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Journal articles on the topic 'HSP27 extracellulaire'

Author: Grafiati

Published: 1 June 2024

Last updated: 31 July 2025

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1

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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2

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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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 (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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5

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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Johnson, John D., Jay Campisi, Craig M. Sharkey, Sarah L. Kennedy, Molly Nickerson, and Monika Fleshner. "Adrenergic receptors mediate stress-induced elevations in extracellular Hsp72." Journal of Applied Physiology 99, no. 5 (2005): 1789–95. http://dx.doi.org/10.1152/japplphysiol.00390.2005.

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Heat-shock protein concentrations in the blood increase after exposure to a variety of stressors, including trauma and psychological stress. Although the physiological function of extracellular heat shock protein remains controversial, there is evidence that extracellular heat shock protein 72 (Hsp72) can facilitate immunologic responses. The signal(s) that mediate(s) the in vivo elevation of extracellular Hsp72 in the blood after stressor exposure remain(s) unknown. Here we report that Hsp72 increases in the circulation via an α1-adrenergic receptor-mediated signaling pathway. Activation of α

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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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8

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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9

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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10

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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11

Arslan, Badel, Nurcan Aras, Selma Yaman, and Ulku Comelekoglu. "Investigation of genetic stress parameters in brain tissues of rats exposed to 1.8 GHz cell phone radiofrequency electromagnetic field." Medicine Science | International Medical Journal 13, no. 1 (2024): 78. http://dx.doi.org/10.5455/medscience.2023.06.094.

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Heat Shock Proteins (HSPs) may induce various cellular processes, including replication, apoptosis, cell-cycle progression. Mitogen-activated protein kinase (MAPK) cascades are the primary mechanism that mediates the cellular stress response to extracellular stimuli and regulates transcriptional activity. It has been shown that mobile phone exposure can stimulate the Hsp27/p38MAPK stress pathway. In this study, twenty-seven mature female Wistar albino rats were exposed to 1.8 GHz radiofrequency electromagnetic field (RF-EMF) 2h/day for 8 weeks (SAR: 0.06 W/kg). Hsp27 and p38MAPK gene expressio

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Shi, Chunhua, Daiana Alvarez-Olmedo, Yuan Zhang, Badal S. B. Pattar, and Edward R. O’Brien. "The Heat Shock Protein 27 Immune Complex Enhances Exosomal Cholesterol Efflux." Biomedicines 8, no. 8 (2020): 290. http://dx.doi.org/10.3390/biomedicines8080290.

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Previously, we demonstrated that Heat Shock Protein 27 (HSP27) reduces the inflammatory stages of experimental atherogenesis, is released by macrophage (MΦ) exosomes and lowers cholesterol levels in atherosclerotic plaques. Recently, we discovered that natural autoantibodies directed against HSP27 enhance its signaling effects, as HSP27 immune complexes (IC) interact at the cell membrane to modulate signaling. We now seek to evaluate the potential role of the HSP27 IC on MΦ exosomal release and cholesterol export. First, in human blood samples, we show that healthy control subjects have 86% mo

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13

Singer, Debora, Verena Ressel, Matthias B. Stope, and Sander Bekeschus. "Heat Shock Protein 27 Affects Myeloid Cell Activation and Interaction with Prostate Cancer Cells." Biomedicines 10, no. 9 (2022): 2192. http://dx.doi.org/10.3390/biomedicines10092192.

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Heat shock proteins are cytoprotective molecules induced by environmental stresses. The small heat shock protein 27 (Hsp27) is highly expressed under oxidative stress conditions, mediating anti-oxidative effects and blocking apoptosis. Since medical gas plasma treatment subjects cancer cells to a multitude of reactive oxygen species (ROS), inducing apoptosis and immunomodulation, probable effects of Hsp27 should be investigated. To this end, we quantified the extracellular Hsp27 in two prostate cancer cell lines (LNCaP, PC-3) after gas plasma-induced oxidative stress, showing a significantly e

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14

Yamboliev, Ilia A., Jason C. Hedges, Jack L. M. Mutnick, Leonard P. Adam, and William T. Gerthoffer. "Evidence for modulation of smooth muscle force by the p38 MAP kinase/HSP27 pathway." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 6 (2000): H1899—H1907. http://dx.doi.org/10.1152/ajpheart.2000.278.6.h1899.

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Mitogen-activated protein (MAP) kinases signal to proteins that could modify smooth muscle contraction. Caldesmon is a substrate for extracellular signal-related kinases (ERK) and p38 MAP kinases in vitro and has been suggested to modulate actin-myosin interaction and contraction. Heat shock protein 27 (HSP27) is downstream of p38 MAP kinases presumably participating in the sustained phase of muscle contraction. We tested the role of caldesmon and HSP27 phosphorylation in the contractile response of vascular smooth muscle by using inhibitors of both MAP kinase pathways. In intact smooth muscle

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15

Hyväri, Laura, Sari Vanhatupa, Miina Ojansivu, et al. "Heat Shock Protein 27 Is Involved in the Bioactive Glass Induced Osteogenic Response of Human Mesenchymal Stem Cells." Cells 12, no. 2 (2023): 224. http://dx.doi.org/10.3390/cells12020224.

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Bioactive glass (BaG) materials are increasingly used in clinics, but their regulatory mechanisms on osteogenic differentiation remain understudied. In this study, we elucidated the currently unknown role of the p38 MAPK downstream target heat shock protein 27 (HSP27), in the osteogenic commitment of human mesenchymal stem cells (hMSCs), derived from adipose tissue (hASCs) and bone marrow (hBMSCs). Osteogenesis was induced with ionic extract of an experimental BaG in osteogenic medium (OM). Our results showed that BaG OM induced fast osteogenesis of hASCs and hBMSCs, demonstrated by enhanced a

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16

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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17

Guay, J., H. Lambert, G. Gingras-Breton, J. N. Lavoie, J. Huot, and J. Landry. "Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27." Journal of Cell Science 110, no. 3 (1997): 357–68. http://dx.doi.org/10.1242/jcs.110.3.357.

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We have studied the contribution of the individual kinases of the MAP (mitogen-activated protein) kinase family, including ERK (extracellular-signal regulated kinase), JNK/SAPK (c-JUN NH2-terminal kinase/stress-activated protein kinase) and p38, to activation of the HSP27 (heat shock protein 27) kinase MAPKAP kinase-2/3 and to HSP27 phosphorylation in Chinese hamster CCL39 cells stimulated by either growth factors, cytokines or stressing agents. In vitro assays using fractionated cell extracts or immunoprecipitates indicated that only fractions containing ERK or p38, and not those containing J

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18

Ishida, Yoshihito, Hiroshi Kubota, Akitsugu Yamamoto, Akira Kitamura, Hans Peter Bächinger, and Kazuhiro Nagata. "Type I Collagen in Hsp47-null Cells Is Aggregated in Endoplasmic Reticulum and Deficient in N-Propeptide Processing and Fibrillogenesis." Molecular Biology of the Cell 17, no. 5 (2006): 2346–55. http://dx.doi.org/10.1091/mbc.e05-11-1065.

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Heat-shock protein of 47 kDa (Hsp47) is a molecular chaperone that recognizes collagen triple helices in the endoplasmic reticulum (ER). Hsp47-knockout mouse embryos are deficient in the maturation of collagen types I and IV, and collagen triple helices formed in the absence of Hsp47 show increased susceptibility to protease digestion. We show here that the fibrils of type I collagen produced by Hsp47-/- cells are abnormally thin and frequently branched. Type I collagen was highly accumulated in the ER of Hsp47-/- cells, and its secretion rate was much slower than that of Hsp47+/+ cells, leadi

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Thuringer, Dominique, Gaetan Jego, Guillaume Wettstein, et al. "Extracellular HSP27 mediates angiogenesis through Toll‐like receptor 3." FASEB Journal 27, no. 10 (2013): 4169–83. http://dx.doi.org/10.1096/fj.12-226977.

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20

Osorio, Luis A., Mauricio Lozano, Paola Soto, et al. "Levels of Small Extracellular Vesicles Containing hERG-1 and Hsp47 as Potential Biomarkers for Cardiovascular Diseases." International Journal of Molecular Sciences 25, no. 9 (2024): 4913. http://dx.doi.org/10.3390/ijms25094913.

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The diagnosis of cardiovascular disease (CVD) is still limited. Therefore, this study demonstrates the presence of human ether-a-go-go-related gene 1 (hERG1) and heat shock protein 47 (Hsp47) on the surface of small extracellular vesicles (sEVs) in human peripheral blood and their association with CVD. In this research, 20 individuals with heart failure and 26 participants subjected to cardiac stress tests were enrolled. The associations between hERG1 and/or Hsp47 in sEVs and CVD were established using Western blot, flow cytometry, electron microscopy, ELISA, and nanoparticle tracking analysis

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Huot, Jacques, François Houle, Simon Rousseau, Réna G. Deschesnes, Girish M. Shah, and Jacques Landry. "SAPK2/p38-dependent F-Actin Reorganization Regulates Early Membrane Blebbing during Stress-induced Apoptosis." Journal of Cell Biology 143, no. 5 (1998): 1361–73. http://dx.doi.org/10.1083/jcb.143.5.1361.

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In endothelial cells, H2O2 induces the rapid formation of focal adhesion complexes at the ventral face of the cells and a major reorganization of the actin cytoskeleton into dense transcytoplasmic stress fibers. This change in actin dynamics results from the activation of the mitogen-activated protein (MAP) kinase stress-activated protein kinase-2/p38 (SAPK2/p38), which, via MAP kinase-activated protein (MAPKAP) kinase-2/3, leads to the phosphorylation of the actin polymerization modulator heat shock protein of 27 kD (HSP27). Here we show that the concomitant activation of the extracellular si

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Asea, Alexzander. "Initiation of the Immune Response by Extracellular Hsp72: Chaperokine Activity of Hsp72." Current Immunology Reviews 2, no. 3 (2006): 209–15. http://dx.doi.org/10.2174/157339506778018514.

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Yamada, Paulette M., Fabiano T. Amorim, Pope Moseley, Robert Robergs, and Suzanne M. Schneider. "Effect of heat acclimation on heat shock protein 72 and interleukin-10 in humans." Journal of Applied Physiology 103, no. 4 (2007): 1196–204. http://dx.doi.org/10.1152/japplphysiol.00242.2007.

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Heat acclimation (HA) results in whole body adaptations that increase heat tolerance, and in addition, HA may also result in protective cellular adaptations. We hypothesized that, after HA, basal intracellular heat shock protein (HSP) 72 and extracellular IL-10 levels would increase, while extracellular HSP72 levels decrease. Ten male and two female subjects completed a 10-day exercise/HA protocol (100-min exercise bout at 56% of maximum O2 uptake in a 42.5°C DB, 27.9% RH environment); subjects exhibited classic adaptations that accompany HA. Peripheral blood mononuclear cells (PBMCs) were iso

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Ganter, Michael T., Lorraine B. Ware, Marybeth Howard, et al. "Extracellular heat shock protein 72 is a marker of the stress protein response in acute lung injury." American Journal of Physiology-Lung Cellular and Molecular Physiology 291, no. 3 (2006): L354—L361. http://dx.doi.org/10.1152/ajplung.00405.2005.

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Previous studies have shown that heat shock protein 72 (Hsp72) is found in the extracellular space (eHsp72) and that eHsp72 has potent immunomodulatory effects. However, whether eHsp72 is present in the distal air spaces and whether eHsp72 could modulate removal of alveolar edema is unknown. The first objective was to determine whether Hsp72 is released within air spaces and whether Hsp72 levels in pulmonary edema fluid would correlate with the capacity of the alveolar epithelium to remove alveolar edema fluid in patients with ALI/ARDS. Patients with hydrostatic edema served as controls. The s

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Xiong, Gaofeng, Jie Chen, Guoying Zhang, et al. "Hsp47 promotes cancer metastasis by enhancing collagen-dependent cancer cell-platelet interaction." Proceedings of the National Academy of Sciences 117, no. 7 (2020): 3748–58. http://dx.doi.org/10.1073/pnas.1911951117.

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Increased expression of extracellular matrix (ECM) proteins in circulating tumor cells (CTCs) suggests potential function of cancer cell-produced ECM in initiation of cancer cell colonization. Here, we showed that collagen and heat shock protein 47 (Hsp47), a chaperone facilitating collagen secretion and deposition, were highly expressed during the epithelial-mesenchymal transition (EMT) and in CTCs. Hsp47 expression induced mesenchymal phenotypes in mammary epithelial cells (MECs), enhanced platelet recruitment, and promoted lung retention and colonization of cancer cells. Platelet depletion

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Gabai, Vladimir L., Julia A. Yaglom, Todd Waldman, and Michael Y. Sherman. "Heat Shock Protein Hsp72 Controls Oncogene-Induced Senescence Pathways in Cancer Cells." Molecular and Cellular Biology 29, no. 2 (2008): 559–69. http://dx.doi.org/10.1128/mcb.01041-08.

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ABSTRACT The heat shock protein Hsp72 is expressed at the elevated levels in various human tumors, and its levels often correlate with poor prognosis. Previously we reported that knockdown of Hsp72 in certain cancer cells, but not in untransformed breast epithelial cells, triggers senescence via p53-dependent and p53-independent mechanisms. Here we demonstrate that the p53-dependent pathway controlled by Hsp72 depends on the oncogenic form of phosphatidylinositol 3-kinase (PI3K). Indeed, upon expression of the oncogenic PI3K, epithelial cells began responding to Hsp72 depletion by activating t

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Beck, Franz-X., Wolfgang Neuhofer, and Eva Müller. "Molecular chaperones in the kidney: distribution, putative roles, and regulation." American Journal of Physiology-Renal Physiology 279, no. 2 (2000): F203—F215. http://dx.doi.org/10.1152/ajprenal.2000.279.2.f203.

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Molecular chaperones are intracellular proteins that prevent inappropriate intra- and intermolecular interactions of polypetide chains. A specific group of highly conserved molecular chaperones are the heat shock proteins (HSPs), many of which are constitutively expressed but most of which are inducible by diverse (in some cases specific) stress factors. HSPs, either alone or in cooperation with “partner” chaperones, are involved in cellular processes as disparate as correct folding and assembly of proteins, transport of proteins to specific intracellular locations, protein degradation, and pr

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Edwards, Helen V., John D. Scott, and George S. Baillie. "The A-kinase-anchoring protein AKAP-Lbc facilitates cardioprotective PKA phosphorylation of Hsp20 on Ser16." Biochemical Journal 446, no. 3 (2012): 437–43. http://dx.doi.org/10.1042/bj20120570.

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Hsp20 (heat-shock protein of 20 kDa; HspB6) is a cardioprotective agent which combats a number of pathophysiological processes in the heart, including hypertrophy, apoptosis and ischaemia/reperfusion injury. The cardioprotective actions of Hsp20 require its phosphorylation by PKA (cAMP-dependent protein kinase) on Ser16. Although the extracellular stimuli that promote cAMP-responsive phosphorylation of Hsp20 are well known, less is understood about the molecular processes that regulate this modification. AKAPs (A-kinase-anchoring proteins) physically compartmentalize PKA to specific locations

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Xue, Jing, Jie Zhou, and Janos Zempleni. "Holocarboxylase synthetase catalyzes biotinylation of heat shock protein 72, thereby inducing RANTES expression in HEK-293 cells." American Journal of Physiology-Cell Physiology 305, no. 12 (2013): C1240—C1245. http://dx.doi.org/10.1152/ajpcell.00279.2013.

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In a recent mass spectrometry screen, we identified 108 new proteins that were modified endogenously by covalent binding of biotin; members of the heat shock superfamily of proteins, including heat shock protein 72 (HSP72), were overrepresented among the biotinylated proteins. Mammals respond to infections by secreting extracellular HSP72 (eHSP72), which elicits an immune response. Here, using mass spectrometry and site-directed mutagenesis, we identified five biotinylation sites in HSP72. We used coimmunoprecipitation, mass spectrometry, and limited proteolysis assays to demonstrate that HSP7

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Lee, W. C., H. C. Wen, C. P. Chang, M. Y. Chen, and M. T. Lin. "Heat shock protein 72 overexpression protects against hyperthermia, circulatory shock, and cerebral ischemia during heatstroke." Journal of Applied Physiology 100, no. 6 (2006): 2073–82. http://dx.doi.org/10.1152/japplphysiol.01433.2005.

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This study extends our earlier studies in rats by applying our heatstroke model to a new species. Additionally, transgenic mice are used to examine the role of heat shock protein (HSP) 72 in experimental heatstroke. Transgenic mice that were heterozygous for a porcine HSP70i gene ([+]HSP72), transgene-negative littermate controls ([−]HSP72), and normal Institute of Cancer Research strain mice (ICR) under pentobarbital sodium anesthesia were subjected to heat stress (40°C) to induce heatstroke. In [−]HSP72 or ICR, the values for mean arterial pressure, the striatal blood flow, and the striatal

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Neuhofer, Wolfgang, Karin Lugmayr, Maria-Luisa Fraek, and Franz-X. Beck. "Regulated Overexpression of Heat Shock Protein 72 Protects Madin-Darby Canine Kidney Cells from the Detrimental Effects of High Urea Concentrations." Journal of the American Society of Nephrology 12, no. 12 (2001): 2565–71. http://dx.doi.org/10.1681/asn.v12122565.

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ABSTRACT. Exposure of renal medullary cells to elevated extracellular NaCl concentrations is associated with increased heat shock protein 72 (HSP72) expression and improved resistance to subsequent exposure to a high urea concentration (600 mM). To establish a causal relationship between HSP72 expression and protection against high urea concentrations, HSP72 was inducibly overexpressed in Madin-Darby canine kidney (MDCK) cells, in the absence of hypertonic stress before urea exposure. For this purpose, the human stress-inducible HSP72 gene was cloned downstream from a dexamethasone (DEX)-induc

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Xiao, Hong-bo, Rui-hong Liu, Guang-hui Ling та ін. "HSP47 regulates ECM accumulation in renal proximal tubular cells induced by TGF-β1 through ERK1/2 and JNK MAPK pathways". American Journal of Physiology-Renal Physiology 303, № 5 (2012): F757—F765. http://dx.doi.org/10.1152/ajprenal.00470.2011.

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Heat shock protein (HSP)47 is a collagen-specific molecular chaperone that is essential for the biosynthesis of collagen molecules. It is likely that increased levels of HSP47 contribute to the assembly of procollagen and thereby cause an excessive accumulation of collagens in disease processes associated with fibrosis. Although HSP47 promotes renal fibrosis, the underlying mechanism and associated signaling events have not been clearly delineated. We examined the role of HSP47 in renal fibrosis using a rat unilateral ureteral obstruction model and transforming growth factor (TGF)-β1-treated h

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Bigham, Michael T., and Hector R. Wong. "THE ROLE OF EXTRACELLULAR HSP72 IN CARDIOMYOCYTE ACTIVATION." Critical Care Medicine 34 (December 2006): A44. http://dx.doi.org/10.1097/00003246-200612002-00153.

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Kim, Sung O., Christopher P. Baines, Stuart D. Critz, et al. "Ischemia induced activation of heat shock protein 27 kinases and casein kinase 2 in the preconditioned rabbit heart." Biochemistry and Cell Biology 77, no. 6 (1999): 559–67. http://dx.doi.org/10.1139/o99-065.

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Protein kinase C (PKC), p38 MAP kinase, and mitogen-activated protein kinase-activated kinases 2 and 3 (MAPKAPK2 and MAPKAPK3) have been implicated in ischemic preconditioning (PC) of the heart to reduce damage following a myocardial infarct. This study examined whether extracellular signal-regulated kinase (Erk) 1, p70 ribosomal S6 kinase (p70 S6K), casein kinase 2 (CK2), and other hsp27 kinases are also activated by PC, and if they are required for protection in rabbit hearts. CK2 and hsp27 kinase activities declined during global ischemia in control hearts, whereas PC with 5 min ischemia an

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Sakamoto, Noriho, Daisuke Okuno, Takatomo Tokito, et al. "HSP47: A Therapeutic Target in Pulmonary Fibrosis." Biomedicines 11, no. 9 (2023): 2387. http://dx.doi.org/10.3390/biomedicines11092387.

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Idiopathic pulmonary fibrosis (IPF) is a chronic lung disease characterized by a progressive decline in lung function and poor prognosis. The deposition of the extracellular matrix (ECM) by myofibroblasts contributes to the stiffening of lung tissue and impaired oxygen exchange in IPF. Type I collagen is the major ECM component and predominant collagen protein deposited in chronic fibrosis, suggesting that type I collagen could be a target of drugs for fibrosis treatment. Heat shock protein 47 (HSP47), encoded by the serpin peptidase inhibitor clade H, member 1 gene, is a stress-inducible coll

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Bruchim, Yaron, Itamar Aroch, Ady Eliav, et al. "Two years of combined high-intensity physical training and heat acclimatization affect lymphocyte and serum HSP70 in purebred military working dogs." Journal of Applied Physiology 117, no. 2 (2014): 112–18. http://dx.doi.org/10.1152/japplphysiol.00090.2014.

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Military working dogs in hot countries undergo exercise training at high ambient temperatures for at least 9 mo annually. Physiological adaptations to these harsh conditions have been extensively studied; however, studies focusing on the underlying molecular adaptations are limited. In the current study, military working dogs were chosen as a model to examine the effects of superimposing endurance exercise on seasonal acclimatization to environmental heat stress. The lymphocyte HSP70 profile and extracellular HSP70 were studied in tandem with physiological performance in the dogs from their re

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Vallés, Gema, Eduardo García-Cimbrelo, and Nuria Vilaboa. "Involvement of extracellular Hsp72 in wear particle-mediated osteolysis." Acta Biomaterialia 8, no. 3 (2012): 1146–55. http://dx.doi.org/10.1016/j.actbio.2011.12.001.

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Salari, Samira, Tara Seibert, Yong-Xiang Chen та ін. "Extracellular HSP27 acts as a signaling molecule to activate NF-κB in macrophages". Cell Stress and Chaperones 18, № 1 (2012): 53–63. http://dx.doi.org/10.1007/s12192-012-0356-0.

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Archer, Ashley E., Alex T. Von Schulze, and Paige C. Geiger. "Exercise, heat shock proteins and insulin resistance." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1738 (2017): 20160529. http://dx.doi.org/10.1098/rstb.2016.0529.

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Best known as chaperones, heat shock proteins (HSPs) also have roles in cell signalling and regulation of metabolism. Rodent studies demonstrate that heat treatment, transgenic overexpression and pharmacological induction of HSP72 prevent high-fat diet-induced glucose intolerance and skeletal muscle insulin resistance. Overexpression of skeletal muscle HSP72 in mice has been shown to increase endurance running capacity nearly twofold and increase mitochondrial content by 50%. A positive correlation between HSP72 mRNA expression and mitochondrial enzyme activity has been observed in human skele

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Whitham, Martin, Gary J. Walker, and Nicolette C. Bishop. "Effect of caffeine supplementation on the extracellular heat shock protein 72 response to exercise." Journal of Applied Physiology 101, no. 4 (2006): 1222–27. http://dx.doi.org/10.1152/japplphysiol.00409.2006.

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The stimulus for the release of 72-kDa heat shock protein (HSP72) during exercise in humans is currently unclear. Recent evidence in an animal model is suggestive of an involvement of catecholamines. The present study, therefore, investigated the effect of caffeine supplementation, a known stimulator of sympathetic activity, on the extracellular (e)HSP72 response to prolonged exercise. Ten healthy male endurance-trained cyclists were recruited (age: 21 ± 1 yr, maximum O2 uptake 61.1 ± 1.7 ml·kg−1·min−1, mean ± SE). Each subject was randomly assigned to ingest either 6 mg/kg body mass of caffei

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Evdonin, Anton, Alexander Kinev, Natalia Tsupkina, Vince Guerriero, Deborah A. Raynes, and Natalia Medvedeva. "Extracellular HspBP1 and Hsp72 synergistically activate epidermal growth factor receptor." Biology of the Cell 101, no. 6 (2009): 351–60. http://dx.doi.org/10.1042/bc20080069.

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Jin, Chunhua, Joseph C. Cleveland, Lihua Ao, et al. "Human Myocardium Releases Heat Shock Protein 27 (HSP27) after Global Ischemia: The Proinflammatory Effect of Extracellular HSP27 through Toll-like Receptor (TLR)-2 and TLR4." Molecular Medicine 20, no. 1 (2014): 280–89. http://dx.doi.org/10.2119/molmed.2014.00058.

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Lunge, Ajitesh, Radhika Gupta, Eira Choudhary, and Nisheeth Agarwal. "The unfoldase ClpC1 of Mycobacterium tuberculosis regulates the expression of a distinct subset of proteins having intrinsically disordered termini." Journal of Biological Chemistry 295, no. 28 (2020): 9455–73. http://dx.doi.org/10.1074/jbc.ra120.013456.

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The human pathogen Mycobacterium tuberculosis (Mtb) harbors a well-orchestrated Clp (caseinolytic protease) proteolytic machinery consisting of two oligomeric segments, a barrel-shaped heterotetradecameric protease core comprising the ClpP1 and ClpP2 subunits, and hexameric ring-like ATP-dependent unfoldases composed of ClpX or ClpC1. The roles of the ClpP1P2 protease subunits are well-established in Mtb, but the potential roles of the associated unfoldases, such as ClpC1, remain elusive. Using a CRISPR interference–mediated gene silencing approach, here we demonstrate that clpC1 is indispensa

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Abell, Amy N., Jaime A. Rivera-Perez, Bruce D. Cuevas, et al. "Ablation of MEKK4 Kinase Activity Causes Neurulation and Skeletal Patterning Defects in the Mouse Embryo." Molecular and Cellular Biology 25, no. 20 (2005): 8948–59. http://dx.doi.org/10.1128/mcb.25.20.8948-8959.2005.

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ABSTRACT Skeletal disorders and neural tube closure defects represent clinically significant human malformations. The signaling networks regulating normal skeletal patterning and neurulation are largely unknown. Targeted mutation of the active site lysine of MEK kinase 4 (MEKK4) produces a kinase-inactive MEKK4 protein (MEKK4K1361R). Embryos homozygous for this mutation die at birth as a result of skeletal malformations and neural tube defects. Hindbrains of exencephalic MEKK4K1361R embryos show a striking increase in neuroepithelial cell apoptosis and a dramatic loss of phosphorylation of MKK

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Solly, Françoise, Pascale Flandrin-Gresta, Carmen Aanei, et al. "High Levels of Heat Shock Proteins 90 and 27 in CD34-Positive Cells from Myelodysplastic Syndromes (MDS) Are Associated with Higher Expression and Activation of Focal Adhesion Kinase (FAK) and with Disease Progression." Blood 114, no. 22 (2009): 289. http://dx.doi.org/10.1182/blood.v114.22.289.289.

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Abstract Abstract 289 MDS are characterized by a high risk of evolution into acute myeloid leukemia (AML). The pathogenesis of this evolution is still unclear. Some studies indicate that aberrant activation of survival signaling pathways is involved. The 90-kDa heat shock protein (HSP90) is implicated in the conformational maturation and stabilization of protein kinases and has key roles in signal transduction, protein folding, and protein degradation. HSP90 levels are increased in AML cells, and associated with resistance to chemotherapy induced apoptosis. Moreover, HSP90 is involved in the f

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Gabai, Vladimir L., Julia A. Yaglom, Vladimir Volloch, et al. "Hsp72-Mediated Suppression of c-Jun N-Terminal Kinase Is Implicated in Development of Tolerance to Caspase-Independent Cell Death." Molecular and Cellular Biology 20, no. 18 (2000): 6826–36. http://dx.doi.org/10.1128/mcb.20.18.6826-6836.2000.

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ABSTRACT Pretreatment with mild heat shock is known to protect cells from severe stress (acquired thermotolerance). Here we addressed the mechanism of this phenomenon by using primary human fibroblasts. Severe heat shock (45°C, 75 min) of the fibroblasts caused cell death displaying morphological characteristics of apoptosis; however, it was caspase independent. This cell death process was accompanied by strong activation of Akt, extracellular signal-regulated kinase 1 (ERK1) and ERK2, p38, and c-Jun N-terminal (JNK) kinases. Suppression of Akt or ERK1 and -2 kinases increased cell thermosensi

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Takamatsu, Hiroyuki, Zhirong Qi, Tomoyuki Sakurai, et al. "Identification of a Novel Auto-Antibody Highly Prevalent in Patients with Hepatitis-Associated and Idiopathic Aplastic Anemia." Blood 114, no. 22 (2009): 3200. http://dx.doi.org/10.1182/blood.v114.22.3200.3200.

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Abstract Abstract 3200 Poster Board III-137 Hepatitis-associated aplastic anemia (HAA) is a subset of acquired AA that is highly responsive to immunosuppressive therapy. The target antigens of the immune system attack in HAA are thought to be a protein shared by both liver and hematopoietic stem cells, since it is usually associated with severe hepatitis of unknown etiology. Screening sera from patients with HAA for the presence of antibodies (Abs) recognizing liver cell-derived proteins may be useful in identifying novel auto-antigens in AA. To test this hypothesis, sera from HAA patients wer

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Abboud, Patricia A., Patrick M. Lahni, Kristen Page, et al. "THE ROLE OF ENDOGENOUSLY PRODUCED EXTRACELLULAR HSP72 IN MONONUCLEAR CELL REPROGRAMMING." Shock 30, no. 3 (2008): 285–92. http://dx.doi.org/10.1097/shk.0b013e318164e2c3.

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Luo, Hongyang, Taixiang Liu, Huasheng Yang, Huijing Ye, and Xin Luo. "Expression of Collagen (Types I, III, and V), HSP47, MMP-2, and TIMP-1 in Retrobulbar Adipose Tissue of Patients with Thyroid-Associated Orbitopathy." Journal of Ophthalmology 2020 (April 23, 2020): 1–5. http://dx.doi.org/10.1155/2020/4929634.

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Objective. This study aimed to investigate the expression of collagen (types I, III, and V), heat shock protein 47 (HSP47), matrix metalloproteinase-2 (MMP-2), and tissue inhibitors of metalloproteinase-1 (TIMP-1) in the retrobulbar adipose tissues of patients with thyroid-associated orbitopathy (TAO). Materials and Methods. The retrobulbar adipose tissues were collected from 4 TAO patients undergoing orbital decompression and 4 ocular enucleation patients with atrophic eyeball caused by ocular trauma between May 2019 and September 2019. Masson staining was performed to analyze the differences

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Thienel, Manuela, Johannes B. Müller-Reif, Zhe Zhang, et al. "Immobility-associated thromboprotection is conserved across mammalian species from bear to human." Science 380, no. 6641 (2023): 178–87. http://dx.doi.org/10.1126/science.abo5044.

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Venous thromboembolism (VTE) comprising deep venous thrombosis and pulmonary embolism is a major cause of morbidity and mortality. Short-term immobility-related conditions are a major risk factor for the development of VTE. Paradoxically, long-term immobilized free-ranging hibernating brown bears and paralyzed spinal cord injury (SCI) patients are protected from VTE. We aimed to identify mechanisms of immobility-associated VTE protection in a cross-species approach. Mass spectrometry–based proteomics revealed an antithrombotic signature in platelets of hibernating brown bears with heat shock p

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