Ablation of the gene encoding p66Shc protects mice against AGE-induced glomerulopathy by preventing oxidant-dependent tissue injury and further AGE accumulation

Menini, S.; Iacobini, C.; Ricci, C.; Oddi, G.; Pesce, C.; Pugliese, F.; Block, K.; Abboud, H. E.; Giorgio, M.; Migliaccio, E.; Pelicci, P. G.; Pugliese, G.

doi:10.1007/s00125-007-0728-7

Cited by 64Advanced Glycation End Products researchChronic Kidney Disease and DiabetesAcute Kidney Injury Research

Ablation of the gene encoding p66Shc protects mice against AGE-induced glomerulopathy by preventing oxidant-dependent tissue injury and further AGE accumulation

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Menini, S., Iacobini, C., Ricci, C., Oddi, G., Pesce, C., Pugliese, F., Block, K., Abboud, H. E. +4 more·2007·Diabetologia

DOI 10.1007/s00125-007-0728-7

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Abstract

Aims/hypothesis AGEs have been implicated in renal disease associated with ageing, diabetes and other age-related disorders. Reactive oxygen species (ROS) promote formation of AGEs, which cause AGE-receptor-mediated ROS generation with activation of signalling pathways leading to tissue injury and further AGE accumulation. ROS generation is regulated by the Src homology 2 domain-containing transforming protein C1 (Shc1) isoform p66(Shc), whose deletion has been shown to protect from tissue injury induced by ageing, diabetes, hyperlipidaemia and ischaemia-reperfusion by preventing oxidative stress. This study was aimed at assessing the role of p66(Shc) in the modulation of oxidative stress and oxidant-dependent renal injury induced by AGEs.Methods For 10 weeks, male p66 (shc) knockout (KO) and wild-type (WT) mice were injected with 60 microg/day albumin modified or unmodified by N epsilon-(carboxymethyl) lysine (CML). Mice were then killed for the assessment of renal function and structure, as well as systemic and renal tissue oxidative stress.Results Upon CML injection, KO mice, in contrast to WT mice, showed no or only mild forms of proteinuria, glomerular hypertrophy, mesangial expansion, glomerular sclerosis, renal/glomerular cell apoptosis and extracellular matrix upregulation. Moreover, KO mice had lower circulating and tissue AGEs than WT mice and unchanged plasma isoprostane 8-epi-prostaglandin-F(2alpha) levels, renal/glomerular CML, 4-hydroxy-2-nonenal, AGE receptor and NAD(P)H oxidase 4 (NOX4) content (and expression of the corresponding genes), and nuclear factor kappaB activation (NFkappaB). Mesangial cells from KO mice exposed to CML showed no or slight increase in ROS levels and NFkappaB activation, again at variance with WT cells.Conclusions/interpretation These data indicate that p66(Shc) participates in the pathogenesis of AGE-dependent glomerulopathy by mediating AGE-induced tissue injury and further AGE formation through ROS-dependent mechanisms involving NFkappaB activation and upregulation of Nox4 expression and NOX4 production.

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p66SHC−/− tissues show reduced oxidative damage to DNA, lipids, carbohydrates, and proteins.
“Accordingly, p66SHC−/− tissues showed a reduced level of oxidative damage to nuclear and mitochondrial DNA (Trinei et al., 2002), lipids (Napoli et al., 2003), carbohydrates (Menini et al., 2007), and proteins (Carpi et al., 2009)”
From P66SHC deletion improves fertility and progeric phenotype of late-generation TERC-deficient mice but not their short lifespan (2016) · cites this paper as Menini et al., 2007
p66SHC null mice are protected from aging-associated diseases.
“P66SHC null mice (p66SHC−/−) develop normally and resulted to be protected from aging‐associated diseases, such as atherosclerosis (Martin‐Padura et al., 2008), diabetes compliances (Menini et al., 2007), onset (Tomilov et al., 2011), cognitive decline (Berry et al., 2007), and neurodegeneration (Savino et al., 2013).”
From P66SHC deletion improves fertility and progeric phenotype of late-generation TERC-deficient mice but not their short lifespan (2016) · cites this paper as Menini et al., 2007

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Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
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Baynes, J. W., & Thorpe, S. R. (1999) · Diabetes · doi:10.2337/diabetes.48.1.1 · Cited by 2,441 · see citing works
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Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712 · see citing works
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Chen, J., Muntner, P., Hamm, L. L., Jones, D. W., Batuman, V., Fonseca, V. A., Whelton, P. K., & He, J. (2004) · Annals of Internal Medicine · doi:10.7326/0003-4819-140-3-200402030-00007 · Cited by 1,354 · see citing works
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Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y., Pinsky, D. J., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36966-1 · Cited by 1,305 · see citing works
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Giorgio, M., Migliaccio, E., Orsini, F., Paolucci, D., Moroni, M., Contursi, C., Pelliccia, G., Luzi, L., Minucci, S., Marcaccio, M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.011 · Cited by 1,176 · see citing works
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Lander, H. M., Tauras, J. M., Ogiste, J. S., Hori, O., Moss, R. A., & Schmidt, A. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17810 · Cited by 813 · see citing works
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Schleicher, E. D., Wagner, E., & Nerlich, A. G. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119180 · Cited by 714 · see citing works
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Advanced glycation end products induce glomerular sclerosis and albuminuria in normal rats.
Vlassara, H., Striker, L. J., Teichberg, S., Fuh, H., Li, Y. M., & Steffes, M. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.24.11704 · Cited by 461 · see citing works
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Self-citation
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Wu, L., & Juurlink, B. H. J. (2002) · Hypertension · doi:10.1161/hy0302.105207 · Cited by 229 · see citing works
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Basta, G., Lazzerini, G., Turco, S. D., Ratto, G. M., Schmidt, A. M., & Caterina, R. D. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000167522.48370.5e · Cited by 212 · see citing works
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Sell, D. R., Nagaraj, R. H., Grandhee, S. K., Odetti, P. R., Lapolla, A., Fogarty, J. F., & Monnier, V. M. (1991) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610070404 · Cited by 187 · see citing works
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Self-citation
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Li, Y. M., Steffes, M. W., Donnelly, T. M., Liu, C., Fuh, H., Basgen, J. M., Bucala, R., & Vlassara, H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.3902 · Cited by 178 · see citing works
Oxidative Stress and Antioxidant Treatment in Hypertension and the Associated Renal Damage
Manning, R. D., Tian, N., & Meng, S. (2005) · American Journal of Nephrology · doi:10.1159/000086411 · Cited by 168 · see citing works
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Pagnin, E., Fadini, G., de Toni, R., Tiengo, A., Calò, L., & Avogaro, A. (2005) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-1283 · Cited by 127 · see citing works
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Khanday, F. A., Yamamori, T., Mattagajasingh, I., Zhang, Z., Bugayenko, A., Naqvi, A., Santhanam, L., Nabi, N., Kasuno, K., Day, B. W., et al. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-06-0570 · Cited by 100 · see citing works
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Li, S. ‐., Liu, Y., Sigmon, V. K., McCort, A., & Ren, J. (2005) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2004.00387.x · Cited by 95 · see citing works
Advanced Glycation End Product Receptor‐Mediated Cellular Dysfunction
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Khanday, F. A., Santhanam, L., Kasuno, K., Yamamori, T., Naqvi, A., DeRicco, J. S., Bugayenko, A., Mattagajasingh, I., Disanza, A., Scita, G., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200506001 · Cited by 82 · see citing works
Activation of nicotinamide adenine dinucleotide phosphate (reduced form) oxidase by advanced glycation end products links oxidative stress to altered retinal vascular endothelial growth factor expression
Li, L., & Renier, G. (2006) · Metabolism · doi:10.1016/j.metabol.2006.06.022 · Cited by 74 · see citing works
Oxidative stress in the pathogenesis of experimental mesangial proliferative glomerulonephritis
Budisavljevic, M. N., Hodge, L., Barber, K., Fulmer, J. R., Durazo-Arvizú, R., Self, S., Kuhlmann, M. K., Raymond, J. R., & Greene, E. L. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00397.2002 · Cited by 59 · see citing works
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Menini, S., Iacobini, C., de Latouliere, L., Manni, I., Ionta, V., Fantauzzi, C. B., Pesce, C. M., Cappello, P., Novelli, F., Piaggio, G., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5072 · Cited by 58 · see citing works
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Hu, Y., Jihong, Y., Feng, Z., Xu, X., Xiaohan, Z., Guangzhi, W., Ma, Z., Dongyan, G., XiaoChi, M., Qing, F., et al. (2014) · Critical Care Medicine · doi:10.1097/ccm.0000000000000246 · Cited by 55 · see citing works
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Shin, H. J., Park, H., Shin, N., Shin, J., Gwon, D. H., Kwon, H. H., Yin, Y., Hwang, J., Hong, J., Heo, J. Y., et al. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s234198 · Cited by 54 · see citing works
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Gorin, Y. C., & Wauquier, F. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.0010 · Cited by 48 · see citing works
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Liang, Y., Jian, J., Liu, Y.-C., Juang, S.-J., Shyu, K., Lai, L., Wang, B., & Leu, J. (2010) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.1100 · Cited by 47 · see citing works
PM2.5 exposure increases dry eye disease risks through corneal epithelial inflammation and mitochondrial dysfunctions
Yu, D.-H., Cai, W.-T., Shen, T., Wu, Y., Ren, C., Li, T., Hu, C.-C., Zhu, M., & Yu, J. (2023) · Cell Biology and Toxicology · doi:10.1007/s10565-023-09791-z · Cited by 41 · see citing works
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Iacobini, C., Menini, S., Fantauzzi, C. B., Pesce, C. M., Giaccari, A., Salomone, E., Lapolla, A., Orioli, M., Aldini, G., & Pugliese, G. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14070 · Cited by 42 · see citing works
Self-citation
Cardiovascular determinants of life span
Shi, Y., Camici, G. G., & Lüscher, T. F. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0727-2 · Cited by 39 · see citing works
Genetic ablation of the p66Shc adaptor protein reverses cognitive deficits and improves mitochondrial function in an APP transgenic mouse model of Alzheimer’s disease
Derungs, R., Camici, G. G., Spescha, R. D., Welt, T., Tackenberg, C., Späni, C. B., Wirth, F., Grimm, A., Eckert, A., Nitsch, R. M., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.112 · Cited by 38 · see citing works
Cardiac mitochondrial dysfunction during hyperglycemia—The role of oxidative stress and p66Shc signaling
Diogo, C. V., Suski, J. M., Lebiedzińska, M., Karkucińska‐Więckowska, A., Wojtala, A., Pronicki, M., Duszyński, J., Pinton, P., Portincasa, P., Oliveira, P. J., et al. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.07.004 · Cited by 38 · see citing works
P66Shc and vascular endothelial function
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Self-citation
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Wright, K. D., Staruschenko, A., & Sorokin, A. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00414.2017 · Cited by 33 · see citing works
Enhancement of endothelial nitric oxide synthase production reverses vascular dysfunction and inflammation in the hindlimbs of a rat model of diabetes
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Oxidative stress, a common molecular pathway for kidney disease: Role of the redox enzyme p66Shc
Yang, S., Xiao, L., Li, J., Liu, F., & Sun, L. (2013) · Renal Failure · doi:10.3109/0886022x.2013.846867 · Cited by 32 · see citing works
AGEs-Induced IL-6 Synthesis Precedes RAGE Up-Regulation in HEK 293 Cells: An Alternative Inflammatory Mechanism?
Șerban, A. I., Stanca, L., Geicu, O. I., & Dinischiotu, A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160920100 · Cited by 32 · see citing works
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Idebenone is a cytoprotective insulin sensitizer whose mechanism is Shc inhibition
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The Endothelium Abridges Insulin Resistance to Premature Aging
Avogaro, A., de Kreutzenberg, S. V., Federici, M., & Fadini, G. P. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000262 · Cited by 30 · see citing works
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Zheng, D., Tao, M., Liang, X., Li, Y., Jin, J., & He, Q. (2020) · PubMed · doi:10.14670/hh-18-178 · Cited by 29 · see citing works
Extracellular matrix is modulated in advanced glycation end products milieu via a RAGE receptor dependent pathway boosted by transforming growth factor‐β1 在晚期糖基化终末产物环境中细胞外基质通过RAGE受体依赖性途径调节，转化生长因子‐β1可以促进这种调节
Șerban, A. I., Stanca, L., Geicu, O. I., Munteanu, M. C., Costache, M., & Dinischiotu, A. (2014) · Journal of Diabetes · doi:10.1111/1753-0407.12154 · Cited by 28 · see citing works
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Teng, L., Fan, L., Peng, Y., He, X., Chen, H., Duan, H., Yang, F., Lin, D., Lin, Z., Li, H., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00026 · Cited by 26 · see citing works
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Xi, G., Shen, X., Radhakrishnan, Y., Maile, L. A., & Clemmons, D. R. (2010) · Endocrinology · doi:10.1210/en.2010-0242 · Cited by 21 · see citing works
Suppression of the p66shc adapter protein by protocatechuic acid prevents the development of lung injury induced by intestinal ischemia reperfusion in mice
Wang, G., Yao, J.-H., Jing, H., Zhang, F., Lin, M., Shi, L., Wu, H., Gao, D.-Y., Liu, K., & Tian, X. (2012) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0b013e318265d069 · Cited by 19 · see citing works
Shc depletion stimulates brown fat activity in vivo and in vitro
Tomilov, A. A., Bettaieb, A., Kim, K., Sahdeo, S., Tomilova, N. B., Lam, A., Hagopian, K., Connell, M. C., Fong, J., Rowland, D. J., et al. (2014) · Aging Cell · doi:10.1111/acel.12267 · Cited by 19 · see citing works
L-alpha-glycerylphosphorylcholine reduces the microcirculatory dysfunction and nicotinamide adenine dinucleotide phosphate-oxidase type 4 induction after partial hepatic ischemia in rats
Hartmann, P., Fet, N., Garab, D., Szabó, A., Kaszaki, J., Srinivasan, P. K., Tolba, R. H., & Boros, M. (2014) · Journal of Surgical Research · doi:10.1016/j.jss.2013.12.025 · Cited by 17 · see citing works
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Chen, S., Ji, B.-B., Yan, Y., He, X., Han, K., Dai, Q., Zhang, M.-X., Mo, Y., & Wang, J. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.01.004 · Cited by 17 · see citing works
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Self-citation
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P66SHC deletion improves fertility and progeric phenotype of late-generation TERC-deficient mice but not their short lifespan
Giorgio, M., Stendardo, M., Migliaccio, E., & Pelicci, P. G. (2016) · Aging Cell · doi:10.1111/acel.12448 · Cited by 11 · see citing works
“…different tissues of p66SHC / mice were found to be resistant to apoptosis induced by paraquat (Migliaccio et al., 1999), hypercholesterolemia (Napoli et al., 2003), hyperglycemia (Menini et al., 2007), immunotoxicity (Su et al., 2012), and ischemia/reperfusion injury (Carpi et al., 2009).”
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Self-citation
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Injury of cortical neurons is caused by the advanced glycation end products-mediated pathway.
Xing, Y., Zhang, X., Song, X., Lv, Z., Hou, L., & Li, F. (2013) · PubMed Central · doi:10.3969/j.issn.1673-5374.2013.10.005 · Cited by 9 · see citing works
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Zanetti, M., Barazzoni, R., Cappellari, G. G., Burekovic, I., Bosutti, A., Stocca, A., Bianco, F., Ianche, M., Panzetta, G. O., & Guarnieri, G. (2011) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2010.12.006 · Cited by 8 · see citing works
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Dong, W., Zhang, C., Zhao, S., Li, Q., Kang, L., Guo, L., Lei, X., & Zhai, X. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s84820 · Cited by 7 · see citing works
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Yang, X., Xu, R., Lin, Y., Zhen, Y., Wei, J., Hu, G., & Sun, H. (2016) · Scientific Reports · doi:10.1038/srep31534 · Cited by 5 · see citing works
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p66Shc signaling does not contribute to tubular damage induced by renal ischemia-reperfusion injury in rat
Miller, B., Regner, K. R., & Sorokin, A. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.03.020 · Cited by 2 · see citing works
A Cross-Sectional Study of p66Shc Gene Expression in Liquid Biopsy of Diabetic Patients. Is it Possible to Predict the Onset of Renal Disease?
Simões, D. P., Perez, M. M., Alves, B. D. C. A., Encinas, J. F. A., Raimundo, J. R. S., Arcia, C. G. C., Mathia, V. L., Mendonça, M. I. S., Maifrino, L. B. M., Murad, N., et al. (2023) · International Journal of Medical Students · doi:10.5195/ijms.2022.1306 · Cited by 2 · see citing works
Current literature in diabetes
(2008) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.844 · Cited by 1 · see citing works
EXPRESSION PROFILING OF BLOOD VESSELS IN PERICYTE DEFICIENCY AND DIABETES
Norlin, J. (2010) · Figshare · Cited by 1 · see citing works
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Iacobini, C., Vitale, M., Sentinelli, F., Lucarelli, A., Haxhi, J., Sergio, I., Pugliese, G., & Menini, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262211096
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Menini, S., Amadio, L., Oddi, G., Ricci, P. C., Pesce, C. M., Pugliese, F. R., Giorgio, M., Migliaccio, E., Pelicci, P. G., Iacobini, C., et al. (2006) · Diabetes · doi:10.2337/db05-1477 · Cited by 183 · see citing works
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Phosphorylation, F., Cai, W., He, C., Zhu, L., Striker, G. E., & Vlassara, H. (2013)
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Cai, W., He, C., Zhu, L., Chen, X., Striker, G. E., & Vlassara, H. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00350.2007 · Cited by 107 · see citing works
Aging phenotype(s) in kidneys of diabetic mice are p66ShcA dependent
Vashistha, H., Marrero, L., Krzysztof Reiss, F., Cohen, A. J., Malhotra, A., Javed, T., Bradley, A., Abbruscato, F. C., Giusti, S., Jimenez, A., et al. (2018) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00608.2017 · Cited by 8 · see citing works
Self-citation
SUN-098 MUTATION OF p66SHC IN RATS CAUSES INCREASED H2O2 PRODUCTION AND LEADS TO REDUCED NUMBER OF GLOMERULI
Sorokin, A., Miller, B., Palygin, O., El‐Meanawy, A., & Staruschenko, A. (2020) · Kidney International Reports · doi:10.1016/j.ekir.2020.02.624

Authors: Menini, S., Iacobini, C., Ricci, C., Oddi, G., Pesce, C., Pugliese, F., Block, K., Abboud, H. E., Giorgio, M., Migliaccio, E., Pelicci, P. G., & Pugliese, G.
Affiliations: Sapienza University of Rome (IT)
University of Genoa (IT)
The University of Texas at San Antonio Health Science Center (US)
European Institute of Oncology (IT)
Corresponding author: Pugliese, G.
ORCID: Menini, S.
Iacobini, C.
Pesce, C.
Pugliese, F.
Abboud, H. E.
Giorgio, M.
Migliaccio, E.
Pelicci, P. G.
Pugliese, G.
Venue: Diabetologia
Publisher: Springer Science and Business Media LLC
Published: 2007-07-05
Volume: 50
Issue: 9
Pages: 1997-2007
ISSN: 0012-186X (ISSN-L)
1432-0428
DOI: 10.1007/s00125-007-0728-7
OpenAlex: W2058050674
Cited by: 64
References: 51
Citations by year: 2025: 2 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 5 · 2019: 6 · 2018: 2 · 2017: 4 · 2016: 6 · 2015: 3 · 2014: 7 · 2013: 4 · 2012: 5
FWCI: 2.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Diabetologia (publishedVersion)
PubMed (publishedVersion)
CINECA IRIS Institutial Research Information System (University of Genoa) (submittedVersion)
IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
Padua Research Archive (University of Padova) (submittedVersion, other-oa)
Funders: European Foundation for the Study of Diabetes
Servier
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
Health Sciences › Medicine › Nephrology › Acute Kidney Injury Research
Keywords: p66Shc, advanced glycation end products, glomerular disease, oxidative stress, reactive oxygen species, kidney injury, NF-κB activation, AGE receptor, mesangial cells, proteinuria, glomerulosclerosis, carboxymethyllysine
MeSH terms: Receptor for Advanced Glycation End Products, Src Homology 2 Domain-Containing, Transforming Protein 1, Animals, Genotype, Glomerular Mesangium, Immunohistochemistry, Kidney Diseases, Kidney Glomerulus, Mice, Inbred Strains, Receptors, Immunologic, NF-kappa B, Reactive Oxygen Species, DNA Primers, Adaptor Proteins, Signal Transducing, Mice, Shc Signaling Adaptor Proteins

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Ablation of the gene encoding p66Shc protects mice against AGE-induced glomerulopathy by preventing oxidant-dependent tissue injury and further AGE accumulation

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