Littérature scientifique sur le sujet « Extracellular HSP27 »
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Articles de revues sur le sujet "Extracellular HSP27"
Stope, Matthias B., Gerd Klinkmann, Karoline Diesing, Dominique Koensgen, Martin Burchardt et Alexander Mustea. « Heat Shock Protein HSP27 Secretion by Ovarian Cancer Cells Is Linked to Intracellular Expression Levels, Occurs Independently of the Endoplasmic Reticulum Pathway and HSP27’s Phosphorylation Status, and Is Mediated by Exosome Liberation ». Disease Markers 2017 (2017) : 1–12. http://dx.doi.org/10.1155/2017/1575374.
Texte intégralWinter, Julia, Elke Hammer, Jacqueline Heger, Heinz-Peter Schultheiss, Ursula Rauch, Ulf Landmesser et Andrea Dörner. « Adenine Nucleotide Translocase 1 Expression Is Coupled to the HSP27-Mediated TLR4 Signaling in Cardiomyocytes ». Cells 8, no 12 (6 décembre 2019) : 1588. http://dx.doi.org/10.3390/cells8121588.
Texte intégralGabai, Vladimir L., et Michael Y. Sherman. « Invited Review : Interplay between molecular chaperones and signaling pathways in survival of heat shock ». Journal of Applied Physiology 92, no 4 (1 avril 2002) : 1743–48. http://dx.doi.org/10.1152/japplphysiol.01101.2001.
Texte intégralSinger, Debora, Can Pascal Wulff, Matthias B. Stope et Sander Bekeschus. « Extracellular Heat Shock Protein 27 Is Released by Plasma-Treated Ovarian Cancer Cells and Affects THP-1 Monocyte Activity ». Plasma 5, no 4 (6 décembre 2022) : 569–78. http://dx.doi.org/10.3390/plasma5040040.
Texte intégralGrotegut, Pia, Sandra Kuehn, H. Burkhard Dick et Stephanie C. Joachim. « Destructive Effect of Intravitreal Heat Shock Protein 27 Application on Retinal Ganglion Cells and Neurofilament ». International Journal of Molecular Sciences 21, no 2 (15 janvier 2020) : 549. http://dx.doi.org/10.3390/ijms21020549.
Texte intégralSevin, Margaux, Nicolas Pernet, Franck Vitte, Selim Ramla, Paul Sagot, Laurent Martin, Jean Luc Villeval et al. « HSP27 : A Therapeutic Target in Myelofibrosis ». Blood 128, no 22 (2 décembre 2016) : 1963. http://dx.doi.org/10.1182/blood.v128.22.1963.1963.
Texte intégralGrotegut, Pia, Philipp Johannes Hoerdemann, Sabrina Reinehr, Nupur Gupta, H. Burkhard Dick et Stephanie C. Joachim. « Heat Shock Protein 27 Injection Leads to Caspase Activation in the Visual Pathway and Retinal T-Cell Response ». International Journal of Molecular Sciences 22, no 2 (6 janvier 2021) : 513. http://dx.doi.org/10.3390/ijms22020513.
Texte intégralBitar, K. N., A. Ibitayo et S. B. Patil. « HSP27 modulates agonist-induced association of translocated RhoA and PKC-α in muscle cells of the colon ». Journal of Applied Physiology 92, no 1 (1 janvier 2002) : 41–49. http://dx.doi.org/10.1152/jappl.2002.92.1.41.
Texte intégralMusiał, Kinga, et Danuta Zwolińska. « Extracellular Hsp27 in patients with chronic kidney disease ». Kidney International 83, no 5 (mai 2013) : 971. http://dx.doi.org/10.1038/ki.2013.33.
Texte intégralHatakeyama, Daijiro, Osamu Kozawa, Masayuki Niwa, Hiroyuki Matsuno, Kanefusa Kato, Norichika Tatematsu, Toshiyuki Shibata et Toshihiko Uematsu. « Inhibition by adenylyl cyclase-cAMP system of ET-1-induced HSP27 in osteoblasts ». American Journal of Physiology-Endocrinology and Metabolism 281, no 6 (1 décembre 2001) : E1260—E1266. http://dx.doi.org/10.1152/ajpendo.2001.281.6.e1260.
Texte intégralThèses sur le sujet "Extracellular HSP27"
Williams, Helen. « Interactions between extracellular Hsp72 and blood cells ». Thesis, University of Chester, 2010. http://hdl.handle.net/10034/277691.
Texte intégralTsai, Tsen-Ni, et 蔡甄妮. « The role of extracellular Hsp72 during sepsis ». Thesis, 2015. http://ndltd.ncl.edu.tw/handle/g5c8ft.
Texte intégral高雄醫學大學
醫學研究所博士班
103
Background: Sepsis, the leading cause of death in intensive care units, annually affects more than 500,000 patients in the United States; despite advances in treatment and supportive care, the mortality rate remains higher than 20%. Our previous study revealed that heat shock reduces the sepsis-related mortality rate by increasing the expression of heat shock protein 72 (Hsp72, also known as Hp70). Hsp72, a molecular chaperone intracellularly induced by stress, exhibits antiinflammatory and antiapoptotic effects. Hsp72 protects cells and is released into the circulation by various cells in response to stress and toxic treatments. However, the precise role of extracellular Hsp72 (eHsp72) during sepsis remains unclear . The present study was divided into two parts; the first part was conducted to clarify the effect of eHsp72 on the sepsis-related survival rate and to determine the underlying factors. The second part was conducted to assess the hypothesis that eHsp72 is involved in reversing sepsis-induced liver dysfunction. Methods: Part 1: Sepsis was induced by cecal ligation and puncture (CLP). Changes in serum levels of Hsp72 and cytokines were determined during sepsis, and the results were correlated with the survival rate. The effects of heat pretreatment on Hsp72 expression in septic rat leukocytes and those of septic rat serum, lipopolysaccharide (LPS), and certain cytokines on Hsp72 expression in macrophage NR8383 cells were 7 determined. Part II: Liver function was determined on the basis of changes in the enzymatic activities of serum glutamic oxaloacetic transaminase (GOT) and glutamic pyruvic transaminase (GPT). Apoptosis was measured using terminal deoxynucleotidyl transferase dUTP nick end labeling staining. The expression of Bcl-2, Bax, cleaved caspase-3 and -9, and cleaved poly(ADP ribose) polymerase (PARP) in liver tissue was analyzed using W estern blotting. Results: Part 1: Circulating Hsp72 levels increased during sepsis (0, 5.5, 6.5, 10, and 6.5 ng/mL at 0, 3, 6, 9, and 18 h after CLP), positively correlating with survival rates. LPS triggered Hsp72 expression in heat-pretreated rats. Heat pretreatment also increased Hsp72 expression in nonseptic (535%, p < 0.01) and septic (116%, p < 0.01) rat leukocytes. Furthermore, incubating the serum of septic rats with NR8383 cells increased eHsp72 levels in a cultured medium. Cytokine profiling revealed that among the 19 cytokines screened, the levels of cytokine-induced neutrophil chemoattractant 3 (211.3%, p < 0.05), interleukin-10 (147%, p < 0.05), monocyte chemotactic protein 1 (MCP-1; 49.6%, p < 0.05), and tumor necrosis factor alpha (51.8%, p < 0.05) increased. MCP-1 and LPS released Hsp72 from NR8383 cells. Part II: The results revealed that GOT and GPT activities increased by 126% and 121%, respectively, during sepsis and returned to the control level following the administration of recombinant human Hsp72 (rhHsp72). During sepsis, apoptotic cells 8 in liver tissue were augmented (665.7%, p < 0.01); however, the effect was reversed on treatment with rhHsp72. Furthermore, during sepsis, Bcl-2/Bax protein expression in liver tissue was downregulated (&;#8722;26%; p < 0.01), and the downregulation was diminished after rhHsp72 treatment. Moreover, during sepsis, expression of cleaved capase-3, cleaved caspase-9, and PARP in liver tissue was upregulated by 40.9%, 103.3%, and 1106%, respectively, and the upregulation was reversed after treatment with rhHsp72. Conclusion: These results demonstrate that increases in levels of circulating Hsp72 improved the survival rate during sepsis. The increases in circulating Hsp72 may be mediated through MCP-1 and/or LPS. Moreover, during sepsis, eHsp72 restored liver function by ameliorating apoptosis through the mitochondria-initiated caspase pathway . Our findings provide a biochemical basis for the development of rhHsp72 as a therapeutic agent for sepsis management.
Chapitres de livres sur le sujet "Extracellular HSP27"
Fleshner, Monika, Thomas Maslanik et Lida A. Beninson. « In Vivo Tissue Source and Releasing Signal for Endogenous Extracellular Hsp72 ». Dans Heat Shock Proteins and Whole Body Physiology, 193–215. Dordrecht : Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3381-9_12.
Texte intégralFLESHNER, MONIKA, CRAIG M. SHARKEY, MOLLY NICKERSON et JOHN D. JOHNSON. « Endogenous Extracellular Hsp72 Release Is an Adaptive Feature of the Acute Stress Response ». Dans Psychoneuroimmunology, 1013–34. Elsevier, 2007. http://dx.doi.org/10.1016/b978-012088576-3/50055-1.
Texte intégralActes de conférences sur le sujet "Extracellular HSP27"
Pommerolle, Lenny, Olivier Burgy, Lucile Dondaine, Pierre-Marie Boutanquoi, Guillaume Beltramo, Julie Tanguy, Sabrina Loriod, Carmen Garrido, Philippe Bonniaud et Françoise Goirand. « Role of Extracellular HSP27 in pulmonary fibrosis ». Dans ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.601.
Texte intégralPommerolle, Lenny, Pierre-Marie Boutanquoi, Florent Thevenet, Lucile Dondaine, Maximilien Spanjaard, Guillaume Beltramo, Carmen Garrido, Philippe Bonniaud et Françoise Goirand. « Role of extracellular HSP27 in idiopathic pulmonary fibrosis (IPF) ». Dans Abstracts from the 17th ERS Lung Science Conference : ‘Mechanisms of Acute Exacerbation of Respiratory Disease’. European Respiratory Society, 2019. http://dx.doi.org/10.1183/23120541.lungscienceconference-2019.pp108.
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