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Human lipodystrophies linked to mutations in A-type lamins and to HIV protease inhibitor therapy are both associated with prelamin A accumulation, oxidative stress and premature cellular senescence
Abstract
Lipodystrophic syndromes associated with mutations in LMNA, encoding A-type lamins, and with HIV antiretroviral treatments share several clinical characteristics. Nuclear alterations and prelamin A accumulation have been reported in fibroblasts from patients with LMNA mutations and adipocytes exposed to protease inhibitors (PI). As genetically altered lamin A maturation also results in premature ageing syndromes with lipodystrophy, we studied prelamin A expression and senescence markers in cultured human fibroblasts bearing six different LMNA mutations or treated with PIs. As compared to control cells, fibroblasts with LMNA mutations or treated with PIs had nuclear shape abnormalities and reduced proliferative activity that worsened with increasing cellular passages. They exhibited prelamin A accumulation, increased oxidative stress, decreased expression of mitochondrial respiratory chain proteins and premature cellular senescence. Inhibition of prelamin A farnesylation prevented cellular senescence and oxidative stress. Adipose tissue samples from patients with LMNA mutations or treated with PIs also showed retention of prelamin A, overexpression of the cell cycle checkpoint inhibitor p16 and altered mitochondrial markers. Thus, both LMNA mutations and PI treatment result in accumulation of farnesylated prelamin A and oxidative stress that trigger premature cellular senescence. These alterations could participate in the pathophysiology of lipodystrophic syndromes and lead to premature ageing complications.
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“To our knowledge, no evidence yet exists on whether antiretroviral compounds can induce senescence in adipocytes in vitro, but it has been demonstrated that protease inhibitors and NRTIs can induce p16 and p21 expression in human adipose tissue (Caron et al, 2007, 2008).”
From The struggle of a good friend getting old: cellular senescence in viral responses and therapy (2021) · cites this paper as Caron et al, 2007
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Self-citationHIV-associated lipodystrophy: from fat injury to premature aging
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DNA repair defects and genome instability in Hutchinson–Gilford Progeria Syndrome
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Zaremba-Czogalla, M., Dubińska–Magiera, M., & Rzepecki, R. (2011) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-010-0038-9 · Cited by 103
Oxidative Stress Accumulates in Adipose Tissue during Aging and Inhibits Adipogenesis
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Self-citationExploring the pathophysiology behind the more common genetic and acquired lipodystrophies
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“…and collaborators demonstrated that several LMNA mutations observed in lipodystrophic patients, or in HIV patients treated with some protease inhibitors, resulted in an accumulation of Prelamin A and an increased oxidative stress that triggers premature cellular senescence (Caron et al., 2007).”
HIV-associated cellular senescence: A contributor to accelerated aging
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“Adipose tissue from lipodystrophic HIV-infected patients who were on these PIs showed an increase in the senescence marker p16, providing an in vivo relationship between senescence and lipodystrophy (Caron et al., 2007).”
Oldenburg, A. R., Briand, N., Sørensen, A. L., Cahyani, I., Shah, A., Moskaug, J. Ø., & Collas, P. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701043 · Cited by 86
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Cenni, V., Capanni, C., Mattioli, E., Schena, E., Squarzoni, S., Bacalini, M. G., Garagnani, P., Salvioli, S., Franceschi, C., & Lattanzi, G. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101073 · Cited by 87
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“Moreover, oxidative stress has been implicated in the pathophysiology of lamin A-linked Amyotrophic Quadricipital Syndrome with cardiac involvement and in human FPLD fibroblasts with lamin A/C mutations which undergo p16-dependent senescent arrest (Caron et al. 2007; Charniot et al. 2007).”
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“23 (PIs), which inhibit Zmpste24 activity and lead to prelamin A accumulation (51), induce the expression of oxidative stress markers in adipose tissue in a manner comparable to that observed in patients with LMNA mutations (52).”
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InfluentialEffects of Mechanical Stress and Carvedilol in Lamin A/C–Deficient Dilated Cardiomyopathy
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“That these phenotypes are generated by bioenergetic dysfunction is supported by the report that cells harboring LMNA mutations exhibit mitochondrial biochemical defects (Caron et al. 2007; Wallace and Fan 2009a).”
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“Some studies have also shown that cells with LMNA mutations that cause partial lipodystrophy lead to increased cellular susceptibility to oxidative stress (Caron et al. 2007; Verstraeten et al. 2009).”
BackgroundAraújo‐Vilar, D., Lattanzi, G., González‐Méndez, B., Costa‐Freitas, A. T., Prieto, D., Columbaro, M., Mattioli, E., Victoria, B., Martínez‐Sánchez, N., Рамазанова, А. Р., et al. (2008) · Journal of Medical Genetics · doi:10.1136/jmg.2008.059485 · Cited by 58
Structure and unique mechanical aspects of nuclear lamin filaments
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“Laminopahties are highly varied and include muscular dystrophies [19], lipodystrophies [20] and progeria syndromes [21] to name a few.”
BackgroundZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders
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“Prelamin A accumulation can be found in the tissues of patients taking HIV-PIs, suggesting a link between inhibition of ZMPSTE24 and the side effects of the drugs (Caron et al., 2007).”
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
“R482W LMNAmutated cells [15], was not detectable in control and patient 1’s cells (Figure 6B).”
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“Nelfinavir induces oxidative stress and can also lead to adipocyte necrosis [43] and premature senescence in human fibroblasts [34].”
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“The present results show that metreleptin therapy also increases insulin secretion in this subgroup of patients, affected by typical Dunnigan syndrome (familial partial lipodystrophy 2) [17] or by previously described mixed laminopathic phenotypes associated with lipodystrophic syndrome and progeroid or cardiomyopathi…”
ResultSelf-citationThe struggle of a good friend getting old: cellular senescence in viral responses and therapy
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“Prelamin A accumulation is observed in AVTIS cells induced by protease inhibitors but senescence induction was less efficient when cells were also treated with protein farnesylation inhibitors pravastatin or zoledronic acid (Caron et al , 2007; Lef (cid”
Global crotonylome reveals hypoxia-mediated lamin A crotonylation regulated by HDAC6 in liver cancer
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“Most of these mutations result in the maturation dysfunction and accumulation of prelamin A at the nuclear envelope [24], eventually causing impaired DNA damage repair, cellular senescence, and dysfunction [25–27].”
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“It has been previously described in the literature that the accumulation of prelamin A induced by some HIV protease inhibitors leads to a premature senescent phenotype in several cell types, including fibroblasts [47], endothelial or peripheral blood mononuclear cells [48].”
BackgroundRequirements for Efficient Proteolytic Cleavage of Prelamin A by ZMPSTE24
Barrowman, J., Hamblet, C., Kane, M. S., & Michaelis, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032120 · Cited by 53
Nuclear 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
“Fibroblasts derived from patients with the LMNA mutations D47Y, L92F, L387V, R399H, L421P, and R482W, causing insulin resistance and/or lipodystrophy, accumulate pre-LA, and this is related to increased oxidative stress and the decreased expression of mitochondrial respiratory chain proteins that trigger premature cel…”
BackgroundGoulbourne, C. N., Malhas, A. N., & Vaux, D. J. (2011) · Journal of Cell Science · doi:10.1242/jcs.091009 · Cited by 50
“The consequences of accumulation of farnesylated prelamin A, whether as a result of drug treatment or mutation, has sparked much interest in several areas of cell biology including HIV therapy (Capeau et al., 2006; Capeau et al., 2005; Caron et al., 2007; Clarke, 2007; Coffinier et al., 2007; Coffinier et al., 2008; G…”
BackgroundBourgeois, C., Gorwood, J., Olivo, A., Pelletier, L., Capeau, J., Lambotte, O., Béréziat, V., & Lagathu, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.670566 · Cited by 51
Self-citationDour, C. L., Schneebeli, S., Bakiri, F., Darcel, F., Jacquemont, M., Maubert, M.-A., Auclair, M., Jeziorowska, D., Reznik, Y., Béréziat, V., et al. (2011) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-2234 · Cited by 48
Self-citationA pathway linking oxidative stress and the Ran GTPase system in progeria
Datta, S., Snow, C. J., & Paschal, B. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0430 · Cited by 47
“LPV is used clinically to inhibit the HIV protease, but it also inhibits Zmpste24, the protease responsible for proteolytic processing of pre–lamin A (Caron et al., 2007; Coffinier et al., 2007; Lefèvre et al., 2010).”
MethodA-type lamins and Hutchinson-Gilford progeria syndrome: pathogenesis and therapy
Jose, M. G. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/216 · Cited by 47
“Cellular senescence is also increased by treatment with inhibitors of the human immunodeficiency virus protease that also inhibit Zmpste24, resulting in accumulation of farnesylated prelamin A (93).”
BackgroundSenolytics: Potential for Alleviating Diabetes and Its Complications
Palmer, A. K., Tchkonia, T., & Kirkland, J. L. (2021) · Endocrinology · doi:10.1210/endocr/bqab058 · Cited by 50
“Similarly, individuals with some progeroid syndromes such as those associated with lamin-A (LMNA) mutations, which involve increased senescent cell burden, are also associated with lipodystrophy, metabolic syndrome, and diabetes (21, 22).”
BackgroundNuclear damages and oxidative stress: new perspectives for laminopathies
Lattanzi, G., Marmiroli, S., Facchini, A., & Maraldi, N. M. (2012) · European Journal of Histochemistry · doi:10.4081/ejh.2012.e45 · Cited by 45
Pellegrini, C., Columbaro, M., Schena, E., Prencipe, S., Andrenacci, D., Iozzo, P., Guzzardi, M. A., Capanni, C., Mattioli, E., Loi, M., et al. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0289-0 · Cited by 44
The R439C mutation in LMNA causes lamin oligomerization and susceptibility to oxidative stress
Verstraeten, V. L. R. M., Caputo, S. M., Steensel, M. A. M. V., Duband‐Goulet, I., Zinn‐Justin, S., Kamps, M. A. F., Kuijpers, H. J. H., Östlund, C., Worman, H. J., Briedé, J. J., et al. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00690.x · Cited by 43
“In particular, high levels of ROS, mostly produced by the mitochondria, were encountered in fibroblasts from patients with an LMNA-associated lipodystrophy [13].”
InfluentialDeng, W., Baki, L., Yin, J., Zhou, H., & Baumgarten, C. M. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.08.013 · Cited by 43
Auclair, M., Afonso, P., Capel, E., Caron-Debarle, M., & Capeau, J. (2014) · Antiviral Therapy · doi:10.3851/imp2752 · Cited by 42
“Senescence Cell senescence was evaluated by the senescenceassociated (SA)-b-galactosidase activity, the protein expression of the senescence markers phospho-p53, p21WAF-1 and p16INK4, and the accumulation of prelamin A, as described previously [29,34].”
MethodSelf-citationA nuclear lamina‐chromatin‐Ran GTPase axis modulates nuclear import and DNA damage signaling
Dworak, N. M., Mąkosa, D., Chatterjee, M., Jividen, K., Yang, C., Snow, C. J., Simke, W. C., Johnson, I. G., Kelley, J. B., & Paschal, B. M. (2018) · Aging Cell · doi:10.1111/acel.12851 · Cited by 41
“LPV treatment results in the accumulation of unprocessed, nuclear membrane‐tethered preLamin A (Caron et al., 2007).”
BackgroundSenescent cells at the crossroads of aging, disease, and tissue homeostasis
Kuehnemann, C., & Wiley, C. D. (2023) · Aging Cell · doi:10.1111/acel.13988 · Cited by 44
“…are treated with the HIV PIs indinavir or nelfinavir, or a combination of atazanavir and ritonavir, they accumulate prelamin A and senescence phenotypes (Caron et al., 2007; Kuehnemann et al., 2023), potentially linking these therapies to senescent cells associated with progeroid disorders.”
BackgroundMutations in LMNA Modulate the Lamin A - Nesprin-2 Interaction and Cause LINC Complex Alterations
Liu, Y., Munck, M., Swaminathan, K., Kapinos, L. E., Noegel, A. A., & Neumann, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071850 · Cited by 46
de Eguino, G. R., Infante, A., Schlangen, K., Aransay, A. M., Fullaondo, A., Soriano‐Navarro, M., García‐Verdugo, J. M., Martín, Á. G., & Rodrı́guez, C. I. (2012) · Stem Cells Translational Medicine · doi:10.5966/sctm.2011-0010 · Cited by 40
Prelamin A processing, accumulation and distribution in normal cells and laminopathy disorders
Casasola, A., Scalzo, D., Nandakumar, V., Halow, J. M., Targa, F. R., Groudine, M. T., & Rincón‐Arano, H. (2016) · Nucleus · doi:10.1080/19491034.2016.1150397 · Cited by 39
“The antibody described here is also a particularly useful tool for the study of prelamin A in progeroid laminopathies, metabolic laminopathies and lipodystrophies.(33,54,57,58,67) Several reports support the involvement of farnesylated prelamin A in these disorders.”
Vigouroux, C., Guénantin, A.-C., Vatier, C., Capel, É., Dour, C. L., Afonso, P., Bidault, G., Béréziat, V., Lascols, O., Capeau, J., et al. (2018) · Nucleus · doi:10.1080/19491034.2018.1456217 · Cited by 42
Self-citationGalant, D., Gaborit, B., Desgrouas, C., Abdesselam, I., Bernard, M., Lévy, N., Merono, F., Coirault, C., Roll, P., Lagarde, A., et al. (2016) · Cells · doi:10.3390/cells5020021 · Cited by 38
“Nevertheless, we showed that the patient’s cells exhibit accelerated senescence and that the senescence rate is similar to the rate observed for fibroblasts carrying the R482W LMNA mutation, responsible for the FPL Dunnigan Type [27].”
ResultGorwood, J., Ejlalmanesh, T., Bourgeois, C., Mantecon, M., Rose, C., Atlan, M., Desjardins, D., Grand, R. L., Fève, B., Lambotte, O., et al. (2020) · Cells · doi:10.3390/cells9040854 · Cited by 40
“First generation PIs induced cellular senescence in fibroblasts [17], endothelial cells [56–58], and in smooth muscle cells [15].”
BackgroundSelf-citationWhat the Genetics of Lipodystrophy Can Teach Us About Insulin Resistance and Diabetes
Vatier, C., Bidault, G., Briand, N., Guénantin, A.-C., Salle-Teyssières, L., Lascols, O., Capeau, J., & Vigouroux, C. (2013) · Current Diabetes Reports · doi:10.1007/s11892-013-0431-7 · Cited by 37
Self-citationPrelamin A is involved in early steps of muscle differentiation
Capanni, C., Coco, R. D., Squarzoni, S., Columbaro, M., Mattioli, E., Camozzi, D., Rocchi, A., Scotlandi, K., Maraldi, N. M., Foisner, R., et al. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.09.026 · Cited by 37
The Cutting Edge: The Role of mTOR Signaling in Laminopathies
Chiarini, F., Evangelisti, C., Cenni, V., Fazio, A., Paganelli, F., Martelli, A. M., & Lattanzi, G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040847 · Cited by 36
“gov/pmc/articles/PMC6412338/ 22/48 At the molecular level, FPLD2, MADA, and MADB are also characterized by accumulation of prelamin A at the nuclear periphery [66,126].”
BackgroundLacombe, M., Lamarche, F., Wever, O. D., Padilla‐Benavides, T., Carlson, A., Khan, I., Huna, A., Vacher, S., Calmel, C., Desbourdes, C., et al. (2021) · BMC Biology · doi:10.1186/s12915-021-01155-5 · Cited by 35
Oldenburg, A. R., Delbarre, E., Thiede, B., Vigouroux, C., & Collas, P. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt509 · Cited by 36
“Disruption of the lamin A–FXR1P interaction by the R482W mutation, and displacement of FXR1P from the nucleus in FPLD2 cells, could be due to pre-lamin A expression in these cells (46,47) and steric inhibition of mature lamin A-FXR1P interaction at the NE.”
BackgroundSelf-citationWarburg effect linked to cognitive‐executive deficits in FMR1 premutation
Napoli, E., Song, G., Schneider, A., Hagerman, R. J., Eldeeb, M. A. A. A., Azarang, A., Tassone, F., & Giulivi, C. (2016) · The FASEB Journal · doi:10.1096/fj.201600315r · Cited by 34
“In this regard,mitochondrial defects have been reported in carriers of lamin A pathogenic mutations along with increased oxidative stress, decreased DNA repair response, and premature cellular aging (87, 88), similar to the lamin A/C dysregulation reported in carriers of the premutation (89).”
BackgroundBone imaging findings in genetic and acquired lipodystrophic syndromes: an imaging study of 24 cases
Teboul-Coré, S., Rey-Jouvin, C., Miquel, A., Vatier, C., Capeau, J., Robert, J., Pham, T., Lascols, O., Berenbaum, F., Larédo, J.-D., et al. (2016) · Skeletal Radiology · doi:10.1007/s00256-016-2457-9 · Cited by 33
“Interestingly, we observed in our study that patients with FPLD had frequently non-specific degenerative joint and tendons abnormalities, which could be favored by insulin resistance and diabetes and/or by the premature cellular senescence associated with LMNA mutations [30].”
BackgroundSelf-citationCaron, M., Vigouroux, C., Bastard, J., & Capeau, J. (2008) · PPAR Research · doi:10.1155/2009/507141 · Cited by 32
“When going further into the mechanism of PI action, we and others demonstrated that some PIs prevented the maturation of lamin A/C [22, 34, 78], a nuclear membrane protein essential for normal nuclear membrane folding and for nuclear penetration of SREBP-1 [59, 79, 80].”
BackgroundSelf-citationKandert, S., Wehnert, M. S., Müller, C. R., Buendia, B., & Dabauvalle, M. (2009) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2009.06.002 · Cited by 33
Clark, K. M., Jenkins, J. L., Fedoriw, N., & Dumont, M. E. (2016) · Protein Science · doi:10.1002/pro.3074 · Cited by 32
LMNA-linked lipodystrophies: from altered fat distribution to cellular alterations
Bidault, G., Vatier, C., Capeau, J., Vigouroux, C., & Béréziat, V. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110675 · Cited by 30
Self-citationAraújo‐Vilar, D., Victoria, B., González‐Méndez, B., Barreiro, F. J. J., Fernández‐Rodríguez, B., Cereijo, R., Gallego-Escuredo, J. M., Villarroya, F., & Pañeda‐Menéndez, A. (2011) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2011.04208.x · Cited by 31
Nuclear Nox4 interaction with prelamin A is associated with nuclear redox control of stem cell aging
Casciaro, F., Beretti, F., Zavatti, M., McCubrey, J. A., Ratti, S., Marmiroli, S., Follo, M. Y., & Maraldi, T. (2018) · Aging · doi:10.18632/aging.101599 · Cited by 30
“Various studies revealed not only that ROS levels are increased in laminopathy patient cells and during prelamin A accumulation, but also that this increase may be attributed to dysfunctional mitochondria [15-18].”
Kuehnemann, C., Hughes, J. B., Desprez, P., Melov, S., Wiley, C. D., & Campisi, J. (2022) · Aging Cell · doi:10.1111/acel.13750 · Cited by 27
Keratins Are Altered in Intestinal Disease-Related Stress Responses
Helenius, T. O., Antman, C., Asghar, M. N., Nyström, J. H., & Toivola, D. M. (2016) · Cells · doi:10.3390/cells5030035 · Cited by 30
“Glial fibrillary acidic protein (GFAP) is upregulated in the oxidative stress reaction in response to brain injury [57], vimentin is three-fold upregulated in senescent fibroblasts [58] and lamin A is upregulated and accumulated in premature cellular senescence [59].”
BackgroundDominici, S., Fiori, V., Magnani, M., Schena, E., Capanni, C., Camozzi, D., D’Apice, M., Dour, C. L., Auclair, M., Caron, M., et al. (2009) · European Journal of Histochemistry · doi:10.4081/ejh.2009.e6 · Cited by 28
“Moreover, they can be used to monitor the effects of drugs acting on prelamin A processing, which are potential therapeutic tools in laminopathies featuring prelamin A accumulation (Caron et al., 2007) and in cancer therapy (Adjei et al., 2000; Ramirez et al., 2007).”
InfluentialSelf-citationPrelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells
Lattanzi, G. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110657 · Cited by 27
Kristiani, L., & Kim, Y. (2023) · Cells · doi:10.3390/cells12091234 · Cited by 26
“The expression of cytochrome c oxidase subunit II (COX 2) is drastically decreased in human fibroblasts and adipocytes bearing lamin A variants, which lowers mitochondrial membrane potential and generates excessive ROS [34].”
Background
Metadata
- Authors
- Caron, M., Auclair, M., Donadille, B., Béréziat, V, Guerci, B., Laville, M., Narbonne, H., Bodemer, C., Lascols, O., Capeau, J., & Vigouroux, C.
- Affiliations
- Inserm (FR)
- Centre Hospitalier Régional et Universitaire de Nancy (FR)
- Hospices Civils de Lyon (FR)
- Assistance Publique Hôpitaux de Marseille (FR)
- Hôpital Necker-Enfants Malades (FR)
- Corresponding author
- Caron, M
- Venue
- Cell Death & Differentiation
- Published
- 2007-07-06
- Volume
- 14
- Issue
- 10
- Pages
- 1759-1767
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- OpenAlex
- W1979927283
- Cited by
- 226
- References
- 45
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 5 · 2023: 8 · 2022: 12 · 2021: 33 · 2020: 8 · 2019: 7 · 2018: 7 · 2017: 9 · 2016: 15 · 2015: 9 · 2014: 12 · 2013: 17 · 2012: 10
- FWCI
- 6.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Death and Differentiation (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Styrelsen för Internationellt Utvecklingssamarbete
- Sidaction
- European Commission
- Institut National de la Santé et de la Recherche Médicale
- Servier
- 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
- Health Sciences › Medicine › Infectious Diseases › HIV-related health complications and treatments
- Keywords
- lipodystrophy, LMNA mutations, A-type lamins, HIV protease inhibitors, oxidative stress, premature aging, farnesylation, p16, mitochondrial respiratory chain, nuclear abnormalities, fibroblasts, adipose tissue
- MeSH terms
- Adult, Biopsy, Cells, Cultured, Child, Female, Fibroblasts, Humans, Middle Aged, Mitochondria, Mutation, Nuclear Proteins, Protein Precursors, Cellular Senescence, HIV Protease Inhibitors, Reactive Oxygen Species, Oxidative Stress, Indinavir, Nelfinavir, Cyclin-Dependent Kinase Inhibitor p16, Lamin Type A, Cyclin-Dependent Kinase Inhibitor p21, Lipodystrophy, Familial Partial, Cell Nucleus Shape
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