminobutyric acid (GABA), in response to heat stress. GABA is made from glutamate in a reaction catalyzed by glutamate decarboxylase (GAD), an enzyme that has been shown by the Israeli PI to be a calmodulin (CaM) binding protein whose activity is regulated in vitro by calcium and CaM. In Arabidopsis there are at least 5 GAD genes, two isoforms of GAD, GAD1 and GAD2, are known to be expressed, both of which appear to be calmodulin-binding proteins. The role of GABA accumulation in stress tolerance remains unclear, and thus the objectives of the proposed work are intended to clarify the possible roles of GABA in stress tolerance by studying the factors which regulate the activity of GAD in vivo. Our intent was to demonstrate the factors that mediate the expression of GAD activity by analyzing the promoters of the GAD1 and GAD2 genes, to determine the role of stress induced calcium signaling in the regulation of GAD activity, to investigate the role of phosphorylation of the CaM-binding domain in the regulation of GAD activity, and to investigate whether ABA signaling could be involved in GAD regulation via the following set of original Project Objectives: 1. Construction of chimeric GAD1 and GAD2 promoter/reporter gene fusions and their utilization for determining cell-specific expression of GAD genes in Arabidopsis. 2. Utilizing transgenic plants harboring chimeric GAD1 promoter-luciferase constructs for isolating mutants in genes controlling GAD1 gene activation in response to heat shock. 3. Assess the role of Ca2+/CaM in the regulation of GAD activity in vivo in Arabidopsis. 4. Study the possible phosphorylation of GAD as a means of regulation of GAD activity. 5. Utilize ABA mutants of Arabidopsis to assess the involvement of this phytohormone in GAD activation by stress stimuli. The major conclusions of Objective 1 was that GAD1 was strongly expressed in the elongating region of the root, while GAD2 was mainly expressed along the phloem in both roots and shoots. In addition, GAD activity was found not to be transcriptionally regulated in response to heat stress. Subsequently, The Israeli side obtained a GAD1 knockout mutation, and in light of the objective 1 results it was determined that characterization of this knockout mutation would contribute more to the project than the proposed Objective 2. The major conclusion of Objective 3 is that heat-stress-induced changes in GAD activity can be explained by heat-stress-induced changes in cytosolic calcium levels. No evidence that GAD activity was transcriptionally or translationally regulated or that protein phosphorylation was involved in GAD regulation (objective 4) was obtained. Previously published data by others showing that in wheat roots ABA regulated GABA accumulation proved not to be the case in Arabidopsis (Objective 5). Consequently, we put the remaining effort in the project into the selection of mutants related to temperature adaptation and GABA utilization and attempting to characterize events resulting from GABA accumulation. A set of 3 heat sensitive mutants that appear to have GABA related mutations have been isolated and partially characterized, and a study linking GABA accumulation to growth stimulation and altered nitrate assimilation were conducted. By providing a better understanding of how GAD activity was and was not regulated in vivo, we have ruled out the use of certain genes for genetically engineering thermotolerance, and suggested other areas of endeavor related to the thrust of the project that may be more likely approaches to genetically engineering thermotolerance.
APA, Harvard, Vancouver, ISO, and other styles
5

CONNECTICUT UNIV HEALTH CENTER FARMINGTON. Heat Shock Protein-Peptide Complexes as Anti-Viral Agents. Fort Belvoir, VA: Defense Technical Information Center, May 1997. http://dx.doi.org/10.21236/ada325919.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Madaeva, I. M., N. A. Kurashova, N. V. Semenova, E. B. Uhinov, S. I. Kolesnikov, and L. I. Kolesnikova. HSP70 HEAT SHOCK PROTEIN IN OXIDATIVE STRESS APNEA PATIENTS. Publishing house of the Russian Academy of Medical Sciences, 2020. http://dx.doi.org/10.18411/1695-1978-2020-62730.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Firon, Nurit, Prem Chourey, Etan Pressman, Allen Hartwell, and Kenneth J. Boote. Molecular Identification and Characterization of Heat-Stress-Responsive Microgametogenesis Genes in Tomato and Sorghum - A Feasibility Study. United States Department of Agriculture, October 2007. http://dx.doi.org/10.32747/2007.7591741.bard.

Full text
Abstract:
Exposure to higher than optimal temperatures - heat-stress (HS) - is becoming increasingly common to all crop plants worldwide. Heat stress coinciding with microgametogenesis, especially during the post-meiotic phase that is marked by starch biosynthesis, is often associated with starch-deficient pollen and male sterility and ultimately, greatly reduced crop yields. The molecular basis for the high sensitivity of developing pollen grains, on one hand, and factors involved in pollen heat-tolerance, on the other, is poorly understood. The long-term goal of this project is to provide a better understanding of the genes that control pollen quality under heat-stress conditions. The specific objectives of this project were: (1) Determination of the threshold heat stress temperature(s) that affects tomato and sorghum pollen quality whether: a) Chronic mild heat stress conditions (CMHS), or b) Acute heat stress (AHS). (2) Isolation of heat-responsive, microgametogenesis-specific sequences. During our one-year feasibility project, we have accomplished the proposed objectives as follows: Objectrive 1: We have determined the threshold HS conditions in tomato and sorghum. This was essential for achieving the 2nd objective, since our accumulated experience (both Israeli and US labs) indicate that when temperature is raised too high above "threshold HS levels" it may cause massive death of the developing pollen grains. Above-threshold conditions have additional major disadvantages including the "noise" caused by induced expression of genes involved in cell death and masking of the differences between heatsensitive and heat-tolerant pollen grains. Two different types of HS conditions were determined: a) Season-long CMHS conditions: 32/26°C day/night temperatures confirmed in tomato and 36/26°C day maximum/night minimum temperatures in sorghum. b) Short-term AHS: In tomato, 2 hour exposure to 42-45°C (at 7 to 3 days before anthesis) followed by transfer to 28/22±2oC day/night temperatures until flower opening and pollen maturation, caused 50% reduced germinating pollen in the heat-sensitive 3017 cv.. In sorghum, 36/26°C day/night temperatures 10 to 5 days prior to panicle emergence, occurring at 35 days after sowing (DAS) in cv. DeKalb28E, produced starch-deficient and sterile pollen. Objective 2: We have established protocols for the high throughput transcriptomic approach, cDNA-AFLP, for identifying and isolating genes exhibiting differential expression in developing microspores exposed to either ambient or HS conditions and created a databank of HS-responsivemicrogametogenesis-expressed genes. A subset of differentially displayed Transcript-Derived Fragments (TDFs) that were cloned and sequenced (35 & 23 TDFs in tomato and sorghum, respectively) show close sequence similarities with metabolic genes, genes involved in regulation of carbohydrate metabolism, genes implicated in thermotolerance (heat shock proteins), genes involved in long chain fatty acids elongation, genes involved in proteolysis, in oxidation-reduction, vesicle-mediated transport, cell division and transcription factors. T-DNA-tagged Arabidopsis mutants for part of these genes were obtained to be used for their functional analysis. These studies are planned for a continuation project. Following functional analyses of these genes under HS – a valuable resource of genes, engaged in the HS-response of developing pollen grains, that could be modulated for the improvement of pollen quality under HS in both dicots and monocots and/or used to look for natural variability of such genes for selecting heat-tolerant germplasm - is expected.
APA, Harvard, Vancouver, ISO, and other styles
8

Carper, Stephen W. Heat Shock Protein 27 Inhibits Apoptosis by Binding Cytochrome C. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada410188.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Carper, Stephen W. Heat Shock Protein 27 Inhibits Apoptosis by Binding Cytochrome c. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada417947.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Podack, Eckhard. Secretory Heat Shock Protein - gp96-Ig Chaperoned her-2/New Vaccines. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada400054.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Heat shock proteins' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography