Relevant bibliographies by topics / Extracellular HSP27

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Extracellular HSP27'

Author: Grafiati
Published: 1 June 2024
Last updated: 31 July 2025

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Journal articles on the topic "Extracellular HSP27"

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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 HSP
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Winter, Julia, Elke Hammer, Jacqueline Heger, et al. "Adenine Nucleotide Translocase 1 Expression Is Coupled to the HSP27-Mediated TLR4 Signaling in Cardiomyocytes." Cells 8, no. 12 (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. Incr
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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 (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 synth
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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 (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 effe
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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 (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 co
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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 (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. Hi
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Bitar, K. N., A. Ibitayo та 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, № 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-PK
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Sevin, Margaux, Nicolas Pernet, Franck Vitte, et al. "HSP27: A Therapeutic Target in Myelofibrosis." Blood 128, no. 22 (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 reporte
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Hatakeyama, Daijiro, Osamu Kozawa, Masayuki Niwa, et al. "Inhibition by adenylyl cyclase-cAMP system of ET-1-induced HSP27 in osteoblasts." American Journal of Physiology-Endocrinology and Metabolism 281, no. 6 (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. Howev
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Musiał, Kinga, and Danuta Zwolińska. "Extracellular Hsp27 in patients with chronic kidney disease." Kidney International 83, no. 5 (2013): 971. http://dx.doi.org/10.1038/ki.2013.33.

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Dissertations / Theses on the topic "Extracellular HSP27"

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Pommerolle, Lenny. "Identification de nouvelles cibles thérapeutiques dans la fibrose pulmonaire idiopathique : Etude du récepteur CD206 et des protéines de choc thermique HSP27 et αB-crystallin". Electronic Thesis or Diss., Bourgogne Franche-Comté, 2021. https://nuxeo.u-bourgogne.fr/nuxeo/site/esupversions/951bd793-5b06-4843-81c4-0d887829fdba.

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La fibrose pulmonaire idiopathique (FPI) est une maladie rare, qui constitue la forme la plus fréquence de pneumopathie interstitielle diffuse de l’adulte. Elle se caractérise par une accumulation massive de matrice extracellulaire, principalement de collagène, dans le parenchyme pulmonaire, ce qui entraine une altération dramatique et irréversible de la fonction respiratoire. La FPI est une pathologie mortelle qui survient principalement après 60 ans, et sa médiane de survie est d’environ 5 ans après diagnostic. Il n’existe aucun traitement curatif. A ce jour seuls 2 médicaments, la pirfénido
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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
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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<br>高雄醫學大學<br>醫學研究所博士班<br>103<br>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
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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. 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. 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, et al. "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, et al. "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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