Identification of mitochondrial dysfunction in Hutchinson–Gilford progeria syndrome through use of stable isotope labeling with amino acids in cell culture
Hutchinson–Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of l...
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| Published in | Journal of proteomics Vol. 91; pp. 466 - 477 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
08.10.2013
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| Online Access | Get full text |
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| Abstract | Hutchinson–Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of lamin A that lacks 50 amino acids and retains a toxic farnesyl modification in its carboxy-terminus. However, the mechanisms underlying cellular damage and senescence and accelerated aging in HGPS are incompletely understood. Here, we analyzed fibroblasts from healthy subjects and HGPS patients using SILAC (stable isotope labeling with amino acids in cell culture). We found in HGPS cells a marked downregulation of mitochondrial oxidative phosphorylation proteins accompanied by mitochondrial dysfunction, a process thought to provoke broad organ decline during normal aging. We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (LmnaG609G/G609G knock-in mice) or prelamin A (Zmpste24-null mice). Analysis of tissues from these mouse models revealed that the damaging effect of these proteins on mitochondrial function is time- and dose-dependent. Mitochondrial alterations were not observed in the brain, a tissue with extremely low progerin expression that seems to be unaffected in HGPS. Remarkably, mitochondrial function was restored in progeroid mouse fibroblasts treated with the isoprenylation inhibitors FTI-277 or pravastatin plus zoledronate, which are being tested in HGPS clinical trials. Our results suggest that mitochondrial dysfunction contributes to premature organ decline and aging in HGPS. Beyond its effects on progeria, prelamin A and progerin may also contribute to mitochondrial dysfunction and organ damage during normal aging, since these proteins are expressed in cells and tissues from non-HGPS individuals, most prominently at advanced ages.
Mutations in LMNA or defective processing of prelamin A causes premature aging disorders, including Hutchinson–Gilford progeria syndrome (HGPS). Most HGPS patients carry in heterozygosis a de-novo point mutation (c.1824C>T: GGC>GGT; p.G608G) which causes the expression of the lamin A mutant protein called progerin. Despite the importance of progerin and prelamin A in accelerated aging, the underlying molecular mechanisms remain largely unknown. To tackle this question, we compared the proteome of skin-derived dermal fibroblast from HGPS patients and age-matched controls using quantitative stable isotope labeling with amino acids in cell culture (SILAC). Our results show a pronounced down-regulation of several components of the mitochondrial ATPase complex accompanied by up-regulation of some glycolytic enzymes. Accordingly, functional studies demonstrated mitochondrial dysfunction in HGPS fibroblasts. Moreover, our expression and functional studies using cellular and animal models confirmed that mitochondrial dysfunction is a feature of progeria which develops in a time- and dose-dependent manner. Finally, we demonstrate improved mitochondrial function in progeroid mouse cells treated with a combination of statins and aminobisphosphonates, two drugs that are being evaluated in ongoing HGPS clinical trials. Although further studies are needed to unravel the mechanisms through which progerin and prelamin A provoke mitochondrial abnormalities, our findings may pave the way to improved treatments of HGPS. These studies may also improve our knowledge of the mechanisms leading to mitochondrial dysfunction during normal aging, since both progerin and prelamin A have been found to accumulate during normal aging.
[Display omitted]
•SILAC analysis identifies multiple proteomic alterations in HGPS (progeria).•Mitochondrial dysfunction is a pathologic feature of HGPS.•Functional studies confirm mitochondrial defects in progeroid mouse models.•Statin+zoledronate ameliorate mitochondrial defects in HGPS mouse models. |
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| AbstractList | Hutchinson–Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of lamin A that lacks 50 amino acids and retains a toxic farnesyl modification in its carboxy-terminus. However, the mechanisms underlying cellular damage and senescence and accelerated aging in HGPS are incompletely understood. Here, we analyzed fibroblasts from healthy subjects and HGPS patients using SILAC (stable isotope labeling with amino acids in cell culture). We found in HGPS cells a marked downregulation of mitochondrial oxidative phosphorylation proteins accompanied by mitochondrial dysfunction, a process thought to provoke broad organ decline during normal aging. We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (LmnaG609G/G609G knock-in mice) or prelamin A (Zmpste24-null mice). Analysis of tissues from these mouse models revealed that the damaging effect of these proteins on mitochondrial function is time- and dose-dependent. Mitochondrial alterations were not observed in the brain, a tissue with extremely low progerin expression that seems to be unaffected in HGPS. Remarkably, mitochondrial function was restored in progeroid mouse fibroblasts treated with the isoprenylation inhibitors FTI-277 or pravastatin plus zoledronate, which are being tested in HGPS clinical trials. Our results suggest that mitochondrial dysfunction contributes to premature organ decline and aging in HGPS. Beyond its effects on progeria, prelamin A and progerin may also contribute to mitochondrial dysfunction and organ damage during normal aging, since these proteins are expressed in cells and tissues from non-HGPS individuals, most prominently at advanced ages.Mutations in LMNA or defective processing of prelamin A causes premature aging disorders, including Hutchinson–Gilford progeria syndrome (HGPS). Most HGPS patients carry in heterozygosis a de-novo point mutation (c.1824C>T: GGC>GGT; p.G608G) which causes the expression of the lamin A mutant protein called progerin. Despite the importance of progerin and prelamin A in accelerated aging, the underlying molecular mechanisms remain largely unknown. To tackle this question, we compared the proteome of skin-derived dermal fibroblast from HGPS patients and age-matched controls using quantitative stable isotope labeling with amino acids in cell culture (SILAC). Our results show a pronounced down-regulation of several components of the mitochondrial ATPase complex accompanied by up-regulation of some glycolytic enzymes. Accordingly, functional studies demonstrated mitochondrial dysfunction in HGPS fibroblasts. Moreover, our expression and functional studies using cellular and animal models confirmed that mitochondrial dysfunction is a feature of progeria which develops in a time- and dose-dependent manner. Finally, we demonstrate improved mitochondrial function in progeroid mouse cells treated with a combination of statins and aminobisphosphonates, two drugs that are being evaluated in ongoing HGPS clinical trials. Although further studies are needed to unravel the mechanisms through which progerin and prelamin A provoke mitochondrial abnormalities, our findings may pave the way to improved treatments of HGPS. These studies may also improve our knowledge of the mechanisms leading to mitochondrial dysfunction during normal aging, since both progerin and prelamin A have been found to accumulate during normal aging. Hutchinson-Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of lamin A that lacks 50 amino acids and retains a toxic farnesyl modification in its carboxy-terminus. However, the mechanisms underlying cellular damage and senescence and accelerated aging in HGPS are incompletely understood. Here, we analyzed fibroblasts from healthy subjects and HGPS patients using SILAC (stable isotope labeling with amino acids in cell culture). We found in HGPS cells a marked downregulation of mitochondrial oxidative phosphorylation proteins accompanied by mitochondrial dysfunction, a process thought to provoke broad organ decline during normal aging. We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (Lmna(G609G/G609G) knock-in mice) or prelamin A (Zmpste24-null mice). Analysis of tissues from these mouse models revealed that the damaging effect of these proteins on mitochondrial function is time- and dose-dependent. Mitochondrial alterations were not observed in the brain, a tissue with extremely low progerin expression that seems to be unaffected in HGPS. Remarkably, mitochondrial function was restored in progeroid mouse fibroblasts treated with the isoprenylation inhibitors FTI-277 or pravastatin plus zoledronate, which are being tested in HGPS clinical trials. Our results suggest that mitochondrial dysfunction contributes to premature organ decline and aging in HGPS. Beyond its effects on progeria, prelamin A and progerin may also contribute to mitochondrial dysfunction and organ damage during normal aging, since these proteins are expressed in cells and tissues from non-HGPS individuals, most prominently at advanced ages. Mutations in LMNA or defective processing of prelamin A causes premature aging disorders, including Hutchinson-Gilford progeria syndrome (HGPS). Most HGPS patients carry in heterozygosis a de-novo point mutation (c.1824C>T: GGC>GGT; p.G608G) which causes the expression of the lamin A mutant protein called progerin. Despite the importance of progerin and prelamin A in accelerated aging, the underlying molecular mechanisms remain largely unknown. To tackle this question, we compared the proteome of skin-derived dermal fibroblast from HGPS patients and age-matched controls using quantitative stable isotope labeling with amino acids in cell culture (SILAC). Our results show a pronounced down-regulation of several components of the mitochondrial ATPase complex accompanied by up-regulation of some glycolytic enzymes. Accordingly, functional studies demonstrated mitochondrial dysfunction in HGPS fibroblasts. Moreover, our expression and functional studies using cellular and animal models confirmed that mitochondrial dysfunction is a feature of progeria which develops in a time- and dose-dependent manner. Finally, we demonstrate improved mitochondrial function in progeroid mouse cells treated with a combination of statins and aminobisphosphonates, two drugs that are being evaluated in ongoing HGPS clinical trials. Although further studies are needed to unravel the mechanisms through which progerin and prelamin A provoke mitochondrial abnormalities, our findings may pave the way to improved treatments of HGPS. These studies may also improve our knowledge of the mechanisms leading to mitochondrial dysfunction during normal aging, since both progerin and prelamin A have been found to accumulate during normal aging. Hutchinson-Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of lamin A that lacks 50 amino acids and retains a toxic farnesyl modification in its carboxy-terminus. However, the mechanisms underlying cellular damage and senescence and accelerated aging in HGPS are incompletely understood. Here, we analyzed fibroblasts from healthy subjects and HGPS patients using SILAC (stable isotope labeling with amino acids in cell culture). We found in HGPS cells a marked downregulation of mitochondrial oxidative phosphorylation proteins accompanied by mitochondrial dysfunction, a process thought to provoke broad organ decline during normal aging. We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (LmnaG609G/G609G knock-in mice) or prelamin A (Zmpste24-null mice). Analysis of tissues from these mouse models revealed that the damaging effect of these proteins on mitochondrial function is time- and dose-dependent. Mitochondrial alterations were not observed in the brain, a tissue with extremely low progerin expression that seems to be unaffected in HGPS. Remarkably, mitochondrial function was restored in progeroid mouse fibroblasts treated with the isoprenylation inhibitors FTI-277 or pravastatin plus zoledronate, which are being tested in HGPS clinical trials. Our results suggest that mitochondrial dysfunction contributes to premature organ decline and aging in HGPS. Beyond its effects on progeria, prelamin A and progerin may also contribute to mitochondrial dysfunction and organ damage during normal aging, since these proteins are expressed in cells and tissues from non-HGPS individuals, most prominently at advanced ages. Hutchinson–Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of lamin A that lacks 50 amino acids and retains a toxic farnesyl modification in its carboxy-terminus. However, the mechanisms underlying cellular damage and senescence and accelerated aging in HGPS are incompletely understood. Here, we analyzed fibroblasts from healthy subjects and HGPS patients using SILAC (stable isotope labeling with amino acids in cell culture). We found in HGPS cells a marked downregulation of mitochondrial oxidative phosphorylation proteins accompanied by mitochondrial dysfunction, a process thought to provoke broad organ decline during normal aging. We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (Lmnaᴳ⁶⁰⁹ᴳ/ᴳ⁶⁰⁹ᴳ knock-in mice) or prelamin A (Zmpste24-null mice). Analysis of tissues from these mouse models revealed that the damaging effect of these proteins on mitochondrial function is time- and dose-dependent. Mitochondrial alterations were not observed in the brain, a tissue with extremely low progerin expression that seems to be unaffected in HGPS. Remarkably, mitochondrial function was restored in progeroid mouse fibroblasts treated with the isoprenylation inhibitors FTI-277 or pravastatin plus zoledronate, which are being tested in HGPS clinical trials. Our results suggest that mitochondrial dysfunction contributes to premature organ decline and aging in HGPS. Beyond its effects on progeria, prelamin A and progerin may also contribute to mitochondrial dysfunction and organ damage during normal aging, since these proteins are expressed in cells and tissues from non-HGPS individuals, most prominently at advanced ages. BIOLOGICAL SIGNIFICANCE: Mutations in LMNA or defective processing of prelamin A causes premature aging disorders, including Hutchinson–Gilford progeria syndrome (HGPS). Most HGPS patients carry in heterozygosis a de-novo point mutation (c.1824C>T: GGC>GGT; p.G608G) which causes the expression of the lamin A mutant protein called progerin. Despite the importance of progerin and prelamin A in accelerated aging, the underlying molecular mechanisms remain largely unknown. To tackle this question, we compared the proteome of skin-derived dermal fibroblast from HGPS patients and age-matched controls using quantitative stable isotope labeling with amino acids in cell culture (SILAC). Our results show a pronounced down-regulation of several components of the mitochondrial ATPase complex accompanied by up-regulation of some glycolytic enzymes. Accordingly, functional studies demonstrated mitochondrial dysfunction in HGPS fibroblasts. Moreover, our expression and functional studies using cellular and animal models confirmed that mitochondrial dysfunction is a feature of progeria which develops in a time- and dose-dependent manner. Finally, we demonstrate improved mitochondrial function in progeroid mouse cells treated with a combination of statins and aminobisphosphonates, two drugs that are being evaluated in ongoing HGPS clinical trials. Although further studies are needed to unravel the mechanisms through which progerin and prelamin A provoke mitochondrial abnormalities, our findings may pave the way to improved treatments of HGPS. These studies may also improve our knowledge of the mechanisms leading to mitochondrial dysfunction during normal aging, since both progerin and prelamin A have been found to accumulate during normal aging. Hutchinson–Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of physiological aging. The disease is caused by a sporadic dominant mutation in the LMNA gene that leads to the expression of progerin, a mutant form of lamin A that lacks 50 amino acids and retains a toxic farnesyl modification in its carboxy-terminus. However, the mechanisms underlying cellular damage and senescence and accelerated aging in HGPS are incompletely understood. Here, we analyzed fibroblasts from healthy subjects and HGPS patients using SILAC (stable isotope labeling with amino acids in cell culture). We found in HGPS cells a marked downregulation of mitochondrial oxidative phosphorylation proteins accompanied by mitochondrial dysfunction, a process thought to provoke broad organ decline during normal aging. We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (LmnaG609G/G609G knock-in mice) or prelamin A (Zmpste24-null mice). Analysis of tissues from these mouse models revealed that the damaging effect of these proteins on mitochondrial function is time- and dose-dependent. Mitochondrial alterations were not observed in the brain, a tissue with extremely low progerin expression that seems to be unaffected in HGPS. Remarkably, mitochondrial function was restored in progeroid mouse fibroblasts treated with the isoprenylation inhibitors FTI-277 or pravastatin plus zoledronate, which are being tested in HGPS clinical trials. Our results suggest that mitochondrial dysfunction contributes to premature organ decline and aging in HGPS. Beyond its effects on progeria, prelamin A and progerin may also contribute to mitochondrial dysfunction and organ damage during normal aging, since these proteins are expressed in cells and tissues from non-HGPS individuals, most prominently at advanced ages. Mutations in LMNA or defective processing of prelamin A causes premature aging disorders, including Hutchinson–Gilford progeria syndrome (HGPS). Most HGPS patients carry in heterozygosis a de-novo point mutation (c.1824C>T: GGC>GGT; p.G608G) which causes the expression of the lamin A mutant protein called progerin. Despite the importance of progerin and prelamin A in accelerated aging, the underlying molecular mechanisms remain largely unknown. To tackle this question, we compared the proteome of skin-derived dermal fibroblast from HGPS patients and age-matched controls using quantitative stable isotope labeling with amino acids in cell culture (SILAC). Our results show a pronounced down-regulation of several components of the mitochondrial ATPase complex accompanied by up-regulation of some glycolytic enzymes. Accordingly, functional studies demonstrated mitochondrial dysfunction in HGPS fibroblasts. Moreover, our expression and functional studies using cellular and animal models confirmed that mitochondrial dysfunction is a feature of progeria which develops in a time- and dose-dependent manner. Finally, we demonstrate improved mitochondrial function in progeroid mouse cells treated with a combination of statins and aminobisphosphonates, two drugs that are being evaluated in ongoing HGPS clinical trials. Although further studies are needed to unravel the mechanisms through which progerin and prelamin A provoke mitochondrial abnormalities, our findings may pave the way to improved treatments of HGPS. These studies may also improve our knowledge of the mechanisms leading to mitochondrial dysfunction during normal aging, since both progerin and prelamin A have been found to accumulate during normal aging. [Display omitted] •SILAC analysis identifies multiple proteomic alterations in HGPS (progeria).•Mitochondrial dysfunction is a pathologic feature of HGPS.•Functional studies confirm mitochondrial defects in progeroid mouse models.•Statin+zoledronate ameliorate mitochondrial defects in HGPS mouse models. |
| Author | Andrés, Vicente Cabezas-Sánchez, Pablo Acín-Perez, Rebeca López-Otín, Carlos Rivera-Torres, José Cámara, Carmen Luque-García, José L. Megias, Diego Osorio, Fernando G. Gonzalez-Gómez, Cristina Enríquez, José Antonio |
| Author_xml | – sequence: 1 givenname: José surname: Rivera-Torres fullname: Rivera-Torres, José email: jrivera@cnic.es organization: Department of Epidemiology, Atherothrombosis and Imaging, Centro Nacional de Investigaciones Cardiovasculares (CNIC), Madrid, Spain – sequence: 2 givenname: Rebeca surname: Acín-Perez fullname: Acín-Perez, Rebeca organization: Department of Cardiovascular Development and Repair, Centro Nacional de Investigaciones Cardiovasculares (CNIC), Madrid, Spain – sequence: 3 givenname: Pablo surname: Cabezas-Sánchez fullname: Cabezas-Sánchez, Pablo organization: Department of Analytical Chemistry, School of Chemical Sciences, Complutense University of Madrid, Madrid, Spain – sequence: 4 givenname: Fernando G. surname: Osorio fullname: Osorio, Fernando G. organization: Departamento de Bioquímica y Biología Molecular, Instituto Universitario de Oncología (IUOPA), Universidad de Oviedo, Oviedo, Spain – sequence: 5 givenname: Cristina surname: Gonzalez-Gómez fullname: Gonzalez-Gómez, Cristina organization: Department of Epidemiology, Atherothrombosis and Imaging, Centro Nacional de Investigaciones Cardiovasculares (CNIC), Madrid, Spain – sequence: 6 givenname: Diego surname: Megias fullname: Megias, Diego organization: Confocal Microscopy Unit, Centro Nacional de Investigaciones Oncológicas (CNIO), Madrid, Spain – sequence: 7 givenname: Carmen surname: Cámara fullname: Cámara, Carmen organization: Department of Analytical Chemistry, School of Chemical Sciences, Complutense University of Madrid, Madrid, Spain – sequence: 8 givenname: Carlos surname: López-Otín fullname: López-Otín, Carlos organization: Departamento de Bioquímica y Biología Molecular, Instituto Universitario de Oncología (IUOPA), Universidad de Oviedo, Oviedo, Spain – sequence: 9 givenname: José Antonio surname: Enríquez fullname: Enríquez, José Antonio organization: Department of Cardiovascular Development and Repair, Centro Nacional de Investigaciones Cardiovasculares (CNIC), Madrid, Spain – sequence: 10 givenname: José L. surname: Luque-García fullname: Luque-García, José L. organization: Department of Analytical Chemistry, School of Chemical Sciences, Complutense University of Madrid, Madrid, Spain – sequence: 11 givenname: Vicente surname: Andrés fullname: Andrés, Vicente email: vandres@cnic.es organization: Department of Epidemiology, Atherothrombosis and Imaging, Centro Nacional de Investigaciones Cardiovasculares (CNIC), Madrid, Spain |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23969228$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | 2013 Elsevier B.V. 2013 Elsevier B.V. All rights reserved. |
| Copyright_xml | – notice: 2013 Elsevier B.V. – notice: 2013 Elsevier B.V. All rights reserved. |
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| DOI | 10.1016/j.jprot.2013.08.008 |
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| Keywords | Molecular biology of aging p70S6K ATP5A1 ATP5C1 OXPHOS ATP5O ENO2 ATP5B Zmpste24 mTOR eIF4 eIF2 FpSDH HGPS Mitochondrial dysfunction Progerin SILAC ATP5F1 COX Lamin A CS MAF PKM Accelerated aging FTI ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 cytochrome c oxidase pyruvate kinase, muscle ATP synthase, H+ transporting, mitochondrial F1 complex, O subunit citrate synthase mammalian target of rapamycin enolase 2 stable isotope labeling with amino acids in cell culture ATP synthase, H+ transporting, mitochondrial F1 complex, gamma polypeptide farnesyltransferase inhibitor Hutchinson–Gilford progeria syndrome zinc metalloproteinase STE24 homolog ribosomal protein S6 kinase, 70kDa, polypeptide 1 mouse adult fibroblast oxidative phosphorylation eukaryotic translation initiation factor 2 eukaryotic translation initiation factor 4 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1 flavoprotein subunit of succinate dehydrogenase |
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| License | 2013 Elsevier B.V. All rights reserved. |
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| Snippet | Hutchinson–Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of... Hutchinson-Gilford progeria syndrome (HGPS) is a rare segmental premature aging disorder that recapitulates some biological and physical aspects of... |
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| SubjectTerms | Accelerated aging Adenosine Triphosphate Adenosine Triphosphate - chemistry Adolescent adults amino acids Amino Acids - chemistry analogs & derivatives animal models Animals brain cell culture chemistry Child clinical trials Diphosphonates Diphosphonates - chemistry drugs Female fibroblasts Fibroblasts - metabolism Galactose Galactose - metabolism Gene Expression Regulation genes Glucose Glucose - chemistry glycolysis H-transporting ATP synthase Humans Hydroxymethylglutaryl-CoA Reductase Inhibitors Hydroxymethylglutaryl-CoA Reductase Inhibitors - chemistry Imidazoles Imidazoles - chemistry isotope labeling Lamin A Lamin Type A Male metabolism Methionine Methionine - analogs & derivatives Methionine - chemistry Mice Mitochondria Mitochondria - metabolism Mitochondria - pathology Mitochondrial dysfunction Molecular biology of aging mutants Mutation Nuclear Proteins Nuclear Proteins - chemistry oxidative phosphorylation Oxygen Consumption pathology patients point mutation Pravastatin Pravastatin - chemistry Progeria Progeria - metabolism Progerin Protein Precursors Protein Precursors - chemistry protein synthesis proteins proteome Proteomics senescence SILAC Skin Skin - metabolism stable isotopes toxicity Zoledronic Acid |
| Title | Identification of mitochondrial dysfunction in Hutchinson–Gilford progeria syndrome through use of stable isotope labeling with amino acids in cell culture |
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