Relevant bibliographies by topics / Extracellular HSP27

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Academic literature on the topic 'Extracellular HSP27'

Author: Grafiati
Published: 1 June 2024

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Journal articles on the topic "Extracellular HSP27"

1

Stope, Matthias B., Gerd Klinkmann, Karoline Diesing, Dominique Koensgen, Martin Burchardt, and 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.

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The heat shock protein HSP27 has been correlated in ovarian cancer (OC) patients with aggressiveness and chemoresistance and, therefore, represents a promising potential biomarker for OC diagnosis, prognosis, and treatment response. Notably, secretion of soluble HSP27 has been described by a few cell types and may take place as well in OC cells. Therefore, we studied HSP27 secretion mechanisms under diverse cellular conditions in an OC cell model system. Secretion of HSP27 was characterized after overexpression of HSP27 by transfected plasmids and after heat shock. Intra- and extracellular HSP27 amounts were assessed by Western blotting and ELISA. Protein secretion was blocked by brefeldin A and the impact of the HSP27 phosphorylation status was analyzed overexpressing HSP27 phosphomutants. The present study demonstrated that HSP27 secretion by OVCAR-3 and SK-OV-3 cells depends on intracellular HSP27 concentrations. Moreover, HSP27 secretion is independent of the endoplasmic reticulum secretory pathway and HSP27 phosphorylation. Notably, analysis of OC cell-born exosomes not only confirmed the concentration-dependent correlation of HSP27 expression and secretion but also demonstrated a concentration-dependent incorporation of HSP27 protein into exosomes. Thus, secreted HSP27 may become more important as an extracellular factor which controls the tumor microenvironment and might be a noninvasive biomarker.
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2

Winter, Julia, Elke Hammer, Jacqueline Heger, Heinz-Peter Schultheiss, Ursula Rauch, Ulf Landmesser, and Andrea Dörner. "Adenine Nucleotide Translocase 1 Expression Is Coupled to the HSP27-Mediated TLR4 Signaling in Cardiomyocytes." Cells 8, no. 12 (December 6, 2019): 1588. http://dx.doi.org/10.3390/cells8121588.

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The cardiac-specific overexpression of the adenine nucleotide translocase 1 (ANT1) has cardioprotective effects in various experimental heart disease models. Here, we analyzed the link between ANT1 expression and heat shock protein 27 (HSP27)-mediated toll-like receptor 4 (TLR4) signaling, which represents a novel communication pathway between mitochondria and the extracellular environment. The interaction between ANT1 and HSP27 was identified by co-immunoprecipitation from neonatal rat cardiomyocytes. ANT1 transgenic (ANT1-TG) cardiomyocytes demonstrated elevated HSP27 expression levels. Increased levels of HSP27 were released from the ANT1-TG cardiomyocytes under both normoxic and hypoxic conditions. Extracellular HSP27 stimulated TLR4 signaling via protein kinase B (AKT). The HSP27-mediated activation of the TLR4 pathway was more pronounced in ANT1-TG cardiomyocytes than in wild-type (WT) cardiomyocytes. HSP27-specific antibodies inhibited TLR4 activation and the expression of HSP27. Inhibition of the HSP27-mediated TLR4 signaling pathway with the TLR4 inhibitor oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine (OxPAPC) reduced the mitochondrial membrane potential (∆ψm) and increased caspase 3/7 activity, which are both markers for cell stress. Conversely, treating cardiomyocytes with recombinant HSP27 protein stimulated TLR4 signaling, induced HSP27 and ANT1 expression, and stabilized the mitochondrial membrane potential. The activation of HSP27 signaling was verified in ischemic ANT1-TG heart tissue, where it correlated with ANT1 expression and the tightness of the inner mitochondrial membrane. Our study shows a new mechanism by which ANT1 is part of the cardioprotective HSP27-mediated TLR4 signaling.
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3

Gabai, Vladimir L., and Michael Y. Sherman. "Invited Review: Interplay between molecular chaperones and signaling pathways in survival of heat shock." Journal of Applied Physiology 92, no. 4 (April 1, 2002): 1743–48. http://dx.doi.org/10.1152/japplphysiol.01101.2001.

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Heat shock of mammalian cells causes protein damage and activates a number of signaling pathways. Some of these pathways enhance the ability of cells to survive heat shock, e.g., induction of molecular chaperones [heat shock protein (HSP) HSP72 and HSP27], activation of the protein kinases extracellular signal-regulated kinase and Akt, and phosphorylation of HSP27. On the other hand, heat shock can activate a stress kinase, c-Jun NH2-terminal kinase, thus triggering both apoptotic and nonapoptotic cell death programs. Recent data indicate that kinases activated by heat shock can regulate synthesis and functioning of the molecular chaperones, and these chaperones modulate activity of the cell death and survival pathways. Therefore, the overall balance of the pathways and their interplay determine whether a cell exposed to heat shock will die or survive and become stress tolerant.
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4

Singer, Debora, Can Pascal Wulff, Matthias B. Stope, and 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 (December 6, 2022): 569–78. http://dx.doi.org/10.3390/plasma5040040.

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Heat shock protein 27 (Hsp27) is a cytoprotective molecule and is inducible via oxidative stress. Anti-cancer therapies, such as the recently investigated gas plasma, subject tumor cells to a plethora of reactive oxygen species (ROS). In ovarian tumor microenvironments (TME), immune cells such as monocytes and macrophages can be found in large numbers and are often associated with cancer progression. Therefore, we quantified extracellular Hsp27 of OVCAR-3 and SK-OV-3 cells after gas plasma exposure in vitro. We found Hsp27 to be significantly increased. Following this, we investigated the effects of Hsp27 on THP-1 monocytes. Live cell imaging of Hsp27-treated THP-1 cells showed decelerated cell numbers and a reduction in cell cluster sizes. In addition, reduced metabolic activity and proliferation were identified using flow cytometry. Mitochondrial ROS production decreased. Using multicolor flow cytometry, the expression profile of eight out of twelve investigated cell surface markers was significantly modulated in Hsp27-treated THP-1 cells. A significantly decreased release of IL18 accommodated this. Taken together, our results suggest an immunomodulatory effect of Hsp27 on THP-1 monocytes. These data call for further investigations on Hsp27’s impact on the interplay of ovarian cancer cells and monocytes/macrophages under oxidative stress conditions.
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Grotegut, Pia, Sandra Kuehn, H. Burkhard Dick, and 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 (January 15, 2020): 549. http://dx.doi.org/10.3390/ijms21020549.

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Heat shock protein 27 (HSP27) is commonly involved in cellular stress. Increased levels of HSP27 as well as autoantibodies against this protein were previously detected in glaucoma patients. Moreover, systemic immunization with HSP27 induced glaucoma-like damage in rodents. Now, for the first time, the direct effects of an intravitreal HSP27 application were investigated. For this reason, HSP27 or phosphate buffered saline (PBS, controls) was applied intravitreally in rats (n = 12/group). The intraocular pressure (IOP) as well as the electroretinogram recordings were comparable in HSP27 and control eyes 21 days after the injection. However, significantly fewer retinal ganglion cells (RGCs) and amacrine cells were observed in the HSP27 group via immunohistochemistry and western blot analysis. The number of bipolar cells, on the other hand, was similar in both groups. Interestingly, a stronger neurofilament degeneration was observed in HSP27 optic nerves, while no differences were noted regarding the myelination state. In summary, intravitreal HSP27 injection led to an IOP-independent glaucoma-like damage. A degeneration of RGCs as well as their axons and amacrine cells was noted. This suggests that high levels of extracellular HSP27 could have a direct damaging effect on RGCs.
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Sevin, 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 (December 2, 2016): 1963. http://dx.doi.org/10.1182/blood.v128.22.1963.1963.

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Abstract Myelofibrosis (MF) is the most aggressive myeloproliferative neoplasms (MPN) with the highest degree of morbidity and mortality, including progressive bone marrow fibrosis resulting into bone marrow failure. JAK2 kinase inhibitors have been successfully used for a few years in MPN and more particularly for MF treatment. Despite their beneficial effects on spleen size and symptoms, JAK2 inhibitors induce low molecular and survival responses underscoring the urgent need for other therapeutic approaches. Recently, heat shock protein 90 (HSP90) - known to stabilize JAK2 - has been reported as a promising therapeutic target in MPN. However HSP90 inhibitors show toxicity and induce the expression of stress-inducible proteins like HSP70 and, most likely HSP27 as previously shown in other cancers. In addition, we and others have shown that HSP27, was strongly expressed in patients with idiopathic pulmonary, lung or kidney tubulointerstitial fibrosis, underlying a relevant role of HSP27 in fibrotic processes. Taking into account both the beneficial effects of HSP inhibitors in leukemia and in MPN, and the possible implication of HSP27 in fibrosis, we have evaluated in this work, the status of HSP27 in MF patient's samples and assess the effectiveness of an HSP27 oligonucleotide inhibitor called OGX-427. In this study, we first assessed the extracellular and intracellular level of HSPs from MF patients by ELISA, flow cytometry and by immunohistochemistry. We observed for the first time a specific increase in both intracellular and extracellular HSP27 in CD34+ circulating hematopoietic progenitor cells (n=9-16; P=0.0097) and in the sera of patients (n=24-27; P<0.0001) with MF compared with healthy donors, respectively. Moreover, we identified the presence of HSP27 in the bone marrow's MF patients. We then investigated the in vivo impact of OGX-427, a specific inhibitor of HSP27, or an oligonucleotide control in a murine TPO-induced MF mouse model. The use of OGX-427 limited the progression of the disease in our MF mouse model (n=9). In particular, OGX-427 was associated with a marked reduction in both the spleen weight and size. Also, we noted a decrease of megakaryocyte hyperplasia in the bone marrow accompanied by a visible restoration of spleen structure and lymphoid white pulp territories with OGX-427. Taking altogether, our results support a key role of HSP27 in the pathophysiology in MF and highlight the potential therapeutic benefit of HSP27 inhibitors in this disorder. Disclosures No relevant conflicts of interest to declare.
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Grotegut, Pia, Philipp Johannes Hoerdemann, Sabrina Reinehr, Nupur Gupta, H. Burkhard Dick, and 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 (January 6, 2021): 513. http://dx.doi.org/10.3390/ijms22020513.

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Heat shock protein 27 (HSP27) is one of the small molecular chaperones and is involved in many cell mechanisms. Besides the known protective and helpful functions of intracellular HSP27, very little is known about the mode of action of extracellular HSP27. In a previous study, we showed that intravitreal injection of HSP27 led to neuronal damage in the retina and optic nerve after 21 days. However, it was not clear which degenerative signaling pathways were induced by the injection. For this reason, the pathological mechanisms of intravitreal HSP27 injection after 14 days were investigated. Histological and RT-qPCR analyses revealed an increase in endogenous HSP27 in the retina and an activation of components of the intrinsic and extrinsic apoptosis pathway. In addition, an increase in nucleus factor-kappa-light-chain-enhancer of activated B cells (NFκB), as well as of microglia/macrophages and T-cells could be observed. In the optic nerve, however, only an increased apoptosis rate was detectable. Therefore, the activation of caspases and the induction of an incipient immune response seem to be the main triggers for retinal degeneration in this intravitreal HSP27 model.
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8

Bitar, K. N., A. Ibitayo, and 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 (January 1, 2002): 41–49. http://dx.doi.org/10.1152/jappl.2002.92.1.41.

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The recruitment of signal transduction molecules to the membrane is crucial for the efficient coupling of extracellular signals and contractile response. The trafficking is dynamic. We have investigated a possible cross talk between agonist-induced association of translocated RhoA and translocated protein kinase C-α (PKC-α) and a role for heat shock protein 27 (HSP27) in mediating this interaction. Immunoprecipitation with HSP27 monoclonal antibody followed by immunoblotting with either RhoA antibody or PKC-α antibody indicated that acetylcholine induced associations of HSP27-RhoA and HSP27-PKC-α in the membrane fraction but not in the cytosolic fraction. Immunoprecipitation with anti-RhoA monoclonal antibody followed by immunoblotting with PKC-α antibody indicated that acetylcholine induced a significant complexing of RhoA-PKC-α in the membrane fraction but not in the cytosolic fraction. In summary, the data indicate that agonist-induced contraction is associated with 1) association of translocated RhoA with HSP27 on the membrane, 2) association of translocated PKC-α with HSP27 on the membrane, and 3) association of PKC-α with RhoA on the membrane. The data suggest an important role for HSP27 in modulating a multiprotein complex that includes translocated RhoA and PKC-α.
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9

Musiał, Kinga, and Danuta Zwolińska. "Extracellular Hsp27 in patients with chronic kidney disease." Kidney International 83, no. 5 (May 2013): 971. http://dx.doi.org/10.1038/ki.2013.33.

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10

Hatakeyama, Daijiro, Osamu Kozawa, Masayuki Niwa, Hiroyuki Matsuno, Kanefusa Kato, Norichika Tatematsu, Toshiyuki Shibata, and 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 (December 1, 2001): E1260—E1266. http://dx.doi.org/10.1152/ajpendo.2001.281.6.e1260.

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We have previously reported that endothelin-1 (ET-1) stimulates heat shock protein (HSP) 27 induction in osteoblast-like MC3T3-E1 cells and that p38 mitogen-activated protein (MAP) kinase acts at a point downstream from protein kinase C (PKC) in HSP27 induction. In the present study, we investigated the effect of the adenylyl cyclase-cAMP system on ET-1-stimulated induction of HSP27 in MC3T3-E1 cells. Dibutyryl-cAMP (DBcAMP) dose dependently inhibited the HSP27 accumulation stimulated by ET-1. Forskolin and cholera toxin significantly suppressed the ET-1-stimulated accumulation of HSP27. However, dideoxyforskolin, a forskolin derivative that does not activate cAMP, failed to suppress the ET-1-induced HSP27 accumulation. Forskolin reduced the p38 MAP kinase phosphorylation induced by ET-1 or 12- O-tetradecanoylphorbol-13-acetate (TPA). PGE1, an extracellular agonist that activates cAMP production, reduced the ET-1-induced HSP27 accumulation. In addition, the phosphorylation of p38 MAP kinase induced by ET-1 or TPA was suppressed by PGE1. Forskolin, DBcAMP, and PGE1suppressed the ET-1-stimulated increase in the mRNA level for HSP27. These results indicate that the adenylyl cyclase-cAMP system has an inhibitory role in ET-1-stimulated HSP27 induction in osteoblasts and that the effect is exerted at the point between PKC and p38 MAP kinase in osteoblasts.
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Dissertations / Theses on the topic "Extracellular HSP27"

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Williams, Helen. "Interactions between extracellular Hsp72 and blood cells." Thesis, University of Chester, 2010. http://hdl.handle.net/10034/277691.

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In recent years, compelling evidence has accumulated suggesting heat shock proteins (HSPs) which are generally believed to be localised and functioning mainly within eukaryotic cells as cyto-protective molecular chaperones, are also localised in the extracellular milieu. Depending on their localisation, on the cell surface (membrance-bound or embedded), or in the peripheral circulation, extracellular HSPs may induce apoptotic cell death, or in contrast protect cells from cell damage and/or cell death when exposed to cellular stress, or may even elicit a stimulatory effect on the innate immune response including cell activiation and cytokine secretion. Hence, the localisation of intracellular and extracellular HSPs appears to be critical in determining their roles in terms of stimulating cell death, cyto-protection, or immune activiation under normal physiological conditions and following exposure to stress stimuli. This thesis describes the intracellular expression, up-regulation, and cell surface localisation of endogenous HSPs: HSP27, Hsp60, Hsp72 and Hsp90 by flow cytometry, florescence microscopy and Western blotting, under control conditions and in response to environmental stress using in vitro and ex vivo models with the intention of determining their physiological roles. The ability of extracellularly administered HSPs (Hsp70 and Hsp72) to protect cultured U937 cells in vitro or peripheral primary human leukogytes or erythrocytes ex vivo from various stress stimuli was demonstrated and was found to be dependent on surface binding and/or internalisation via scavenger receptors (SRs) or phosphatidylserine (PS), which could be blocked by receptor specific ligands. Extracellular HSPs were also shown to be able to stimulate an immune response through the induction of U937 monocyte differentiation into macrophages as evidenced through the up-regulation of the surface receptors: CD36, SR-A1 and CD91 analysed by flow cytometry. These proteins were able to stimulate TNF-x and IL-10 production and secretion by U937 macrophages, shown by ELISA, and chemotatic properties were demonstrated using Boyden chambers. The cyto-protective and immune regulatory effects of extracellular HSPs have potential therapeutic value as treatments in a wide variety of clinical situations.
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Tsai, Tsen-Ni, and 蔡甄妮. "The role of extracellular Hsp72 during sepsis." Thesis, 2015. http://ndltd.ncl.edu.tw/handle/g5c8ft.

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博士
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.
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Book chapters on the topic "Extracellular HSP27"

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Fleshner, Monika, Thomas Maslanik, and Lida A. Beninson. "In Vivo Tissue Source and Releasing Signal for Endogenous Extracellular Hsp72." In 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.

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FLESHNER, MONIKA, CRAIG M. SHARKEY, MOLLY NICKERSON, and JOHN D. JOHNSON. "Endogenous Extracellular Hsp72 Release Is an Adaptive Feature of the Acute Stress Response." In Psychoneuroimmunology, 1013–34. Elsevier, 2007. http://dx.doi.org/10.1016/b978-012088576-3/50055-1.

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Conference papers on the topic "Extracellular HSP27"

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Pommerolle, Lenny, Olivier Burgy, Lucile Dondaine, Pierre-Marie Boutanquoi, Guillaume Beltramo, Julie Tanguy, Sabrina Loriod, Carmen Garrido, Philippe Bonniaud, and Françoise Goirand. "Role of Extracellular HSP27 in pulmonary fibrosis." In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.601.

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Pommerolle, Lenny, Pierre-Marie Boutanquoi, Florent Thevenet, Lucile Dondaine, Maximilien Spanjaard, Guillaume Beltramo, Carmen Garrido, Philippe Bonniaud, and Françoise Goirand. "Role of extracellular HSP27 in idiopathic pulmonary fibrosis (IPF)." In 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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