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Auteur : Grafiati
Publié le 11 mars 2023

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1

Hu, Yuanyu, Xueying Wang, Li Zeng, De-Yu Cai, Kanaga Sabapathy, Stephen P. Goff, Eduardo J. Firpo et Baojie Li. « ERK Phosphorylates p66shcA on Ser36 and Subsequently Regulates p27kip1 Expression via the Akt-FOXO3a Pathway : Implication of p27kip1 in Cell Response to Oxidative Stress ». Molecular Biology of the Cell 16, no 8 (août 2005) : 3705–18. http://dx.doi.org/10.1091/mbc.e05-04-0301.

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Mice deficient for p66shcA represent an animal model to link oxidative stress and aging. p66shcA is implicated in oxidative stress response and mitogenic signaling. Phosphorylation of p66shcA on Ser36 is critical for its function in oxidative stress response. Here we report the identification of ERK as the kinase phosphorylating p66shcA on Ser36. Activation of ERKs was necessary and sufficient for Ser36 phosphorylation. p66shcA interacted with ERK and was demonstrated to be a substrate for ERK, with Ser36 being the major phosphorylation site. Furthermore, in response to H2O2, inhibition of ERK activation repressed p66shcA-dependent phosphorylation of FOXO3a and the down-regulation of its target gene p27kip1. Down-regulation of p27 might promote cell survival, as p27 played a proapoptotic role in oxidative stress response. As a feedback regulation, Ser36 phosphorylated p66shcA attenuated H2O2-induced ERK activation, whereas p52/46shcA facilitated ERK activation, which required tyrosine phosphorylation of CH1 domain. p66shcA formed a complex with p52/46ShcA, which may provide a platform for efficient signal propagation. Taken together, the data suggest there exists an interplay between ERK and ShcA proteins, which modulates the expression of p27 and cell response to oxidative stress.
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Husain, Mohammad, Leonard G. Meggs, Himanshu Vashistha, Sonia Simoes, Kevin O. Griffiths, Dileep Kumar, Joanna Mikulak et al. « Inhibition of p66ShcA Longevity Gene Rescues Podocytes from HIV-1-induced Oxidative Stress and Apoptosis ». Journal of Biological Chemistry 284, no 24 (21 avril 2009) : 16648–58. http://dx.doi.org/10.1074/jbc.m109.008482.

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Glomerular visceral epithelial cells (podocytes) play a critical role in the pathogenesis of human immunodeficiency virus (HIV)-associated nephropathy. A key question concerns the mechanism(s) by which the HIV-1 genome alters the phenotype of the highly specialized, terminally differentiated podocytes. Here, using an in vitro system of conditionally immortalized differentiated human podocytes (CIDHPs), we document a pivotal role for the p66ShcA protein in HIV-1-induced reactive oxygen species generation and CIDHP apoptosis. CIDHP transfected with truncated HIV-1 construct (NL4-3) exhibit increased reactive oxygen species metabolism, DNA strand breaks, and a 5-fold increase in apoptosis, whereas the opposite was true for NL4-3/CIDHP co-transfected with mu-36p66ShcA (mu-36) dominant negative expression vector or isoform-specific p66-small interfering RNA. Phosphorylation at Ser-36 of the wild type p66ShcA protein, required for p66ShcA redox function and inhibition of the potent stress response regulator Foxo3a, was unchanged in mu-36/NL4-3/CIDHP but increased in NL4-3/CIDHP. Acute knockdown of Foxo3a by small interfering RNA induced a 50% increase in mu-36/NL4-3/CIDHP apoptosis, indicating that Foxo3a-dependent responses promote the survival phenotype in mu-36 cells. We conclude that inhibition of p66ShcA redox activity prevents generation of HIV-1 stress signals and activation of the CIDHP apoptosis program.
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Canedo, Eduardo Cepeda, Sonia Del Rincon, Peter Siegel, Michael Witcher et Josie Ursini-Siegel. « Abstract 131 : The role of p66ShcA in the melanoma oncogenesis process ». Cancer Research 82, no 12_Supplement (15 juin 2022) : 131. http://dx.doi.org/10.1158/1538-7445.am2022-131.

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Abstract Background: The identification of crucial driver mutations that affect the MAPK signaling pathway (BRAF, NRAS, NF1) in melanomas, has allowed for the development of targeted therapies and shed light on the process of melanocyte transformation. Gain of function mutations in proteins within the Ras/MAPK pathway in melanocytes leads to the formation of benign neoplasms, or nevi. Multiple mechanisms prevent the transformation of nevi into invasive cancer, namely, oncogene-induced senescence (OIS) and immunosurveillance. Of interest to the melanomagenesis process is the p66ShcA redox protein. We have found that compared to other solid cancers, the majority of primary human melanomas, patient-derived xenografts and melanoma cell lines strongly overexpress p66ShcA, an adaptor protein that induces production of reactive oxygen species (ROS) in response to stress stimuli. Indeed, UV light, increases p66ShcA levels and p66ShcA-induced oxidative stress, which is relevant to this disease as sun exposure contributes significantly to melanoma development. We hypothesized that p66ShcA may play a crucial role in the early steps of melanocyte transformation, possibly by contributing to the overriding of OIS and immune surveillance. Methods: Melanoma initiation and progression will be examined in a known transgenic mouse model (Tyr::CRE/brafCA/ptenlox/lox) either in the presence of endogenous levels of p66ShcA or in an inducible p66ShcA over-expression setting. The necessity of p66ShcA-high expression for melanocyte BRAFV600E-transformation will be tested in immortalized melanocytes. Lastly, to explore the potential selection advantage conferred by p66ShcA, its expression will be silenced in a panel of known melanoma cell lines. Clonogenic assays as well as mouse xenografts will be performed. Results: TCGA melanoma datasets, immunoblot analysis of human melanoma cell lines (n>10), and a collection of metastatic patient-derived xenografts (PDX) (n=6) indicate uniformly elevated p66ShcA levels compared to other cancer types. Knock-down of p66ShcA in multiple melanoma cell lines reduces their clonogenic potential. This reduction in colony formation is independent of driver mutation (e.g., BRAF, NRAS, NF1). Suggesting that p66ShcA may sustain melanoma proliferation. Furthermore, xenografts of the murine YUMM1.7 cell line (braf mutant, cdkn2a null and pten null) in immune-deficient and immune-competent mice indicate that loss of p66ShcA (YUMM1.7 p66ShcA-KO) delays tumor formation, specifically in mice with an intact immune system. Citation Format: Eduardo Cepeda Canedo, Sonia Del Rincon, Peter Siegel, Michael Witcher, Josie Ursini-Siegel. The role of p66ShcA in the melanoma oncogenesis process [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 131.
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Malhotra, Ashwani, Himanshu Vashistha, Virendra S. Yadav, Michael G. Dube, Satya P. Kalra, Maha Abdellatif et Leonard G. Meggs. « Inhibition of p66ShcA redox activity in cardiac muscle cells attenuates hyperglycemia-induced oxidative stress and apoptosis ». American Journal of Physiology-Heart and Circulatory Physiology 296, no 2 (février 2009) : H380—H388. http://dx.doi.org/10.1152/ajpheart.00225.2008.

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Apoptotic myocyte cell death, diastolic dysfunction, and progressive deterioration in left ventricular pump function characterize the clinical course of diabetic cardiomyopathy. A key question concerns the mechanism(s) by which hyperglycemia (HG) transmits danger signals in cardiac muscle cells. The growth factor adapter protein p66ShcA is a genetic determinant of longevity, which controls mitochondrial metabolism and cellular responses to oxidative stress. Here we demonstrate that interventions which attenuate or prevent HG-induced phosphorylation at critical position 36 Ser residue (phospho-Ser36) inhibit the redox function of p66ShcA and promote the survival phenotype. Adult rat ventricular myocytes obtained by enzymatic dissociation were transduced with mutant-36 p66ShcA (mu-36) dominant-negative expression vector and plated in serum-free media containing 5 or 25 mM glucose. At HG, adult rat ventricular myocytes exhibit a marked increase in reactive oxygen species production, upregulation of phospho-Ser36, collapse of mitochondrial transmembrane potential, and increased formation of p66ShcA/cytochrome- c complexes. These indexes of oxidative stress were accompanied by a 40% increase in apoptosis and the upregulation of cleaved caspase-3 and the apoptosis-related proteins p53 and Bax. To test whether p66ShcA functions as a redox-sensitive molecular switch in vivo, we examined the hearts of male Akita diabetic nonobese (C57BL/6J) mice. Western blot analysis detected the upregulation of phospho-Ser36, the translocation of p66ShcA to mitochondria, and the formation of p66ShcA/cytochrome- c complexes. Conversely, the correction of HG by recombinant adeno-associated viral delivery of leptin reversed these alterations. We conclude that p66ShcA is a molecular switch whose redox function is turned on by phospho-Ser36 and turned off by interventions that prevent this modification.
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Vashistha, H., L. Marrero, K. Reiss, A. J. Cohen, A. Malhotra, T. Javed, A. Bradley et al. « Aging phenotype(s) in kidneys of diabetic mice are p66ShcA dependent ». American Journal of Physiology-Renal Physiology 315, no 6 (1 décembre 2018) : F1833—F1842. http://dx.doi.org/10.1152/ajprenal.00608.2017.

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The p66ShcA protein controls cellular responses to oxidative stress, senescence, and apoptosis. Here, we test the hypothesis that aging phenotype(s) commonly associated with the broad category of chronic kidney disease are accelerated in diabetic kidneys and linked to the p66ShcA locus. At the organ level, tissue stem cells antagonize senescent phenotypes by replacing old dysfunctional cells. Using established methods, we isolated a highly purified population of stem cell antigen-1-positive mesenchymal stem cells (Sca-1+ MSCs) from kidneys of wild-type (WT) and p66 knockout (p66 KO) mice. Cells were plated in culture medium containing normal glucose (NG) or high glucose (HG). Reactive oxygen species (ROS) metabolism was substantially increased in WT MSCs in HG medium in association with increased cell death by apoptosis and acquisition of the senescent phenotype. DNA microarray analysis detected striking differences in the expression profiles of WT and p66 KO-MSCs in HG medium. Unexpectedly, the analysis for p66 KO-MSCs revealed upregulation of Wnt genes implicated in self-renewal and differentiation. To test the in vivo consequences of constitutive p66 expression in diabetic kidneys, we crossed the Akita diabetic mouse with the p66KO mouse. Homozygous mutation at the p66 locus delays or prevents aging phenotype(s) in the kidney that may be precursors to diabetic nephropathy.
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Miyazawa, Masaki, et Yoshiaki Tsuji. « Evidence for a novel antioxidant function and isoform-specific regulation of the human p66Shc gene ». Molecular Biology of the Cell 25, no 13 (juillet 2014) : 2116–27. http://dx.doi.org/10.1091/mbc.e13-11-0666.

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The mammalian Shc family, composed of p46, p52, and p66 isoforms, serves as an adaptor protein in cell growth and stress response. p66Shc was shown to be a negative lifespan regulator by acting as a prooxidant protein in mitochondria; however, the regulatory mechanisms of p66Shc expression and function are incompletely understood. This study provides evidence for new features of p66Shc serving as an antioxidant and critical protein in cell differentiation. Unique among the Shc family, transcription of p66Shc is activated through the antioxidant response element (ARE)–nuclear factor erythroid 2–related factor 2 (Nrf2) pathway in K562 human erythroleukemia and other cell types after treatment with hemin, an iron-containing porphyrin. Phosphorylated p66Shc at Ser-36, previously reported to be prone to mitochondrial localization, is increased by hemin treatment, but p66Shc remains exclusively in the cytoplasm. p66Shc knockdown inhibits hemin-induced erythroid differentiation, in which reactive oxygen species production and apoptosis are significantly enhanced in conjunction with suppression of other ARE-dependent antioxidant genes. Conversely, p66Shc overexpression is sufficient for inducing erythroid differentiation. Collectively these results demonstrate the isoform-specific regulation of the Shc gene by the Nrf2-ARE pathway and a new antioxidant role of p66Shc in the cytoplasm. Thus p66Shc is a bifunctional protein involved in cellular oxidative stress response and differentiation.
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Betts, Dean H., Nathan T. Bain et Pavneesh Madan. « The p66Shc Adaptor Protein Controls Oxidative Stress Response in Early Bovine Embryos ». PLoS ONE 9, no 1 (24 janvier 2014) : e86978. http://dx.doi.org/10.1371/journal.pone.0086978.

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Pacini, Sonia, Michela Pellegrini, Enrica Migliaccio, Laura Patrussi, Cristina Ulivieri, Andrea Ventura, Fabio Carraro et al. « p66SHC Promotes Apoptosis and Antagonizes Mitogenic Signaling in T Cells ». Molecular and Cellular Biology 24, no 4 (15 février 2004) : 1747–57. http://dx.doi.org/10.1128/mcb.24.4.1747-1757.2004.

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ABSTRACT Of the three Shc isoforms, p66Shc is responsible for fine-tuning p52/p46Shc signaling to Ras and has been implicated in apoptotic responses to oxidative stress. Here we show that human peripheral blood lymphocytes and mouse thymocytes and splenic T cells acquire the capacity to express p66Shc in response to apoptogenic stimulation. Using a panel of T-cell transfectants and p66Shc−/− T cells, we show that p66Shc expression results in increased susceptibility to apoptogenic stimuli, which depends on Ser36 phosphorylation and correlates with an altered balance in apoptosis-regulating gene expression. Furthermore, p66Shc blunts mitogenic responses to T-cell receptor engagement, at least in part by transdominant inhibition of p52Shc signaling to Ras/mitogen-activated protein kinases, in an S36-dependent manner. The data highlight a novel interplay between p66Shc and p52Shc in the control of T-cell fate.
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Migliaccio, Enrica, Marco Giorgio, Simonetta Mele, Giuliana Pelicci, Paolo Reboldi, Pier Paolo Pandolfi, Luisa Lanfrancone et Pier Giuseppe Pelicci. « The p66shc adaptor protein controls oxidative stress response and life span in mammals ». Nature 402, no 6759 (novembre 1999) : 309–13. http://dx.doi.org/10.1038/46311.

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Sun, Lin, Li Xiao, Jing Nie, Fu-you Liu, Guang-hui Ling, Xue-jing Zhu, Wen-bin Tang et al. « p66Shc mediates high-glucose and angiotensin II-induced oxidative stress renal tubular injury via mitochondrial-dependent apoptotic pathway ». American Journal of Physiology-Renal Physiology 299, no 5 (novembre 2010) : F1014—F1025. http://dx.doi.org/10.1152/ajprenal.00414.2010.

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p66Shc, a promoter of apoptosis, modulates oxidative stress response and cellular survival, but its role in the progression of diabetic nephropathy is relatively unknown. In this study, mechanisms by which p66Shc modulates high-glucose (HG)- or angiotensin (ANG) II-induced mitochondrial dysfunction were investigated in renal proximal tubular cells (HK-2 cells). Expression of p66Shc and its phosphorylated form (p-p66Shc, serine residue 36) and apoptosis were notably increased in renal tubules of diabetic mice, suggesting an increased reactive oxygen species production. In vitro, HG and ANG II led to an increased expression of total and p-p66Shc in HK-2 cells. These changes were accompanied with increased production of mitochondrial H2O2, reduced mitochondrial membrane potential, increased translocation of mitochondrial cytochrome c from mitochondria into cytosol, upregulation of the expression of caspase-9, and ultimately reduced cell survival. Overexpression of a dominant-negative Ser36 mutant p66Shc (p66ShcS36A) or treatment of p66Shc- or PKC-β-short interfering RNAs partially reversed these changes. Treatment of HK-2 cells with HG and ANG II also increased the protein-protein association between p-p66Shc and Pin1, an isomerase, in the cytosol, and with cytochrome c in the mitochondria. These interactions were partially disrupted with the treatment of PKC-β inhibitor or Pin1-short interfering RNA. These data suggest that p66Shc mediates HG- and ANG II-induced mitochondrial dysfunctions via PKC-β and Pin1-dependent pathways in renal tubular cells.
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Ren, Chaoxing, Xiaowei Zhou, Xiaowen Bao, Jie Zhang, Jun Tang, Zhiming Zhu, Nan Zhang et al. « Dioscorea zingiberensis ameliorates diabetic nephropathy by inhibiting NLRP3 inflammasome and curbing the expression of p66Shc in high-fat diet/streptozotocin-induced diabetic mice ». Journal of Pharmacy and Pharmacology 73, no 9 (1 juin 2021) : 1218–29. http://dx.doi.org/10.1093/jpp/rgab053.

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Abstract Objectives Diabetic nephropathy (DN) is a severe diabetic complication. Dioscorea zingiberensis (DZ) possesses excellent pharmacological properties with lower toxicity. The purpose of this study was to investigate the efficacy and mechanism of DZ in DN. Methods DN was established by the high-fat diet combining intraperitoneal injection of streptozotocin in mice. The DZ (125 and 250 mg/kg/day) were intragastrical administered for 8 consecutive weeks. After treatment, blood, urine and kidney tissue were collected for biological detection, renal morphology, fibrosis and molecular mechanism research, respectively. Key findings This study has shown that DZ significantly ameliorated kidney hypertrophy, renal structural damage and abnormal function of the kidney indicators (creatinine, urinary protein and blood urea nitrogen). Further molecular mechanism data suggested that the NLRP3/Cleaved-caspase-1 signal pathway was remarkably activated in DN, and DZ treatment reversed these changes, which indicated that it effectively attenuated inflammatory response caused by hyperglycaemia. In addition, DN inhibits hyperglycaemia-induced activation of oxidative stress by suppressing the expression of p66Shc proteins. Conclusions DZ could efficiently suppress oxidative stress and inflammatory responses to postpone the development of DN, and its mechanism might be related to inhibition of NLRP3 and p66Shc activities. Thus, DZ could be developed into a new therapeutic agent for DN.
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Chintapalli, Janaki, Shuo Yang, David Opawumi, Sunita Ray Goyal, Nazia Shamsuddin, Ashwani Malhotra, Krzysztof Reiss et Leonard G. Meggs. « Inhibition of wild-type p66ShcA in mesangial cells prevents glycooxidant-dependent FOXO3a regulation and promotes the survival phenotype ». American Journal of Physiology-Renal Physiology 292, no 2 (février 2007) : F523—F530. http://dx.doi.org/10.1152/ajprenal.00215.2006.

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Hyperglycemia triggers an exponential increase in reactive oxygen species (ROS) at the cellular level. Here, we demonstrate induction of the oxidant-resistant phenotype in mesangial cells by silencing the wild-type (WT) p66ShcA gene. Two approaches were employed to inhibit WTp66ShcA in SV40 murine mesangial cells and normal human mesangial cells: transient transfection with isoform-specific p66ShcA short-intervening RNA and stable transfection with mutant 36 p66ShcA expression vector. At high ambient glucose (HG), p66ShcA-deficient cells exhibit resistance to HG-induced ROS generation and attenuation in the amplitude of the kinetic curves for intracellular ROS metabolism, indicative of the pivotal role of WTp66ShcA in the generation of HG oxidant stress. We next examined phosphorylation and subcellular distribution of FKHRL1 (FOXO3a), a potent stress response regulator and downstream target of WTp66ShcA redox function. At HG, cell extracts of p66ShcA-deficient cells analyzed by immunoblotting show attenuation of FOXO3a phosphorylation at Thr-32, and indirect immunofluorescence of p66ShcA-deficient cells, cotransfected with HA-FOXO3a, show predominant HA-FOXO3a nuclear localization. Conversely, parental cells at HG show upregulation of phos-Thr-32 and nuclear export of HA-FOXO3a. To determine whether inhibition of cross talk between WTp66ShcA and FOXO3a confers protection against oxidant-induced DNA damage, DNA strand breaks (DSB) and apoptosis were examined. At HG, p66ShcA-deficient cells exhibit increased resistance to DSB and apoptosis, while parental cells show a striking increase in both parameters. We conclude that knockdown of WTp66ShcA redox function prevents HG-dependent FOXO3a regulation and promotes the survival phenotype.
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Salhan, Divya, Shresh Pathak, Mohammad Husain, Pranai Tandon, Dileep Kumar, Ashwani Malhotra, Leonard G. Meggs et Pravin C. Singhal. « HIV gene expression deactivates redox-sensitive stress response program in mouse tubular cells both in vitro and in vivo ». American Journal of Physiology-Renal Physiology 302, no 1 (1 janvier 2012) : F129—F140. http://dx.doi.org/10.1152/ajprenal.00024.2011.

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Human immunodeficiency virus (HIV)-1 has been reported to cause tubular cell injury both in in vivo and in vitro studies. In the present study, we evaluated the role of oxidative stress in the induction of apoptosis in HIV gene expressing mouse tubular cells in in vivo (Tg26, a transgenic mouse model of HIV-associated nephropathy) and in vitro (tubular cells were transduced with pNL4-3: ΔG/P-GFP, VSV.G psueudo typed virus) studies. Although Tg26 mice showed enhanced tubular cell reactive oxygen species (ROS) generation and apoptosis, renal tissue did not display a robust antioxidant response in the form of enhanced free radical scavenger (MnSOD/catalase) expression. Tg26 mice not only showed enhanced tubular cell expression of phospho-p66ShcA but also displayed nuclear Foxo3a translocation to the cytoplasm. These findings indicated deactivation of tubular cell Foxo3A-dependent redox-sensitive stress response program (RSSRP) in Tg26 mice. In in vitro studies, NL4-3 (pNL4-3: ΔG/P-GFP, VSV.G pseudotyped virus)-transduced mouse proximal tubular cells (NL4-3/MPTEC) displayed enhanced phosphorylation of p66ShcA. NL4-3/MPTECs also displayed greater ( P < 0.01) ROS generation when compared with empty vector-transduced tubular cells; however, both diminution of p66ShcA and N-acetyl cysteine attenuated NL4-3-induced tubular cell ROS generation as well as apoptosis. In addition, both antioxidants and free radical scavengers partially inhibited HIV-induced tubular cell apoptosis. NL4-3/MPTEC displayed deactivation of RSSRP in the form of enhanced phosphorylation of Foxo3A and attenuated expression of superoxide dismutase (SOD) and catalase. Since both SOD and catalase were able to provide protection against HIV-1-induced tubular cell apoptosis, it suggests that HIV-1-induced proapoptotic effect may be a consequence of the deactivated RSSRP.
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Di Stefano, Valeria, Chiara Cencioni, Germana Zaccagnini, Alessandra Magenta, Maurizio C. Capogrossi et Fabio Martelli. « p66ShcA modulates oxidative stress and survival of endothelial progenitor cells in response to high glucose ». Cardiovascular Research 82, no 3 (4 mars 2009) : 421–29. http://dx.doi.org/10.1093/cvr/cvp082.

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Rattanavich, Rungwasee, Andrei Plagov, Dileep Kumar, Partab Rai, Rivka Lederman, Divya Salhan, Himanshu Vashistha, Ashwani Malhotra, Leonard G. Meggs et Pravin C. Singhal. « Deficit of p66ShcA restores redox-sensitive stress response program in cisplatin-induced acute kidney injury ». Experimental and Molecular Pathology 94, no 3 (juin 2013) : 445–52. http://dx.doi.org/10.1016/j.yexmp.2013.03.001.

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Rai, Partab, Andrei Plagov, Xiqian Lan, Nirupama Chandel, Tejinder Singh, Rivka Lederman, Kamesh R. Ayasolla et al. « mTOR plays a critical role in p53-induced oxidative kidney cell injury in HIVAN ». American Journal of Physiology-Renal Physiology 305, no 3 (1 août 2013) : F343—F354. http://dx.doi.org/10.1152/ajprenal.00135.2013.

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Oxidative stress has been implicated to contribute to HIV-induced kidney cell injury; however, the role of p53, a modulator of oxidative stress, has not been evaluated in the development of HIV-associated nephropathy (HIVAN). We hypothesized that mammalian target of rapamycin (mTOR) may be critical for the induction of p53-mediated oxidative kidney cell injury in HIVAN. To test our hypothesis, we evaluated the effect of an mTOR inhibitor, rapamycin, on kidney cell p53 expression, downstream signaling, and kidney cell injury in both in vivo and in vitro studies. Inhibition of the mTOR pathway resulted in downregulation of renal tissue p53 expression, associated downstream signaling, and decreased number of sclerosed glomeruli, tubular microcysts, and apoptosed and 8-hydroxy deoxyguanosine (8-OHdG)-positive (+ve) cells in Tg26 mice. mTOR inhibition not only attenuated kidney cell expression of p66ShcA and phospho-p66ShcA but also reactivated the redox-sensitive stress response program in the form of enhanced expression of manganese superoxide dismutase (MnSOD) and catalase. In in vitro studies, the mTOR inhibitor also provided protection against HIV-induced podocyte apoptosis. Moreover, mTOR inhibition downregulated HIV-induced podocyte (HP/HIV) p53 expression. Since HP/HIV silenced for mTOR displayed a lack of expression of p53 as well as attenuated podocyte apoptosis, this suggests that mTOR is critical for kidney cell p53 activation and associated oxidative kidney cell injury in the HIV milieu.
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Yoshida, Hiderou. « ER stress response, peroxisome proliferation, mitochondrial unfolded protein response and Golgi stress response ». IUBMB Life 61, no 9 (septembre 2009) : 871–79. http://dx.doi.org/10.1002/iub.229.

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Flick, Karin, et Peter Kaiser. « Protein degradation and the stress response ». Seminars in Cell & ; Developmental Biology 23, no 5 (juillet 2012) : 515–22. http://dx.doi.org/10.1016/j.semcdb.2012.01.019.

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Little, Tom J., Lenny Nelson et Ted Hupp. « Adaptive Evolution of a Stress Response Protein ». PLoS ONE 2, no 10 (10 octobre 2007) : e1003. http://dx.doi.org/10.1371/journal.pone.0001003.

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Schröder, Martin, et Randal J. Kaufman. « ER stress and the unfolded protein response ». Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 569, no 1-2 (janvier 2005) : 29–63. http://dx.doi.org/10.1016/j.mrfmmm.2004.06.056.

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Dietrich, C. J., I. S. Richards, T. E. Bernard et Y. Y. Hammad. « Human stress protein response to formaldehyde exposure ». Experimental and Toxicologic Pathology 48, no 6 (novembre 1996) : 518–19. http://dx.doi.org/10.1016/s0940-2993(96)80071-6.

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Sheppard, Terry L. « Unfolded protein response : Letting go of stress ». Nature Chemical Biology 10, no 11 (17 octobre 2014) : 877. http://dx.doi.org/10.1038/nchembio.1676.

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Solé, M., Y. Morcillo et C. Porte. « Stress–Protein Response in Tributyltin-Exposed Clams ». Bulletin of Environmental Contamination and Toxicology 64, no 6 (30 juin 2000) : 852–58. http://dx.doi.org/10.1007/s001280000081.

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Solé, M., Y. Morcillo et C. Porte. « Stress–Protein Response in Tributyltin-Exposed Clams ». Bulletin of Environmental Contamination and Toxicology 64, no 6 (juin 2000) : 852–58. http://dx.doi.org/10.1007/s0012800081.

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Zhang, Guangyu, Xiaoding Wang, Chao Li, Qinfeng Li, Yu A. An, Xiang Luo, Yingfeng Deng, Thomas G. Gillette, Philipp E. Scherer et Zhao V. Wang. « Integrated Stress Response Couples Mitochondrial Protein Translation With Oxidative Stress Control ». Circulation 144, no 18 (2 novembre 2021) : 1500–1515. http://dx.doi.org/10.1161/circulationaha.120.053125.

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Background: The integrated stress response (ISR) is an evolutionarily conserved process to cope with intracellular and extracellular disturbances. Myocardial infarction is a leading cause of death worldwide. Coronary artery reperfusion, the most effective means to mitigate cardiac damage of myocardial infarction, causes additional reperfusion injury. This study aimed to investigate the role of the ISR in myocardial ischemia/reperfusion (I/R). Methods: Cardiac-specific gain- and loss-of-function approaches for the ISR were used in vivo. Myocardial I/R was achieved by ligation of the cardiac left anterior descending artery for 45 minutes followed by reperfusion for different times. Cardiac function was assessed by echocardiography. Cultured H9c2 cells, primary rat cardiomyocytes, and mouse embryonic fibroblasts were used to dissect underlying molecular mechanisms. Tandem mass tag labeling and mass spectrometry was conducted to identify protein targets of the ISR. Pharmacologic means were tested to manipulate the ISR for therapeutic exploration. Results: We show that the PERK (PKR-like endoplasmic reticulum resident kinase)/eIF2α (α subunit of eukaryotic initiation factor 2) axis of the ISR is strongly induced by I/R in cardiomyocytes in vitro and in vivo. We further reveal a physiologic role of PERK/eIF2α signaling by showing that acute activation of PERK in the heart confers robust cardioprotection against reperfusion injury. In contrast, cardiac-specific deletion of PERK aggravates cardiac responses to reperfusion. Mechanistically, the ISR directly targets mitochondrial complexes through translational suppression. We identify NDUFAF2 (NADH:ubiquinone oxidoreductase complex assembly factor 2), an assembly factor of mitochondrial complex I, as a selective target of PERK. Overexpression of PERK suppresses the protein expression of NDUFAF2 and PERK inhibition causes an increase of NDUFAF2. Silencing of NDUFAF2 significantly rescues cardiac cell survival from PERK knockdown under I/R. We show that activation of PERK/eIF2α signaling reduces mitochondrial complex–derived reactive oxygen species and improves cardiac cell survival in response to I/R. Moreover, pharmacologic stimulation of the ISR protects the heart against reperfusion damage, even after the restoration of occluded coronary artery, highlighting clinical relevance for myocardial infarction treatment. Conclusions: These results suggest that the ISR improves cell survival and mitigates reperfusion damage by selectively suppressing mitochondrial protein synthesis and reducing oxidative stress in the heart.
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Gower, David J., Carol Hollman, K. Stuart Lee et Michael Tytell. « Spinal cord injury and the stress protein response ». Journal of Neurosurgery 70, no 4 (avril 1989) : 605–11. http://dx.doi.org/10.3171/jns.1989.70.4.0605.

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✓ The heat shock or stress response is a highly conserved primary cellular response to injury. Synthesis of stress proteins (also called “heat shock proteins”) is an integral component of this response. Protection from various forms of sublethal stress following increased production of stress proteins has been demonstrated in a number of systems, including the retina. This immunocytochemical study demonstrates the synthesis, accumulation, and redistribution of the 70-kD stress protein following spinal cord injury in rats. The observations confirm that stress protein production is a fundamental feature of the molecular response of the spinal cord to injury, and raise the possibility that augmentation of this response could enhance posttraumatic neuronal survival.
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Moore, J., R. Flynn, R. C. Dwyer et E. Duly. « Stress protein response and analgesic treatment during labour ». Journal of Obstetrics and Gynaecology 11, no 6 (janvier 1991) : 414–16. http://dx.doi.org/10.3109/01443619109013580.

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Götz, Claudia, et Mathias Montenarh. « Protein kinase CK2 in the ER stress response ». Advances in Biological Chemistry 03, no 03 (2013) : 1–5. http://dx.doi.org/10.4236/abc.2013.33a001.

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Lai, Elida, Tracy Teodoro et Allen Volchuk. « Endoplasmic Reticulum Stress : Signaling the Unfolded Protein Response ». Physiology 22, no 3 (juin 2007) : 193–201. http://dx.doi.org/10.1152/physiol.00050.2006.

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The endoplasmic reticulum (ER) is the cellular site of newly synthesized secretory and membrane proteins. Such proteins must be properly folded and posttranslationally modified before exit from the organelle. Proper protein folding and modification requires molecular chaperone proteins as well as an ER environment conducive for these reactions. When ER lumenal conditions are altered or chaperone capacity is overwhelmed, the cell activates signaling cascades that attempt to deal with the altered conditions and restore a favorable folding environment. Such alterations are referred to as ER stress, and the response activated is the unfolded protein response (UPR). When the UPR is perturbed or not sufficient to deal with the stress conditions, apoptotic cell death is initiated. This review will examine UPR signaling that results in cell protective responses, as well as the mechanisms leading to apoptosis induction, which can lead to pathological states due to chronic ER stress.
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Shao, Chunhong, Qunye Zhang, Yundong Sun, Zhifang Liu, Jiping Zeng, Yabin Zhou, Xiuping Yu et Jihui Jia. « Helicobacter pylori protein response to human bile stress ». Journal of Medical Microbiology 57, no 2 (1 février 2008) : 151–58. http://dx.doi.org/10.1099/jmm.0.47616-0.

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The ability of Helicobacter pylori to tolerate bile is likely to be important for its colonization and survival in the gastrointestinal tract of humans. As bile can be acidified after reflux into the low pH of the human stomach, the inhibitory effect of fresh human bile with normal appearance on H. pylori before and after acidification was tested first. The results showed that acidification of bile attenuated its inhibitory activity towards H. pylori. Next, the protein profiles of H. pylori under human bile and acidified bile stress were obtained by two-dimensional electrophoresis. Protein spots with differential expression were identified using tandem matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The results showed that the changes in proteomic profiles under bile and acidified bile stress were similar when compared with that of normal H. pylori. Expression of 28 proteins was found to be modulated, with the majority being induced during bile or acidified bile exposure. These proteins included molecular chaperones, proteins involved in iron storage, chemotaxis protein, enzymes related to energy metabolism and flagellar protein. These results indicate that H. pylori responds to bile and acidified bile stress through multiple mechanisms involving many signalling pathways.
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Ofenstein, John P., Sabrina M. Heidemann, Amy M. Juett et Ashok P. Sarnaik. « ENDOTOXEMIA INDUCES THE STRESS RESPONSE PROTEIN HSP70. † 210 ». Pediatric Research 41 (avril 1997) : 37. http://dx.doi.org/10.1203/00006450-199704001-00230.

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Kapoor, Ashwani, et Arun J. Sanyal. « Endoplasmic Reticulum Stress and the Unfolded Protein Response ». Clinics in Liver Disease 13, no 4 (novembre 2009) : 581–90. http://dx.doi.org/10.1016/j.cld.2009.07.004.

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Thede, G. L., D. C. Arthur, R. A. Edwards, D. R. Buelow, J. L. Wong, T. L. Raivio et J. N. M. Glover. « Structure of the Periplasmic Stress Response Protein CpxP ». Journal of Bacteriology 193, no 9 (11 février 2011) : 2149–57. http://dx.doi.org/10.1128/jb.01296-10.

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Abbondanzieri, Elio A., Natalia Vtyurina et Anne Meyer. « Nucleoid Reorganization by the Stress Response Protein Dps ». Biophysical Journal 106, no 2 (janvier 2014) : 79a. http://dx.doi.org/10.1016/j.bpj.2013.11.511.

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Uckelmann, Hannah, Sandra Blaszkiewicz et Marieke Essers. « Extracellular matrix protein Matn4 regulates HSC stress response ». Experimental Hematology 43, no 9 (septembre 2015) : S45. http://dx.doi.org/10.1016/j.exphem.2015.06.051.

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Wong, H. R., et J. R. Wispe. « The stress response and the lung ». American Journal of Physiology-Lung Cellular and Molecular Physiology 273, no 1 (1 juillet 1997) : L1—L9. http://dx.doi.org/10.1152/ajplung.1997.273.1.l1.

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The stress response is a highly conserved cellular defense mechanism defined by the rapid and specific expression of stress proteins, with concomitant transient inhibition of nonstress protein gene expression. The stress proteins mediate cellular and tissue protection against diverse cytotoxic stimuli. Among the many classes of stress proteins, heat shock protein 70 and heme oxygenase-1 are the best characterized with respect to lung biology. A potential role for stress proteins in human lung disease is inferred from studies demonstrating stress protein expression in the lungs of patients with cancer, asthma, and acute lung injury. Several examples of stress protein-mediated cytoprotection exist in cell and animal models of acute lung injury. Stress protein induction protects rats against acute lung injury caused by either systemic administration of endotoxin or intratracheal administration of phospholipase A1. In vitro, increased expression of stress proteins protects lung cells against endotoxin-mediated apoptosis and oxidant injury. The mechanisms of stress response-mediated cytoprotection may involve the enzymatic and molecular chaperone properties of stress proteins. Alternatively, the stress response may protect by modulating lung proinflammatory responses. Data from extrapulmonary systems suggest that stress response-associated factors (heat shock protein 70 and heat shock factor) are directly involved in modulation of proinflammatory gene expression. Recent evidence also demonstrates interactions between the stress response and the I-kappa B/nuclear factor-kappa B pathway in cultured lung cells. Increased understanding about the role of stress proteins in lung biology may support efforts to selectively increase expression of one or more stress proteins to provide protection against human acute lung injury.
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Jiang, Mengxi, Susan M. Sullivan, Patrice K. Wout et Janine R. Maddock. « G-Protein Control of the Ribosome-Associated Stress Response Protein SpoT ». Journal of Bacteriology 189, no 17 (6 juillet 2007) : 6140–47. http://dx.doi.org/10.1128/jb.00315-07.

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ABSTRACT The bacterial response to stress is controlled by two proteins, RelA and SpoT. RelA generates the alarmone (p)ppGpp under amino acid starvation, whereas SpoT is responsible for (p)ppGpp hydrolysis and for synthesis of (p)ppGpp under a variety of cellular stress conditions. It is widely accepted that RelA is associated with translating ribosomes. The cellular location of SpoT, however, has been controversial. SpoT physically interacts with the ribosome-associated GTPase CgtA, and we show here that, under an optimized salt condition, SpoT is also associated with a pre-50S particle. Analysis of spoT and cgtA mutants and strains overexpressing CgtA suggests that the ribosome associations of SpoT and CgtA are mutually independent. The steady-state level of (p)ppGpp is increased in a cgtA mutant, but the accumulation of (p)ppGpp during amino acid starvation is not affected, providing strong evidence that CgtA regulates the (p)ppGpp level during exponential growth but not during the stringent response. We show that CgtA is not associated with pre-50S particles during amino acid starvation, indicating that under these conditions in which (p)ppGpp accumulates, CgtA is not bound either to the pre-50S particle or to SpoT. We propose that, in addition to its role as a 50S assembly factor, CgtA promotes SpoT (p)ppGpp degradation activity on the ribosome and that the loss of CgtA from the ribosome is necessary for maximal (p)ppGpp accumulation under stress conditions. Intriguingly, we found that in the absence of spoT and relA, cgtA is still an essential gene in Escherichia coli.
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Johnston, Benjamin P., et Craig McCormick. « Herpesviruses and the Unfolded Protein Response ». Viruses 12, no 1 (21 décembre 2019) : 17. http://dx.doi.org/10.3390/v12010017.

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Herpesviruses usurp cellular stress responses to promote viral replication and avoid immune surveillance. The unfolded protein response (UPR) is a conserved stress response that is activated when the protein load in the ER exceeds folding capacity and misfolded proteins accumulate. The UPR aims to restore protein homeostasis through translational and transcriptional reprogramming; if homeostasis cannot be restored, the UPR switches from “helper” to “executioner”, triggering apoptosis. It is thought that the burst of herpesvirus glycoprotein synthesis during lytic replication causes ER stress, and that these viruses may have evolved mechanisms to manage UPR signaling to create an optimal niche for replication. The past decade has seen considerable progress in understanding how herpesviruses reprogram the UPR. Here we provide an overview of the molecular events of UPR activation, signaling and transcriptional outputs, and highlight key evidence that herpesviruses hijack the UPR to aid infection.
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Adachi, Masaaki, Yaohua Liu, Kyoko Fujii, Stuart K. Calderwood, Akira Nakai, Kohzoh Imai et Yasuhisa Shinomura. « Oxidative Stress Impairs the Heat Stress Response and Delays Unfolded Protein Recovery ». PLoS ONE 4, no 11 (11 novembre 2009) : e7719. http://dx.doi.org/10.1371/journal.pone.0007719.

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Hetz, Claudio, Fabio Martinon, Diego Rodriguez et Laurie H. Glimcher. « The Unfolded Protein Response : Integrating Stress Signals Through the Stress Sensor IRE1α ». Physiological Reviews 91, no 4 (octobre 2011) : 1219–43. http://dx.doi.org/10.1152/physrev.00001.2011.

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Stress induced by accumulation of unfolded proteins at the endoplasmic reticulum (ER) is a classic feature of secretory cells and is observed in many tissues in human diseases including cancer, diabetes, obesity, and neurodegeneration. Cellular adaptation to ER stress is achieved by the activation of the unfolded protein response (UPR), an integrated signal transduction pathway that transmits information about the protein folding status at the ER to the nucleus and cytosol to restore ER homeostasis. Inositol-requiring transmembrane kinase/endonuclease-1 (IRE1α), the most conserved UPR stress sensor, functions as an endoribonuclease that processes the mRNA of the transcription factor X-box binding protein-1 (XBP1). IRE1α signaling is a highly regulated process, controlled by the formation of a dynamic scaffold onto which many regulatory components assemble, here referred to as the UPRosome. Here we provide an overview of the signaling and regulatory mechanisms underlying IRE1α function and discuss the emerging role of the UPR in adaptation to protein folding stress in specialized secretory cells and in pathological conditions associated with alterations in ER homeostasis.
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Lee, Jaemin, et Umut Ozcan. « Unfolded Protein Response Signaling and Metabolic Diseases ». Journal of Biological Chemistry 289, no 3 (9 décembre 2013) : 1203–11. http://dx.doi.org/10.1074/jbc.r113.534743.

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The endoplasmic reticulum (ER) is a central organelle for protein biosynthesis, folding, and traffic. Perturbations in ER homeostasis create a condition termed ER stress and lead to activation of the complex signaling cascade called the unfolded protein response (UPR). Recent studies have documented that the UPR coordinates multiple signaling pathways and controls various physiologies in cells and the whole organism. Furthermore, unresolved ER stress has been implicated in a variety of metabolic disorders, such as obesity and type 2 diabetes. Therefore, intervening in ER stress and modulating signaling components of the UPR would provide promising therapeutics for the treatment of human metabolic diseases.
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Rzymski, Tomasz, et Adrian L. Harris. « The Unfolded Protein Response and Integrated Stress Response to Anoxia : Fig. 1. » Clinical Cancer Research 13, no 9 (1 mai 2007) : 2537–40. http://dx.doi.org/10.1158/1078-0432.ccr-06-2126.

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Wang, Yijie, et Jose Ramón Botella. « Heterotrimeric G Protein Signaling in Abiotic Stress ». Plants 11, no 7 (25 mars 2022) : 876. http://dx.doi.org/10.3390/plants11070876.

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As sessile organisms, plants exhibit extraordinary plasticity and have evolved sophisticated mechanisms to adapt and mitigate the adverse effects of environmental fluctuations. Heterotrimeric G proteins (G proteins), composed of α, β, and γ subunits, are universal signaling molecules mediating the response to a myriad of internal and external signals. Numerous studies have identified G proteins as essential components of the organismal response to stress, leading to adaptation and ultimately survival in plants and animal systems. In plants, G proteins control multiple signaling pathways regulating the response to drought, salt, cold, and heat stresses. G proteins signal through two functional modules, the Gα subunit and the Gβγ dimer, each of which can start either independent or interdependent signaling pathways. Improving the understanding of the role of G proteins in stress reactions can lead to the development of more resilient crops through traditional breeding or biotechnological methods, ensuring global food security. In this review, we summarize and discuss the current knowledge on the roles of the different G protein subunits in response to abiotic stress and suggest future directions for research.
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Xu, Delin, Bo Yu, Yan Zhang, Miao Cui et Qizhong Zhang. « Metallothionein Protein Expression ofCrassostrea hongkongensisin Response to Cadmium Stress ». Journal of Shellfish Research 34, no 2 (août 2015) : 311–18. http://dx.doi.org/10.2983/035.034.0213.

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Smirnova, E. V., T. V. Rakitina, O. V. Bogatova, D. L. Ivanova, E. E. Vorobyeva, A. V. Lipkin, I. A. Kostanyan et V. M. Lipkin. « Novel protein haponin regulates cellular response to oxidative stress ». Doklady Biochemistry and Biophysics 440, no 1 (octobre 2011) : 225–27. http://dx.doi.org/10.1134/s1607672911050097.

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Oosthuizen, I. B., H. A. Snyman et J. C. Pretorius. « Protein concentration in response to water stress inThemeda triandraForsk ». South African Journal of Plant and Soil 23, no 1 (janvier 2006) : 43–48. http://dx.doi.org/10.1080/02571862.2006.10634728.

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Roy, Anirban, et Ashok Kumar. « ER Stress and Unfolded Protein Response in Cancer Cachexia ». Cancers 11, no 12 (3 décembre 2019) : 1929. http://dx.doi.org/10.3390/cancers11121929.

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Cancer cachexia is a devastating syndrome characterized by unintentional weight loss attributed to extensive skeletal muscle wasting. The pathogenesis of cachexia is multifactorial because of complex interactions of tumor and host factors. The irreversible wasting syndrome has been ascribed to systemic inflammation, insulin resistance, dysfunctional mitochondria, oxidative stress, and heightened activation of ubiquitin-proteasome system and macroautophagy. Accumulating evidence suggests that deviant regulation of an array of signaling pathways engenders cancer cachexia where the human body is sustained in an incessant self-consuming catabolic state. Recent studies have further suggested that several components of endoplasmic reticulum (ER) stress-induced unfolded protein response (UPR) are activated in skeletal muscle of animal models and muscle biopsies of cachectic cancer patients. However, the exact role of ER stress and the individual arms of the UPR in the regulation of skeletal muscle mass in various catabolic states including cancer has just begun to be elucidated. This review provides a succinct overview of emerging roles of ER stress and the UPR in cancer-induced skeletal muscle wasting.
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Gardner, B. M., D. Pincus, K. Gotthardt, C. M. Gallagher et P. Walter. « Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response ». Cold Spring Harbor Perspectives in Biology 5, no 3 (6 février 2013) : a013169. http://dx.doi.org/10.1101/cshperspect.a013169.

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Balodimos, I. A., E. Rapaport et E. R. Kashket. « Protein phosphorylation in response to stress in Clostridium acetobutylicum. » Applied and Environmental Microbiology 56, no 7 (1990) : 2170–73. http://dx.doi.org/10.1128/aem.56.7.2170-2173.1990.

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Hetz, Claudio, et Smita Saxena. « ER stress and the unfolded protein response in neurodegeneration ». Nature Reviews Neurology 13, no 8 (21 juillet 2017) : 477–91. http://dx.doi.org/10.1038/nrneurol.2017.99.

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