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Oxidative stress induces an ATM‐independent senescence pathway through p38 MAPK‐mediated lamin B1 accumulation
Open accessAbstract
We report crosstalk between three senescence-inducing conditions, DNA damage response (DDR) defects, oxidative stress (OS) and nuclear shape alterations. The recessive autosomal genetic disorder Ataxia telangiectasia (A-T) is associated with DDR defects, endogenous OS and premature ageing. Here, we find frequent nuclear shape alterations in A-T cells, as well as accumulation of the key nuclear architecture component lamin B1. Lamin B1 overexpression is sufficient to induce nuclear shape alterations and senescence in wild-type cells, and normalizing lamin B1 levels in A-T cells reciprocally reduces both nuclear shape alterations and senescence. We further show that OS increases lamin B1 levels through p38 Mitogen Activated Protein kinase activation. Lamin B1 accumulation and nuclear shape alterations also occur during stress-induced senescence and oncogene-induced senescence (OIS), two canonical senescence situations. These data reveal lamin B1 as a general molecular mediator that controls OS-induced senescence, independent of established Ataxia Telangiectasia Mutated (ATM) roles in OIS.
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“Since then, several studies have confirmed the reduction of LMNB1 in various senescent cell types (Barascu et al. 2012; Freund et al. 2012; Dreesen et al. 2013; Sadaie et al. 2013; Shah et al. 2013).”
From Cellular senescence and its effector programs (2014) · cites this paper as Barascu et al. 2012
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“Other DNA lesions—such as those caused by oxidative stress—may also drive cells into senescence (35–38).”
From Aging, Cellular Senescence, and Cancer (2013) · cites this paper as [35]
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“Oxidative stress has been ensured as a crucial factor for cellular senescence through shortening telomere and causing DNA double-strand breaks.209,210”
From Inflammation and aging: signaling pathways and intervention therapies (2023) · cites this paper as [209]
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“Compared with LMNB1 depletion, phenotypes induced by ectopic LMNB1 were more heterogeneous between studies: Overexpression of LMNB1 either delays (Shimi et al. 2011) or enhances senescence (Barascu et al. 2012; Dreesen et al. 2013) or exhibits a minimal effect on proliferation (Sadaie et al. 2013).”
From Cellular senescence and its effector programs (2014) · cites this paper as Barascu et al. 2012
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“Similarly, Barascu et al. (2012) showed that increased levels of LMNB1 are associated with ROS up-regulation and senescence.”
From Cellular senescence and its effector programs (2014) · cites this paper as Barascu et al. 2012
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WITHDRAWN: Oxidative stress in aging: Theoretical outcomes and clinical evidences in humans
del Valle, L. G. (2010) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2010.09.010 · Cited by 36
RetractedAging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567
A biomarker that identifies senescent human cells in culture and in aging skin in vivo.
Dimri, G. P., Lee, X., Basile, G., Acosta, M., Scott, G., Roskelley, C., Medrano, E. E., Linskens, M., Rubelj, I., & Pereira-Smith, O. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9363 · Cited by 7,477
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075
Direct observation of individual endogenous protein complexes in situ by proximity ligation
Söderberg, O., Gullberg, M., Jarvius, M., Ridderstråle, K., Leuchowius, K.-J., Jarvius, J., Wester, K., Hydbring, P., Bahram, F., Larsson, L.-G., et al. (2006) · Nature Methods · doi:10.1038/nmeth947 · Cited by 2,419
Persistent DNA damage signalling triggers senescence-associated inflammatory cytokine secretion
Rodier, F., Coppé, J.-P., Patil, C. K., Hoeijmakers, W. A. M., Muñoz, D. P., Raza, S. R., Freund, A., Campeau, E., Davalos, A. R., & Campisi, J. (2009) · Nature Cell Biology · doi:10.1038/ncb1909 · Cited by 2,232
Four faces of cellular senescence
Rodier, F., & Campisi, J. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201009094 · Cited by 2,070 · cited 1×
“On the other hand, in contrast, beside its putative role in organism ageing, recent data have proposed that senescent cells could favour tumour proliferation or invasion by secreting inflammatory factors (Rodier et al , 2009; Campisi et al , 2011; Rodier and Campisi, 2011).”
Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints
Bartkova, J., Rezaei, N., Liontos, M., Karakaidos, P., Kletsas, D., Issaeva, N., Vassiliou, L.-V. F., Kolettas, E., Niforou, K., Zoumpourlis, V. C., et al. (2006) · Nature · doi:10.1038/nature05268 · Cited by 1,986
Oncogene-induced senescence is a DNA damage response triggered by DNA hyper-replication
Di Micco, R., Fumagalli, M., Cicalese, A., Piccinin, S., Gasparini, P., Luise, C., Schurra, C., Garre’, M., Giovanni Nuciforo, P., Bensimon, A., et al. (2006) · Nature · doi:10.1038/nature05327 · Cited by 1,821
Protein detection using proximity-dependent DNA ligation assays
Fredriksson, S., Gullberg, M. T., Jarvius, J., Olsson, C., Pietras, K., Gustafsdottir, S., Östman, A., & Landegren, U. D. (2002) · Nature Biotechnology · doi:10.1038/nbt0502-473 · Cited by 1,518
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Aging, Cellular Senescence, and Cancer
Campisi, J. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183653 · Cited by 2,954
Inflammation and aging: signaling pathways and intervention therapies
Li, X., Li, C., Zhang, W., Wang, Y., Qian, P., & Huang, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01502-8 · Cited by 1,443
“Oxidative stress has been ensured as a crucial factor for cellular senescence through shortening telomere and causing DNA double-strand breaks.(209,210) Moreover, infections,(211) environmental pollution,(212,213) and adverse lifestyle habits(214) can increase oxidative stress.”
BackgroundLamin B1 loss is a senescence-associated biomarker
Freund, A., Laberge, R.-M., Demaria, M., & Campisi, J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-10-0884 · Cited by 1,046
“A recent report (Barascu et al., 2012) showed that oxidative stress induces senescence via an increase in lamin B1 expres-”
BackgroundCellular senescence and its effector programs
Salama, R., Sadaie, M., Hoare, M., & Narita, M. (2014) · Genes & Development · doi:10.1101/gad.235184.113 · Cited by 855
“Since then, several studies have confirmed the reduction of LMNB1 in various senescent cell types (Barascu et al. 2012; Freund et al. 2012; Dreesen et al. 2013; Sadaie et al. 2013; Shah et al. 2013).”
BackgroundInfluentialShah, P. P., Donahue, G., Otte, G. L., Capell, B. C., Nelson, D. M., Cao, K., Aggarwala, V., Cruickshanks, H. A., Rai, T. S., McBryan, T., et al. (2013) · Genes & Development · doi:10.1101/gad.223834.113 · Cited by 550
“We note that certain cell types and disease states exhibit opposite effects of lamin B1 alteration (Barascu et al. 2012; Dreesen et al. 2013).”
BackgroundThe nuclear lamins: flexibility in function
Burke, B. E., & Stewart, C. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3488 · Cited by 563
Gruenbaum, Y., & Foisner, R. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034115 · Cited by 565
Repression of the Antioxidant NRF2 Pathway in Premature Aging
Kubben, N., Zhang, W., Wang, L., Voss, T. C., Yang, J., Qu, J., Liu, G.-H., & Misteli, T. (2016) · Cell · doi:10.1016/j.cell.2016.05.017 · Cited by 489
“Furthermore, elevated levels of oxidative stress itself, induced by H2O2 pro-oxidant treatment, was sufficient for WT fibroblasts to phenotypically mimic HGPS cells for all tested defects, with the anticipated exception of lamin B1 (Barascu et al., 2012) (Figures 4E and S4G–S4I).”
Sadaie, M., Salama, R., Carroll, T., Tomimatsu, K., Chandra, T., Young, A. R. J., Narita, M., Pérez-Mancera, P. A., Bennett, D. C., Chong, H., et al. (2013) · Genes & Development · doi:10.1101/gad.217281.113 · Cited by 323
“Recent reports have shown that the global LMNB1 level is altered during senescence (Shimi et al. 2011; Barascu et al. 2012; Freund et al. 2012; Dreesen et al. 2013).”
BackgroundLamin B1 fluctuations have differential effects on cellular proliferation and senescence
Dreesen, O., Chojnowski, A., Ong, P. F., Zhao, T. Y., Common, J. E., Lunny, D., Lane, E. B., Lee, S. J., Vardy, L. A., Stewart, C. L., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201206121 · Cited by 250
“Consistent with Barascu et al. (2012), the LMNB1 overexpression–induced proliferation defect led to increased numbers of SA--gal–positive cells (26.6% in control vs. 42.8% in LMNB1-expressing cells; Fig.”
BackgroundInfluentialNuclear lamin functions and disease
Butin‐Israeli, V., Adam, S. A., Goldman, A. E., & Goldman, R. D. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.06.001 · Cited by 239
“Furthermore, lamin B1 protein and mRNA levels are reduced both in normal cellular senescence and in premature senescence induced by oncogenic Ras [20].”
BackgroundSaheb-Al-Zamani, M., Yan, Y., Farber, S. J., Hunter, D. A., Newton, P., Wood, M. D., Stewart, S. A., Johnson, P. J., & Mackinnon, S. E. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.04.011 · Cited by 213
“Interestingly, ischemic events in nerve have been associated with oxidative stress in SCs (Iida et al., 2004; Qi et al., 2001; Wang et al., 2005), which is associated with the induction of senescence (Barascu et al., 2012; Chen et al., 2001; Nogueira et al., 2008; Parrinello et al., 2003).”
BackgroundCellular senescence: Molecular mechanisms and pathogenicity
Wei, W., & Ji, S. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26956 · Cited by 214
“The result of this study is consistent with an early study that found that OS increases the expression of lamin B1 by activating the p38 MAPK pathway which induces cellular senescence (Barascu et al., 2012).”
ResultSizing and shaping the nucleus: mechanisms and significance
Jevtić, P., Edens, L. J., Vukovic, L. D., & Levy, D. L. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.01.003 · Cited by 204
“Abnormal nuclear shape and premature senescence of Ataxia telangiectasia cells were rescued by reducing lamin B1 levels [33].”
BackgroundBorodkina, A. V., Shatrova, A. N., Abushik, P. A., Nikolsky, N. N., & Burova, E. (2014) · Aging · doi:10.18632/aging.100673 · Cited by 214
“The pharmacological inhibition of p38 activation may be considered as a possible strategy for senescence prevention [45, 49].”
BackgroundRole of sphingolipids in senescence: implication in aging and age-related diseases
Trayssac, M., Hannun, Y. A., & Obeid, L. M. (2018) · Journal of Clinical Investigation · doi:10.1172/jci97949 · Cited by 216
Profiling senescent cells in human brains reveals neurons with CDKN2D/p19 and tau neuropathology
Dehkordi, S. K., Walker, J., Sah, E., Bennett, E., Atrian, F., Frost, B., Woost, B., Bennett, R. E., Orr, T. C., Zhou, Y., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00142-3 · Cited by 169
The ATM signaling network in development and disease
Stracker, T. H., Roig, I., Knobel, P. A., & Marjanović, M. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00037 · Cited by 192
“…be partially rescued by decreasing the gene dosage of lamin A. Additional links between ATM and the nuclear lamina were uncovered by the Bertrand laboratory that found lamin B protein, but not mRNA, is overexpressed in ATM-deficient cells, leading to morphological defects (Barascu et al., 2012).”
BackgroundAge-Associated Loss of Lamin-B Leads to Systemic Inflammation and Gut Hyperplasia
Chen, H., Zheng, X., & Zheng, Y. (2014) · Cell · doi:10.1016/j.cell.2014.10.028 · Cited by 168
“…lamin-B1 loss, increased secretion of inflammatory factors (also called senescence associated secretory phenotype, SASP), but it remains unknown whether lamin-B1 loss in vitro (Barascu et al., 2012; Dreesen et al., 2013; Freund et al., 2012; Shimi et al., 2011) or upon aging in vivo leads to SASP.”
Lau, V. Z., Ramer, L. M., & Tremblay, M. (2023) · Nature Communications · doi:10.1038/s41467-023-37304-3 · Cited by 175
Zhang, D., Hu, X., Li, J., Liu, J., Bulte, L. B.-T., Wiersma, M., Malik, N.-U.-A., van Marion, D. M. S., Tolouee, M., Hoogstra‐Berends, F., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09014-2 · Cited by 166
Han, J., Wu, J., & Silke, J. (2020) · F1000Research · doi:10.12688/f1000research.22092.1 · Cited by 163
Cell Senescence, DNA Damage, and Metabolism
Shmulevich, R., & Krizhanovsky, V. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8043 · Cited by 157
“Senescence may result in response to multiple stress stimuli such as telomere dysfunction, oxidative stress, active onco-genes, and DNA damage (7, 15, 27, 28, 63, 72, 82, 98a) (Fig.”
Senescence and the tumor-immune landscape: Implications for cancer immunotherapy
Chibaya, L., Snyder, J. T., & Ruscetti, M. A. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.02.005 · Cited by 146
Senolytics for Cancer Therapy: Is All that Glitters Really Gold?
Carpenter, V. J., Saleh, T., & Gewirtz, D. A. (2021) · Cancers · doi:10.3390/cancers13040723 · Cited by 124
“Lamin B1 may accumulate [17], providing another example of the phenotypic variability of senescence.”
BackgroundDiverse lamin-dependent mechanisms interact to control chromatin dynamics
Camozzi, D., Capanni, C., Cenni, V., Mattioli, E., Columbaro, M., Squarzoni, S., & Lattanzi, G. (2014) · Nucleus · doi:10.4161/nucl.36289 · Cited by 118
“However, lamin B1 accumulation has been also observed in cells subjected to oxidative stress and entering senescence.(89) Further, SUN1 recruitment at the nuclear envelope in centenarian cells has been observed.”
The Paradoxical Role of Cellular Senescence in Cancer
Yang, J., Liu, M., Hong, D., Zeng, M., & Zhang, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.722205 · Cited by 125
“Oxidative stress and several DNA-damaging agents often induce DNA base damage and single-strand breaks (Robles and Adami, 1998; Chang et al., 2002; Parrinello et al., 2003; Sedelnikova et al., 2004; Barascu et al., 2012).”
BackgroundNuclear envelope dysfunction and its contribution to the aging process
Martins, F., Sousa, J., Pereira, C. D., Silva, O. A. B. D. C. E., & Rebelo, S. (2020) · Aging Cell · doi:10.1111/acel.13143 · Cited by 114
“However, recent studies showed that lamin B1 reduction has a minimal effect on cell proliferation but renders cells more susceptible to senescence (Dreesen, Chojnowski, et al., 2013), while lamin B1 overexpression induces senescence (Barascu et al., 2012; Dreesen, Chojnowski, et al., 2013).”
BackgroundIakovou, E., & Kourti, M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.827900 · Cited by 119
“Oxidative stress is highly associated with cellular senescence, because it drives DNA lesions, accelerates telomere shortening, and activates molecular pathways leading to growth arrest (Chen et al., 2001; Nogueira et al., 2008; Barascu et al., 2012; Benkafadar et al., 2019).”
BackgroundYang, Z., Sun, Q., Guo, J., Wang, S., Song, G., Liu, W., Liu, M., & Tang, H. (2018) · Autophagy · doi:10.1080/15548627.2018.1539590 · Cited by 95
RetractedThe role of lamin B1 for the maintenance of nuclear structure and function
Camps, J., Erdos, M. R., & Ried, T. (2015) · Nucleus · doi:10.1080/19491034.2014.1003510 · Cited by 97
“On the other hand, while loss of LMNB1 is a senescence-associated biomarker in primary human and murine cultured normal fibroblasts induced by DNA damage, replicative exhaustion, or oncogene expression,(9,10) increased levels of LMNB1 in response to reactive oxygen species (ROS)-induced senescence through p38 MAPK act…”
BackgroundGuo, T., Mao, X., Zhang, H., Zhang, Y., Fu, M., Sun, Z., Kuai, P., Lou, Y., & Fang, Y. (2017) · Molecular Plant · doi:10.1016/j.molp.2017.09.008 · Cited by 87
Recent advances in understanding nuclear size and shape
Mukherjee, R. N., Chen, P., & Levy, D. L. (2016) · Nucleus · doi:10.1080/19491034.2016.1162933 · Cited by 95
Poppler, L. H., Ee, X., Schellhardt, L., Hoben, G. M., Pan, D., Hunter, D. A., Yan, Y., Moore, A. M., Snyder‐Warwick, A. K., Stewart, S. A., et al. (2016) · Tissue Engineering Part A · doi:10.1089/ten.tea.2016.0003 · Cited by 87
The wide and growing range of lamin B-related diseases: from laminopathies to cancer
Evangelisti, C., Rusciano, I., Mongiorgi, S., Ramazzotti, G., Lattanzi, G., Manzoli, L., Cocco, L., & Ratti, S. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04084-2 · Cited by 97
“Of note, it has been also shown that different senescence-inducing conditions as oncogene expression or oxidative stress elicit different effects on lamin B1 levels [30].”
BackgroundInfluentialCellular Senescence: Mechanisms and Therapeutic Potential
Liao, Z., Yeo, H. L., Wong, S. W., & Zhao, Y. X. (2021) · Biomedicines · doi:10.3390/biomedicines9121769 · Cited by 89
“Both lamin B1 overexpression and its reduction have been found to induce senescence in fibroblasts, but the overexpression of lamin B1 has also been associated with an increased proliferative capability and a delay in the onset of senescence [23,26,28].”
BackgroundType I interferons and related pathways in cell senescence
Frisch, S. M., & MacFawn, I. (2020) · Aging Cell · doi:10.1111/acel.13234 · Cited by 89
“…DNA repair, or down-regulation of cytoplasmic DNases have been shown to generate a senescent phenotype as well, by novel mechanisms that will be addressed below (Barascu et al., 2012; Dou et al., 2017; Gluck et al., 2017; Graziano, Kreienkamp, CollBonfill, & Gonzalo, 2018; Takahashi et al., 2018).”
BackgroundCong, Q., Jia, H., Li, P., Qiu, S., Yeh, J., Wang, Y., Zhang, Z., Ao, J., Li, B., & Liu, H. (2017) · Scientific Reports · doi:10.1038/srep45964 · Cited by 85
Autophagy at the intersection of aging, senescence, and cancer
Cassidy, L. D., & Narita, M. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13269 · Cited by 93
Role of Lamin B1 in Chromatin Instability
Butin‐Israeli, V., Adam, S. A., Jain, N., Otte, G. L., Neems, D. S., Wiesmüller, L., Berger, S. L., & Goldman, R. D. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01145-14 · Cited by 88
“regulates cell proliferation are complex (17, 18, 21).”
BackgroundCellular Senescence and Vascular Disease: Novel Routes to Better Understanding and Therapy
Yin, H., & Pickering, J. G. (2016) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2016.02.051 · Cited by 82
Grabowska, W., Staniak, K., Wnuk, M., Lewińska, A., Suszek, M., Przybylska, D., Mosieniak, G., Sikora, E., & Bielak-Żmijewska, A. (2015) · AGE · doi:10.1007/s11357-014-9744-y · Cited by 71
“(Barascu et al. 2012).”
Nuclear envelope-related lipodystrophies
Guénantin, A.-C., Briand, N., Bidault, G., Afonso, P., Béréziat, V., Vatier, C., Lascols, O., Caron, M., Capeau, J., & Vigouroux, C. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.12.015 · Cited by 67
Lamins in development, tissue maintenance and stress
Zuela-Sopilniak, N., Bar, D. Z., & Gruenbaum, Y. (2012) · EMBO Reports · doi:10.1038/embor.2012.167 · Cited by 70
“Interestingly, in these ataxia telangiectasia cells, the levels of lamin B1 are regulated by the p38 MAPK, in an ATM-independent manner [95].”
Phytochemical-induced nucleolar stress results in the inhibition of breast cancer cell proliferation
Lewińska, A., Bednarz, D., Adamczyk‐Grochala, J., & Wnuk, M. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.014 · Cited by 69
“However, both elevated and diminished levels of lamin B1 may be associated with senescence in response to disturbed ROS homeostasis [66,67], but, in general, healthy early passage cells are characterized by balanced lamin B1/lamin A ratio and stressed/senescent cells are characterized by unbalanced lamin B1/ lamin A r…”
BackgroundLivanos, P., Apostolakos, P., & Galatis, B. (2012) · Plant Signaling & Behavior · doi:10.4161/psb.20530 · Cited by 69
Li, X., Si, Y., Liang, J., Li, M., Wang, Z., Qin, Y., & Sun, L. (2024) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2024.05.209 · Cited by 72
Centenarian lamins: rapamycin targets in longevity
Lattanzi, G., Ortolani, M., Columbaro, M., Prencipe, S., Mattioli, E., Lanzarini, C., Maraldi, N. M., Cenni, V., Garagnani, P., Salvioli, S., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.133983 · Cited by 70
Lamin in inflammation and aging
Tran, J. R., Chen, H., Zheng, X., & Zheng, Y. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.03.004 · Cited by 66
Wilhelm, T., Ragu, S., Magdalou, I., Machon, C., Dardillac, E., Técher, H., Guitton, J., Debatisse, M., & López, B. S. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006007 · Cited by 75
Rolyan, H., Tyurina, Y. Y., Hernandez, M., Amoscato, A. A., Sparvero, L. J., Nmezi, B., Lu, Y., Estecio, M. R., Lin, K., Chen, J., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1668-15.2015 · Cited by 68
“Altered LMNB1 expression has been associated with increased levels of reactive oxygen species and this may be a potential pathway that triggers an inflammatory response independent of lipid dysregulation (Malhas et al., 2009; Shimi et al., 2011; Barascu et al., 2012; Hutchison, 2012).”
BackgroundLamins as mediators of oxidative stress
Sieprath, T., Darwiche, R., & Vos, W. H. D. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.058 · Cited by 67
B-type lamins in health and disease
Hutchison, C. J. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.12.012 · Cited by 64
“In an apparently contradictory study, entry into a senescent state as a result of MAPK activation and oxidative stress was accompanied by up-regulated expression of lamin B1 suggesting a novel mechanism of ATM-independent stress sensing [36].”
BackgroundAutophagy-mediated degradation of nuclear envelope proteins during oncogene-induced senescence
Lenain, C., Gusyatiner, O., Douma, S., van den Broek, B., & Peeper, D. S. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv124 · Cited by 65
“Nuclear shape alterations were also reported in the context of Ras-induced senescence and IR-induced senescence, although in this study senescence was associated with lamin B1 upregulation rather than downregulation (32).”
BackgroundThe p38‐activated ER stress‐ATF6α axis mediates cellular senescence
Kim, H. S., Kim, Y.-J., Lim, M. J., Park, Y.-G., Park, S. I., & Sohn, J. (2018) · The FASEB Journal · doi:10.1096/fj.201800836r · Cited by 65
“Ectopic expression of the cleaved ATF6a [ATF6 (1-373)], but not that of a DNA-binding mutant of the ATF6a (1-373) [ATF6 (1-373)m1], induced cellular senescence (Fig.”
BackgroundMethodInfluentialAge-associated stresses induce an anti-inflammatory senescent phenotype in endothelial cells
Coleman, P. R., Chang, G., Hutás, G., Grimshaw, M. J., Vadas, M. A., & Gamble, J. R. (2013) · Aging · doi:10.18632/aging.100622 · Cited by 60
“p38MAPK has been linked to senescence and SASP induction in fibroblasts by multiple stimuli [24, 25].”
BackgroundChen, X., Zhao, X., Cai, H. “., Sun, H., Hu, Y., Huang, X., Kong, W., & Kong, W. (2017) · Redox Biology · doi:10.1016/j.redox.2017.04.031 · Cited by 60
“As reported by Barascu and coworker, oxidative stress increases the expression of lamin B1, and it acts as a general molecular mediator that controls oxidative stress-induced senescence [43].”
BackgroundGe, Q., Wang, Z., Wu, Y., Huo, Q., Qian, Z., Tian, Z., Ren, W., Zhang, X., & Han, J. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700134 · Cited by 58
“Other signaling mechanisms involved in synaptic plasticity, including the extracellular signal-regulated kinase (ERK) pathway, could also be affected by oxidative stress [24].”
BackgroundCorpet, A., & Stucki, M. (2014) · Chromosoma · doi:10.1007/s00412-014-0469-6 · Cited by 60
“Two studies reported increased senescence upon overexpression of LMNB1 (Barascu et al. 2012; Dreesen et al. 2013), while others found delayed senescence (Shimi et al.”
BackgroundPartial lipodystrophy with severe insulin resistance and adult progeria Werner syndrome
Donadille, B., D’anella, P., Auclair, M., Uhrhammer, N. A., Sorel, M., Grigorescu, R., Ouzounian, S., Cambonie, G., Boulot, P., Laforêt, P., et al. (2013) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-8-106 · Cited by 56
Nuclear Nestin deficiency drives tumor senescence via lamin A/C-dependent nuclear deformation
Zhang, Y., Wang, J., Huang, W., Cai, J., Ba, J., Wang, Y., Ke, Q., Huang, Y., Liu, X., Qiu, Y., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05808-y · Cited by 56
Andrenacci, D., Cavaliere, V., & Lattanzi, G. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100995 · Cited by 64
Oxidative stress and aging: synergies for age related diseases
Santos, D. F., Simão, S., Nóbrega, C., Bragança, J., Castelo‐Branco, P., & Araújo, I. M. (2024) · FEBS Letters · doi:10.1002/1873-3468.14995 · Cited by 67
“…several components of the senescence-associated secretory phenotype accelerate telomere shortening, as well as potentiate DNA lesions and activates cell arrest-related molecular pathways, contributing to strength the association of oxidative stress to cellular senescence [168,180,181,182].”
Heat stress: A risk factor for skin carcinogenesis
Calapre, L., Gray, E. S., & Ziman, M. R. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.05.039 · Cited by 57
“BCC is defined as a malignant tumour of follicular germinative cells or trichloroblasts (Barascu et al., 2012; Hsieh et al., 2014).”
BackgroundHelbling-Leclerc, A., Garcin, C., & Rosselli, F. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00764-5 · Cited by 58
“envelope structure is altered because of p53- and p16dependent downregulation of lamin B1 [53].”
BackgroundLamin B1 sequesters 53BP1 to control its recruitment to DNA damage
Etourneaud, L., Moussa, A., Rass, E., Genet, D., Willaume, S., Chabance-Okumura, C., Wanschoor, P., Picotto, J., Thézé, B., Dépagne, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abb3799 · Cited by 54
“We showed that normalizing lamin B1 rescued the nuclear shape alteration (NSA) and decreased the premature senescence observed in these cells (38).”
BackgroundSelf-citationBiomechanical defects and rescue of cardiomyocytes expressing pathologic nuclear lamins
Laurini, E., Martinelli, V. C., Lanzicher, T., Puzzi, L., Borin, D., Chen, S. N., Long, C. S., Lee, P., Mestroni, L., Taylor, M. R. G., et al. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy040 · Cited by 56
“Interestingly, silencing of p38 MAPK in human fibroblasts characterized by ataxia telangiectasia also led to a reduction in the frequency of cells with alterations in nuclear shape and concomitantly to a reduction in the frequency of senescent cells.(66) Furthermore, in mice with LMNA mutations, there is a loss of fun…”
Potential role of senescence in radiation-induced damage of the aged skeleton
Chandra, A., Park, S. S., & Pignolo, R. J. (2018) · Bone · doi:10.1016/j.bone.2018.12.006 · Cited by 53
Bourgeois, B. M. R., Gilquin, B., Tellier-Lebègue, C., Östlund, C., Wu, W., Pérez, J., Hage, P. E., Lallemand, F., Worman, H. J., & Zinn‐Justin, S. (2013) · Science Signaling · doi:10.1126/scisignal.2003411 · Cited by 52
“Several inner nuclear membrane proteins regulate critical signaling pathways and can be viewed as intranuclear regulators of signaling pathways that receive and transduce signals from the extracellular matrix and cytoskeleton, participating in cellular responses to developmental cues or stresses (3, 4).”
BackgroundNuclear Lamins and Oxidative Stress in Cell Proliferation and Longevity
Shimi, T., & Goldman, R. D. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-8032-8_19 · Cited by 54
“However, it has been reported that fibroblasts derived from patients with the recessive autosomal genetic disorder ataxia telangiectasia show an increase in LB1 expression in response to oxidative stress mediated by the activation of p38 mitogenactivated protein (MAP) kinase [29].”
BackgroundTelomeres and telomerase dance to the rhythm of the cell cycle
Londoño‐Vallejo, A., & Wellinger, R. J. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.05.004 · Cited by 52
Sadaie, M., Dillon, C., Narita, M., Young, A. R. J., Cairney, C. J., Godwin, L. S., Torrance, C. J., Bennett, D. C., Keith, W. N., & Narita, M. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-01-0003 · Cited by 53
“, 2002, 2005), alterations of lamin B1 and other components of the nuclear envelope (Maeshima et al., 2006; Barascu et al., 2012; Freund et al., 2012; Dreesen et al., 2013; Sadaie et al., 2013; Shah et al., 2013), and alterations of nuclear shape (Matsumura et al.”
BackgroundShi, Q., Liao, K.-S., Zhao, K., Wang, W., Zuo, T., Deng, W., Chen, C., Yu, J., Guo, W., He, X., et al. (2015) · Mediators of Inflammation · doi:10.1155/2015/685043 · Cited by 49
Sidler, C. L., Wóycicki, R. K., Li, D., Wang, B., Kovalchuk, I., & Kovalchuk, O. (2014) · Aging · doi:10.18632/aging.100678 · Cited by 51
The contrasting roles of lamin B1 in cellular aging and human disease
Dreesen, O., Ong, P. F., Chojnowski, A., & Colman, A. (2013) · Nucleus · doi:10.4161/nucl.25808 · Cited by 53
“Interestingly, sparsely plated lamin and fibroblasts from patients with ataxia telangiectasia (AT), whose clinical traits include neurological defects.(9) AT is caused by mutations in ATM (ataxia telangiectasia mutated), a protein kinase that controls early steps during DNA damage response signaling.”
BackgroundInfluentialRichardson, M., & Richardson, D. R. (2023) · Molecular Pharmacology · doi:10.1124/molpharm.123.000803 · Cited by 48
The hallmarks of aging in Ataxia-Telangiectasia
Aguado, J., Gómez‐Inclán, C., Leeson, H. C., Lavin, M. F., Shiloh, Y., & Wolvetang, E. J. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101653 · Cited by 47
Wu, W., Menon, R., Xu, Y.-Y., Zhao, J.-R., Wang, Y.-L., Liu, Y., & Zhang, H.-J. (2016) · Scientific Reports · doi:10.1038/srep38946 · Cited by 47
“The oxidative stress–induced p38-MAPK activation was also involved in cellular senescence 27,28 .”
Lewińska, A., Adamczyk‐Grochala, J., Kwasniewicz, E., & Wnuk, M. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25848 · Cited by 48
“…et al., 2011), for example, both increased and decreased levels of lamin B1 may be related to senescence in response to disturbed ROS homeostasis (Barascu et al., 2012; Shimi et al., 2011), and both depletion and overexpression of lamin B1 may inhibit cell proliferation (Dreesen et al., 2013).”
BackgroundNeuron type‐specific increase in lamin B1 contributes to nuclear dysfunction in Huntington’s disease
Alcalá‐Vida, R., García-Forn, M., Castany‐Pladevall, C., Creus‐Muncunill, J., Ito, Y., Blanco, E., Golbano, A., Crespí‐Vázquez, K., Parry, A., Slater, G., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012105 · Cited by 48
NADPH oxidase 4 is a critical mediator in Ataxia telangiectasia disease
Weyemi, U., Redon, C. E., Aziz, T., Choudhuri, R., Maeda, D., Parekh, P. R., Bonner, M. Y., Arbiser, J. L., & Bonner, W. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418139112 · Cited by 47
“Human primary A-T fibroblasts were also found to exhibit increased replicative senescence (31).”
BackgroundATM at the crossroads of reactive oxygen species and autophagy
Xie, X., Zhang, Y., Wang, Z., Wang, S., Jiang, X.-Y., Cui, H., Zhou, T., He, Z., Feng, H., Guo, Q., et al. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.63963 · Cited by 44
“However, the function of ATM/DDR pathway is different from that of ROS in aging process, and these two pathways play roles in different aging stages [82].”
BackgroundCano, M., Guerrero‐Castilla, A., Nabavi, S. M., Ayala, A., & Argüelles, S. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.05.052 · Cited by 42
Regulation of Nucleotide Excision Repair by Nuclear Lamin B1
Butin‐Israeli, V., Adam, S. A., & Goldman, R. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069169 · Cited by 46
“suggests that the mechanisms by which LB1 regulates cell proliferation are complex [17,19].”
BackgroundOxydative stress alters nuclear shape through lamins dysregulation
Barascu, A., Chalony, C. L., Pennarun, G., Genet, D., Zaarour, N., & Bertrand, P. (2012) · Nucleus · doi:10.4161/nucl.21674 · Cited by 42
Self-citationRegulation of Myelination in the Central Nervous System by Nuclear Lamin B1 and Non-coding RNAs
Lin, S.-T., Heng, M. Y., Ptáček, L. J., & Fu, Y.-H. (2014) · Translational Neurodegeneration · doi:10.1186/2047-9158-3-4 · Cited by 40
“reported to play a role in cell proliferation and senescence in culture [56-58], and both silencing and overexpressing lamin B1 have been linked to senescence [56,57,59].”
BackgroundNair, R. R., Bagheri, M., & Saini, D. K. (2014) · Journal of Cell Science · doi:10.1242/jcs.159517 · Cited by 38
“…made because such discrepancies could be due to differences in the senescence stage in which the experiments were performed and the methods which were used for senescence generation (Barascu et al., 2012; Lee et al., 1999; Passos and Von Zglinicki, 2006; Pospelova et al., 2009; Qu et al., 2014).”
MethodMaitra, D., Elenbaas, J. S., Whitesall, S. E., Basrur, V., D’Alecy, L. G., & Omary, M. B. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.636001 · Cited by 38
“Changes in nuclear shape were analyzed using a previously published method with minor modifications (12), using image analysis software ImageJ (13), available at http://imagej.”
BackgroundMethodRegulation of homologous recombinational repair by lamin B1 in radiation‐induced DNA damage
Liu, N., Sun, J., Kono, K., Horikoshi, Y., Ikura, T., Tong, X., Haraguchi, T., & Tashiro, S. (2015) · The FASEB Journal · doi:10.1096/fj.14-265546 · Cited by 36
“LaminB1 expression is increased in lymphoblasts and fibroblasts frompatientswith ataxia telangiectasia, which showdefects in the DNA damage response (20).”
BackgroundEnpp1 is an anti-aging factor that regulates Klotho under phosphate overload conditions
Watanabe, R., Fujita, N., Sato, Y., Kobayashi, T., Morita, M., Oike, T., Miyamoto, K., Kuro‐o, M., Michigami, T., Fukumoto, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-07341-2 · Cited by 36
Role of the Nuclear Lamina in Age-Associated Nuclear Reorganization and Inflammation
Kristiani, L., Kim, M., & Kim, Y. (2020) · Cells · doi:10.3390/cells9030718 · Cited by 36
“Studies revealed that lamin B1 overexpression induced cellular senescence and impaired proliferation, whereas shRNA-mediated lamin B1 depletion inhibited proliferation but did not induce cellular senescence in human fibroblasts [86,93].”
BackgroundPark, S. S., Lee, Y., Choi, Y. W., Lim, S. B., Park, S. H., Kim, H. K., Shin, J. S., Kim, Y. H., Lee, D. H., Kim, J., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113912 · Cited by 39
“26,52 Therefore, decrease in lamin B1 could not be an appropriate marker to detect STCs in CRC.”
BackgroundWang, H., Karuppan, M. K. M., Devadoss, D., Nair, M., Chand, H. S., & Lakshmana, M. K. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.06.003 · Cited by 35
Altered expression pattern of Nrf2/HO-1 axis during accelerated-senescence in HIV-1 transgenic rat
Davinelli, S., Scapagnini, G., Denaro, F., Calabrese, V., Benedetti, F., Krishnan, S., Curreli, S., Bryant, J., & Zella, D. (2014) · Biogerontology · doi:10.1007/s10522-014-9511-6 · Cited by 35
Luo, X., Suzuki, M., Ghandhi, S. A., Amundson, S. A., & Boothman, D. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099983 · Cited by 35
Kim, Y. (2023) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102257 · Cited by 35
Giacosa, S., Pillet, C., Séraudie, I., Guyon, L., Wallez, Y., Roelants, C., Battail, C., Evrard, B., Chalmel, F., Barette, C., et al. (2021) · Cancers · doi:10.3390/cancers13030576 · Cited by 43
Mytych, J., Pacyk, K., Pępek, M., Żebrowski, J., Lewińska, A., & Wnuk, M. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.02.072 · Cited by 35
Vascularization is delayed in long nerve constructs compared with nerve grafts
Farber, S. J., Hoben, G. M., Hunter, D. A., Yan, Y., Johnson, P. J., Mackinnon, S. E., & Wood, M. D. (2016) · Muscle & Nerve · doi:10.1002/mus.25173 · Cited by 33
BHPF exposure impairs mouse and human decidualization
Zhi-yong, J., Liu, C.-K., Hong, Y., Liang, Y., Liu, L., & Yang, Z. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.119222 · Cited by 33
Metadata
- Authors
- Barascu, A., Le Chalony, C., Pennarun, G., Genet, D., Imam, N., Lopez, B., & Bertrand, P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Bertrand, Pascale
- Venue
- The EMBO Journal
- Published
- 2012-01-13
- Volume
- 31
- Issue
- 5
- Pages
- 1080-1094
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3297999
- OpenAlex
- W2160703969
- Cited by
- 206
- References
- 84
- Citations by year
- 2026: 6 · 2025: 14 · 2024: 12 · 2023: 8 · 2022: 11 · 2021: 16 · 2020: 17 · 2019: 9 · 2018: 12 · 2017: 12 · 2016: 17 · 2015: 15 · 2014: 24 · 2013: 15 · 2012: 18
- FWCI
- 9.25
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- oxidative stress, cellular senescence, ATM, lamin B1, p38 MAPK, ataxia telangiectasia, DNA damage response, stress-induced senescence, oncogene-induced senescence, nuclear organization, premature aging
- MeSH terms
- Aging, Cells, Cultured, Humans, Signal Transduction, Oxidative Stress, Lamin Type B, p38 Mitogen-Activated Protein Kinases
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