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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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“Similarly, it has been shown that human skin fibroblasts isolated from lipodystrophy syndrome patients with LMNA mutations have increased p16 and p21 expression, leading to senescence with increasing cellular passages (32).”
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“It has been previously observed that FPLD, HGPS, and RD cells are characterized by a “ROS-generating environment” [3,4], a peculiar metabolic status also detected in lamin A/C depleted cells [15,16].”
BackgroundThe nuclear envelope and its involvement in cellular stress responses
Malhas, A. N., & Vaux, D. J. (2011) · Biochemical Society Transactions · doi:10.1042/bst20110719 · Cited by 18
“Elevated levels of ROS have also been reported in fibroblasts from lipodystrophy patients with LMNA mutations and cells in which prelamin A accumulation is induced using HIV protease inhibitors [12].”
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“In agreement with earlier reports [33,34], we observed a high percentage of FPLD patient cells containing grossly mis-shaped nuclei with invaginations and/ or blebs, which were also apparent by staining with general lamin A/C antibodies (data not shown) or Hoechst DNA staining (Figure S2A).”
ResultA Clinical Guide to Monogenic Diabetes
Carmody, D., Støy, J., Greeley, S. A. W., Bell, G. I., & Philipson, L. H. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800892-8.00002-6 · Cited by 18
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“FPLD2 results from missense mutations in the lamin A/C gene (LMNA).(1,6) Symptoms usually start in late childhood or at puberty with gradual loss of subcutaneous fat in the extremities, anterior chest, and abdomen; accumulation of fat in the face, chin, neck, and vulva; and muscular hypertrophy of the calves.”
BackgroundIgnatieva, E. V., Ivanova, O. A., Sorokina, M. Y., Khromova, N. V., Polev, D. E., Kostareva, A. A., Sergushichev, A., & Dmitrieva, R. I. (2020) · Genes · doi:10.3390/genes11091057 · Cited by 19
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BackgroundModulation of muscle redox and protein aggregation rescues lethality caused by mutant lamins
Coombs, G. S., Rios-Monterrosa, J. L., Lai, S., Dai, Q., Goll, A. C., Ketterer, M. R., Valdes, M. F., Uche, N., Benjamin, I. J., & Wallrath, L. L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102196 · Cited by 20
Integrated High-Content Quantification of Intracellular ROS Levels and Mitochondrial Morphofunction
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“Although no reported in DCM, CDKN1A is implicated in LMNA-mediated cellular stress responses, and the mutation of LMNA is one of the important mechanisms DCM (50, 51).”
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“The saquinavir family of HIV aspartyl PIs, including lopinavir and atazanavir, can affect the physiological maturation of prelamin A to lamin A, a key structural component of the nuclear lamina, at least in part through inhibition of the zinc metalloprotease ZMPSTE24 and possibly through other mechanisms.(31,32) This…”
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“Ex vivo analyses have previously been performed on adipose tissue from patients being treated with indinavir or nelfinavir regimens who presented with abnormal fat repartition (ART mean duration: 3 years, [36,37]).”
InfluentialBelo, S., Magalhães, Â., Freitas, P., & Carvalho, D. M. (2015) · BMC Research Notes · doi:10.1186/s13104-015-1065-4 · Cited by 16
“the premature death of adipocytes [17-19].”
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Age-Related Lipid Metabolic Signature in Human LMNA -Lipodystrophic Stem Cell-Derived Adipocytes
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“Even if the recent hypothesis of the miRNA-related heterochromatin alterations is gaining more relevance, we have to take into account that this was demonstrated only for the R482W variant [21], and it cannot be ruled out that the accumulation of immature prelamin altering adipogenesis by sequestering certain transcri…”
BackgroundBone mineral density in familial partial lipodystrophy
Fernández‐Pombo, A., Ossandon‐Otero, J. A., Guillín‐Amarelle, C., Sánchez‐Iglesias, S., Castro, A. I., González‐Méndez, B., Rodríguez‐García, S., Rodríguez‐Cañete, L., Casanueva, F. F., & Araújo‐Vilar, D. (2017) · Clinical Endocrinology · doi:10.1111/cen.13504 · Cited by 13
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“In recent years, several groups performed protein gel blots on FPLD fibroblasts with commercial antibodies and concluded that FPLD mutations (including the classic R482W mutation) are associated with an accumulation of prelamin A.(6,22-24) These reports were intriguing, but we reasoned that caution was warranted.”
BackgroundLipodystrophy: beyond generalization?
Freitas, P., & Carvalho, D. M. (2013) · PubMed · Cited by 11
Lamines A et syndromes progéroïdes
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Enhanced cell viscosity: A new phenotype associated with lamin A/C alterations
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“…(1) the canonical FPLD2-associated lamin A/C R482W pathogenic variant and (2) an in vitro treatment with Atazanavir, a HIV protease inhibitor known to induce senescence phenotypes associated to lamin A/C alterations (Caron et al., 2007; Bonello-Palot et al., 2014; López-Otín et al., 2013).”
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“In one study (32), prelamin A was detected”
BackgroundTranscriptomic study reveals changes of lncRNAs in PBMCs from HIV-1 patients before and after ART
Zhou, Y., Huang, Y., Chen, X., Chen, T., Hu, W., Hou, W., Zhang, Q., & Xiong, Y. (2023) · Scientific Reports · doi:10.1038/s41598-023-49595-z · Cited by 8
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“p16 is induced in multiple contexts associated with enhanced prelamin A expression [42, 47, 49, 56, 57], as is induction of p53 [19, 58].”
BackgroundOverview of cellular homeostasis-associated nuclear envelope lamins and associated input signals
Kim, H. J., Lee, P. C.-W., & Hong, J. H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1173514 · Cited by 8
“Human fibroblasts with LMNA, LMNA, LMNA, LMNA, LMNA, and LMNA, which accumulate prelamin-A, also enhance oxidative stress and mediate premature features (Caron et al., 2007).”
BackgroundLaminopathy-inducing mutations reduce nuclear import of expressed prelamin A
Kiel, T., Busch, A., Meyer-Rachner, A., & Hubner, S. E. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.035 · Cited by 7
Long‐term expression of the lamin A mutant associated with dilated cardiomyopathy induces senescence
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“…that the p53 and p16INK4a–pRb pathways are involved in the premature senescence of fibroblasts derived from progeria and lipodystrophy patients (Caron et al. 2007; Kudlow et al. 2008), to the best of our knowledge, this is the first study to show that mutant lamin A associated with FDC…”
BackgroundTanaka, T., Nakazawa, H., Kuriyama, N., & Kaneki, M. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.5526 · Cited by 7
“ZMPSTE 24 is the key enzyme in the maturation of prelamin A, which is encoded by the LMNA gene and some mutations in the LMNA or ZMPSTE 24 gene cause lipodystrophy and premature aging syndrome such as Hutchinson‑Gilford progeria syndrome (HGPS) (14,15).”
Impaired differentiation of small airway basal stem/progenitor cells in people living with HIV
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Freitas, P., Carvalho, D. M., Souto, S. B., Sarmento, A., & Luis, J. (2013) · InTech eBooks · doi:10.5772/52685 · Cited by 5
“PIs may cause lipodystrophy by inhibiting ZMPSTE24, resulting in accumulation of tox‐ ic farnesylated prelamin A [128], increased oxidative stress and altered adipokine and cyto‐ kine production [89, 127, 129].”
BackgroundPathologically Relevant Prelamin A Interactions with Transcription Factors
Infante, A., & Rodrı́guez, C. I. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.08.032 · Cited by 6
“Current knowledge comes largely from cultured fibroblasts derived from accessible tissue such as skin biopsies (Caron et al., 2007).”
BackgroundGenetic Testing in Diabetes Mellitus
Philipson, L. H., Murphy, R., Ellard, S., Hattersley, A. T., Støy, J., Greeley, S. A. W., Bell, G. I., & Polonsky, K. S. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374430-2.00002-x · Cited by 6
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“As prelamin A tends to accumulate in FPLD2 cells [10,11,31,35], we analyzed MR fate in the presence of LA-C661M encoding the full-length unprocessable prelamin A, which is accumulated in the nuclear lamina as non-farnesylated prelamin A, or LA-L647R, which encodes an uncleavable permanently…”
BackgroundIvanova, O. A., Predeus, A. V., Sorokina, M. Y., Ignatieva, E. V., Bobkov, D. E., Сухарева, К. С., Kostareva, A. A., & Dmitrieva, R. I. (2025) · Scientific Reports · doi:10.1038/s41598-025-88219-6 · Cited by 4
Capeau, J. (2011) · Bulletin de l Académie Nationale de Médecine · doi:10.1016/s0001-4079(19)31893-x · Cited by 4
Self-citationProteolysis targeting chimeras as senolytics: An emerging senotherapy for combating aging
Cruickshank-Taylor, A. B., Kozora, J. S., Carew, J. S., Nawrocki, S. T., & Wang, W. (2025) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2025.103752 · Cited by 4
The tripartite architecture of the eukaryotic integral membrane protein zinc metalloprotease Ste24
Goblirsch, B. R., Pryor, E. E., & Wiener, M. C. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25841 · Cited by 4
“Deficiencies in HsSte24 activity, whether by mutation(18,21,22) or inhibition,(23,24) restrict prelamin A maturation and lead to disease states known as laminopathies, which range from progerias (premature aging syndrome) to lipodystrophies.(25,26) Inhibition of HsSte24”
BackgroundHutchinson-Gilford progeria syndrome cardiovascular disease and oxidative stress
Andrés, V. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/s226 · Cited by 4
Adipose tissue aging partially accounts for fat alterations in HIV lipodystrophy
Domingo, P., Giralt, M., Gavaldà‐Navarro, A., Blasco‐Roset, A., Delgado‐Anglés, A., Gallego-Escuredo, J. M., Gutiérrez, M. D. M., Mateo, G. M., Cereijo, R., Domingo, J. C., et al. (2022) · Adipocyte · doi:10.1080/21623945.2022.2042962 · Cited by 3
“Increased levels of p16 was reported in adipose tissue from four HIV patients with lipodystrophy treated with protease inhibitor-type antiretroviral drugs [33].”
BackgroundSeguret, M., Jouve, C., Ruiz‐Velasco, A., Deshayes, L., Guesmia, Z., Pereira, C., Wahbi, K., Fauconnier, J., Bonne, G., Muchir, A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.21.609073 · Cited by 3
Effect of β-Estradiol on Adipogenesis in a 3T3-L1 Cell Model of Prelamin A Accumulation
Cobelo-Gómez, S., Sánchez‐Iglesias, S., Fernández‐Pombo, A., & Araújo‐Vilar, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021282 · Cited by 2
“Thus, given that fat loss appears in women after puberty, affecting anatomical areas dependent on sex hormones (limbs and buttocks) [14] and, on the other hand, many women adopt an android pattern of fat distribution after menopause [10–12], it is appealing to hypothesize that female sexual…”
BackgroundPlasma Proteomic Signature as a Predictor of Age Advancement in People Living With HIV
Navas, A., Matzaraki, V., van Eekeren, L. E., Blaauw, M. J. T., Groenendijk, A. L., Vos, W. A. J. W., Cleophas, M. C. P., dos Santos, J. C., van der Ven, A. J. A. M., Joosten, L. A. B., et al. (2025) · Aging Cell · doi:10.1111/acel.14468 · Cited by 3
Cardiac phenotypes in LMNA mutations
Rouhi, L. (2025) · Current Opinion in Cardiology · doi:10.1097/hco.0000000000001209 · Cited by 2
DNA repair-related genes and adipogenesis: Lessons from congenital lipodystrophies
Campos, J. T. A. D. M., de Oliveira, M. S., Soares, L. P., de Medeiros, K. A., Campos, L. R. D. S., & Lima, J. G. (2022) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2022-0086 · Cited by 3
“The LMNA gene and FPLD2 The link between changes in redox homeostasis, cell cycle, and senescence was investigated in fibroblasts from FPLD2 subjects carrying the pathogenic variants p.D47Y, p.L92F, p.L387V, p.R399H, p.L421P, and p.R482W in the LMNA genes (Caron et al., 2007).”
Restored lncRNAs After ART Therapy Have Potential Key Roles in the Recovery From AIDSPreprint
Zhou, Y., Huang, Y., Chen, T., Hu, W., Chen, X., Hou, W., Zhang, Q., & Xiong, Y. (2021) · Research Square · doi:10.21203/rs.3.rs-871811/v1 · Cited by 2
Genetic and Acquired Lipodystrophic Syndromes
Vigouroux, C., Béréziat, V., Caron, M., & Capeau, J. (2012) · Springer eBooks · doi:10.1007/978-2-8178-0343-2_25 · Cited by 1
Self-citationA-type lamins and Hutchinson-Gilford progeria syndrome pathogenesis and therapy
Andrés, V. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/s216 · Cited by 2
Pathogenesis of Antiretroviral Treatment-Associated Metabolic Syndrome
Capeau, J., Caron, M., & Boccara, F. (2009) · Springer eBooks · doi:10.1007/978-88-470-0761-1_3 · Cited by 1
Self-citationWondimnew, T., Genet, S., & Gnanasekaran, N. (2021) · Free Radicals and Antioxidants · doi:10.5530/fra.2020.2.14 · Cited by 1
Till Disassembly Do Us Part: A Happy Marriage of Nuclear Envelope and Chromatin
Tsuchiya, Y. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm219 · Cited by 1
Une brève histoire des laminopathies
Vigouroux, C., Lascols, O., Béréziat, V., Dour, C. L., Hernàndez-Vallejo, S. J., Caron, M., & Capeau, J. (2008) · Médecine des Maladies Métaboliques · doi:10.1016/s1957-2557(08)74038-0 · Cited by 1
Self-citationSyndromes lipodystrophiques génétiques et acquis
Vigouroux, C., Béréziat, V., Caron, M., & Capeau, J. (2013) · Springer eBooks · doi:10.1007/978-2-8178-0332-6_25
Self-citationVigouroux, C., Bidault, G., & Capeau, J. (2013) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0024915
Self-citationVigouroux, C., Caron, M., Bastard, J., Boccara, F., & Capeau, J. (2008) · Médecine des Maladies Métaboliques · doi:10.1016/s1957-2557(08)74920-4
Self-citationUne farnésylation persistante aux conséquences dramatiques
Navarro, C. L., Poitelon, Y., & Lévy, N. (2008)
Barros, S. D. (2007) · OpenGrey (Institut de l'Information Scientifique et Technique)
Vigouroux, C., & Capeau, J. (2009) · EMC - Endocrinologie - Nutrition · doi:10.1016/s1155-1941(09)51223-1
Self-citationMolecular dissection of A-type lamin-regulated pathways
Corne, T. (2017) · Ghent University Academic Bibliography (Ghent University)
Mammalian Farnesylated Protein-Converting Enzyme 1
Young, S. G., Coffinier, C., Jung, H.-J., & Fong, L. G. (2012) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00142-3
Nucleocytoplasmic Communication in Progeria
Snow, C. J. (2014) · doi:10.18130/v3k522
Maraldi, N. M., & Lattanzi, G. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-788-0_18
Cellular Defects in Hutchinson-Gilford Progeria Syndrome
Datta, S. (2013) · doi:10.18130/v3kv4q
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Redox Homeostasis and Nitro-Oxidative Stress in Obesity-Linked InflammationPreprint
Treiber, G., Samouda, H., Nobécourt, E., & Bottari, S. P. (2022) · Preprints.org · doi:10.20944/preprints202202.0180.v2
Lacombe, M., Lamarche, F., Wever, O. D., Padilla‐Benavides, T., Carlson, A., Khan, I., Huna, A., Vacher, S., Calmel, C., Desbourdes, C., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16851126
Lacombe, M., Lamarche, F., Wever, O. D., Padilla‐Benavides, T., Carlson, A., Khan, I., Huna, A., Vacher, S., Calmel, C., Desbourdes, C., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16851066
Karthik, V., Basheer, S., Jabbar, P. K., & Gomez, R. (2024) · BMJ Case Reports · doi:10.1136/bcr-2024-262102
“6 Interestingly, our patient’s parents, who were heterozygous for the mutation, did not exhibit any features of premature ageing.”
Lacombe, M., Lamarche, F., Wever, O. D., Padilla‐Benavides, T., Carlson, A., Khan, I., Huna, A., Vacher, S., Calmel, C., Desbourdes, C., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16851102
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Lacombe, M., Lamarche, F., Wever, O. D., Padilla‐Benavides, T., Carlson, A., Khan, I., Huna, A., Vacher, S., Calmel, C., Desbourdes, C., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16851156
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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