![]() Antioxid Redox Signal 9:2305–2321īaindur-Hudson S, Edkins AL, Blatch GL (2015) Hsp70/Hsp90 organising protein (hop): beyond interactions with chaperones and prion proteins. ![]() Am J Physiol Heart Circ Physiol 291:H1411–H1420īailey D, O’Hare P (2007) Transmembrane bZIP transcription factors in ER stress signaling and the unfolded protein response. Biol Trace Elem Res 149:123–132Īzfer A, Niu J, Rogers LM, Adamski FM, Kolattukudy PE (2006) Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. J Biochem 149:507–518Īueviriyavit S, Phummiratch D, Kulthong K, Maniratanachote R (2012) Titanium dioxide nanoparticles-mediated in vitro cytotoxicity does not induce Hsp70 and Grp78 expression in human bronchial epithelial A549 cells. Mol Boil cell 16:5891–5900Īsada R, Kanemoto S, Kondo S, Saito A, Imaizumi K (2011) The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology. Nat Med 5:745–751Īrndt V, Daniel C, Nastainczyk W, Alberti S, Höhfeld J (2005) BAG-2 Acts as an Inhibitor of the Chaperone-associated Ubiquitin Ligase CHIP. Semin Cell Dev Bio 10:495–505Īridor M, Balch WE (1999) Integration of endoplasmic reticulum signaling in health and disease. Immunol Rev 222:155–161Īrgon Y, Simen BB (1999) GRP94, an ER chaperone with protein and peptide binding properties. Neurochem Res 34:453–462Īllavena P, Sica A, Garlanda C, Mantovani A (2008) The Yin-Yang of tumor-associated macrophages in neoplastic progression and immune surveillance. Cell Stress Chaperones 8:225–231Īllagui MS, Nciri R, Rouhaud MF, Murat JC, El Feki A, Croute F, Vincent C (2009) Long-term exposure to low lithium concentrations stimulates proliferation, modifies stress protein expression pattern and enhances resistance to oxidative stress in SH-SY5Y cells. J Cell Sci 116:3557–3570Īlberti S, Esser C, Höhfeld J (2003) BAG-1–a nucleotide exchange factor of Hsc70 with multiple cellular functions. KeywordsĪlastalo TP, Hellesuo M, Sandqvist A, Hietakangas V, Kallio M, Sistonen L (2003) Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70. In the present chapter, we have summarized the advances made in the manifold roles of HSP that govern ER stress signaling in health. ![]() The HSP in ER stress have been implicated in diverse pathophysiological conditions like cardiovascular diseases, cancer, aging, diabetes and obesity. In addition, the HSP are also responsible for the ER associated degradation of unfolded proteins when ER stress persists for a long time. In recent years, studies have revealed the roles of HSP in sensing the ER stress and activating the three axes of UPR. A diverse group of heat shock proteins (HSP) has been implicated in this ER stress response. An evolutionarily conserved signal transduction mechanism called unfolded protein response (UPR) recuperates the ER function and proteostasis in the ER. ER stress accumulates and aggregates unfolded proteins within the ER lumen. When this dynamic equilibrium gets imbalanced due to perturbations in the ER functions, a condition termed ER stress occurs. The efficient functions of the ER regulate the cellular processes and maintain cell homeostasis. The endoplasmic reticulum (ER) is a dynamic as well as an intricate organelle that carries out diverse essential functions within the cell.
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