GPMDB00205OtherGueugneau M, et al.InstrumentNot AvailableNot availableHomo_sapiens_viruses, Human_femalebechet.daniel@clermont.inra.fr25532418http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006878http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006879http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006876http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006877http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006870http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006871http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006750http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006874http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006875http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006872http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006873http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006867http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006746http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006868http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006747http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006744http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006865http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006745http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006866http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006748http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006869http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006749http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006860http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006742http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006863http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006864http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006743http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006740http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006861http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006741http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006862http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006713http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006834http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006714http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006835http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006711http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006832http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006712http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006833http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006838http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006717http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006839http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006718http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006836http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006715http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006837http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006716http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006831http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006710http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006719http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006702http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006703http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006706http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006707http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006704http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006705http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006708http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006709http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006856http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006735http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006736http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006857http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006854http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006733http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006734http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006739http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006737http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006858http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006859http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006738http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006731http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006852http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006853http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006732http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006850http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006730http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006851http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006845http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006724http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006846http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006725http://gp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UMR 1019, Centre de recherche en nutrition humaine, Universite d-AuvergneNot availableGPMDBMuscle ageing contributes to both loss of functional autonomy and increased morbidity. Muscle atrophy accelerates after 50 years of age, but the mechanisms involved are complex and likely result from the alteration of a variety of interrelated functions. In order to better understand the molecular mechanisms underlying muscle chronological ageing in human, we have undertaken a top-down differential proteomic approach to identify novel biomarkers after the fifth decade of age.This study describes the most extensive proteomic analysis of muscle ageing in humans, and identified 34 new potential biomarkers. None of them were previously recognized as differentially expressed in old muscles, and each may represent a novel starting point to elucidate the mechanisms of muscle chronological ageing in humans.Muscle samples were compared between adult (56 years) and old (78 years) post-menopausal women. In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins. Two-dimensional gel electrophoreses with overlapping IPGs were used to improve the separation of muscle proteins. Overall, 1919 protein spots were matched between all individuals, 95 were differentially expressed and identified by mass spectrometry, and they corresponded to 67 different proteins. Our results suggested important modifications in cytosolic, mitochondrial and lipid energy metabolism, which may relate to dysfunctions in old muscle force generation. A fraction of the differentially expressed proteins were linked to the sarcomere and cytoskeleton (myosin light-chains, troponin T, ankyrin repeat domain-containing protein-2, vinculin, four and a half LIM domain protein-3), which may account for alterations in contractile properties. In line with muscle contraction, we also identified proteins related to calcium signal transduction (calsequestrin-1, sarcalumenin, myozenin-1, annexins). Muscle ageing was further characterized by the differential regulation of several proteins implicated in cytoprotection (catalase, peroxiredoxins), ion homeostasis (carbonic anhydrases, selenium-binding protein 1) and detoxification (aldo-keto reductases, aldehyde dehydrogenases). Notably, many of the differentially expressed proteins were central for proteostasis, including heat shock proteins and proteins involved in proteolysis (valosin-containing protein, proteasome subunit beta type-4, mitochondrial elongation factor-Tu).Muscle ageing contributes to both loss of functional autonomy and increased morbidity. Muscle atrophy accelerates after 50 years of age, but the mechanisms involved are complex and likely result from the alteration of a variety of interrelated functions. In order to better understand the molecular mechanisms underlying muscle chronological ageing in human, we have undertaken a top-down differential proteomic approach to identify novel biomarkers after the fifth decade of age.Muscle samples were compared between adult (56 years) and old (78 years) post-menopausal women. In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins. Two-dimensional gel electrophoreses with overlapping IPGs were used to improve the separation of muscle proteins. Overall, 1919 protein spots were matched between all individuals, 95 were differentially expressed and identified by mass spectrometry, and they corresponded to 67 different proteins. Our results suggested important modifications in cytosolic, mitochondrial and lipid energy metabolism, which may relate to dysfunctions in old muscle force generation. A fraction of the differentially expressed proteins were linked to the sarcomere and cytoskeleton (myosin light-chains, troponin T, ankyrin repeat domain-containing protein-2, vinculin, four and a half LIM domain protein-3), which may account for alterations in contractile properties. In line with muscle contraction, we also identified proteins related to calcium signal transduction (calsequestrin-1, sarcalumenin, myozenin-1, annexins). Muscle ageing was further characterized by the differential regulation of several proteins implicated in cytoprotection (catalase, peroxiredoxins), ion homeostasis (carbonic anhydrases, selenium-binding protein 1) and detoxification (aldo-keto reductases, aldehyde dehydrogenases). Notably, many of the differentially expressed proteins were central for proteostasis, including heat shock proteins and proteins involved in proteolysis (valosin-containing protein, proteasome subunit beta type-4, mitochondrial elongation factor-Tu).This study describes the most extensive proteomic analysis of muscle ageing in humans, and identified 34 new potential biomarkers. None of them were previously recognized as differentially expressed in old muscles, and each may represent a novel starting point to elucidate the mechanisms of muscle chronological ageing in humans.<h4>Background</h4>Muscle ageing contributes to both loss of functional autonomy and increased morbidity. Muscle atrophy accelerates after 50 years of age, but the mechanisms involved are complex and likely result from the alteration of a variety of interrelated functions. In order to better understand the molecular mechanisms underlying muscle chronological ageing in human, we have undertaken a top-down differential proteomic approach to identify novel biomarkers after the fifth decade of age.<h4>Results</h4>Muscle samples were compared between adult (56 years) and old (78 years) post-menopausal women. In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins. Two-dimensional gel electrophoreses with overlapping IPGs were used to improve the separation of muscle proteins. Overall, 1919 protein spots were matched between all individuals, 95 were differentially expressed and identified by mass spectrometry, and they corresponded to 67 different proteins. Our results suggested important modifications in cytosolic, mitochondrial and lipid energy metabolism, which may relate to dysfunctions in old muscle force generation. A fraction of the differentially expressed proteins were linked to the sarcomere and cytoskeleton (myosin light-chains, troponin T, ankyrin repeat domain-containing protein-2, vinculin, four and a half LIM domain protein-3), which may account for alterations in contractile properties. In line with muscle contraction, we also identified proteins related to calcium signal transduction (calsequestrin-1, sarcalumenin, myozenin-1, annexins). Muscle ageing was further characterized by the differential regulation of several proteins implicated in cytoprotection (catalase, peroxiredoxins), ion homeostasis (carbonic anhydrases, selenium-binding protein 1) and detoxification (aldo-keto reductases, aldehyde dehydrogenases). Notably, many of the differentially expressed proteins were central for proteostasis, including heat shock proteins and proteins involved in proteolysis (valosin-containing protein, proteasome subunit beta type-4, mitochondrial elongation factor-Tu).<h4>Conclusions</h4>This study describes the most extensive proteomic analysis of muscle ageing in humans, and identified 34 new potential biomarkers. None of them were previously recognized as differentially expressed in old muscles, and each may represent a novel starting point to elucidate the mechanisms of muscle chronological ageing in humans.Proteomics of muscle chronological ageing in post-menopausal women.Gueugneau Marine M,Coudy-Gandilhon Cécile C,Gourbeyre Ophélie O,Chambon Christophe C,Combaret Lydie L,Polge Cécile C,Taillandier Daniel D,Attaix Didier D,Friguet Bertrand B,Maier Andrea B AB,Butler-Browne Gillian G,Béchet Daniel D,Gueugneau Marine M, Coudy-Gandilhon Cécile C, Gourbeyre Ophélie O, Chambon Christophe C, Combaret Lydie L, Polge Cécile C, Taillandier Daniel D, Attaix Didier D, Friguet Bertrand B, Maier Andrea B AB, Butler-Browne Gillian G, Béchet Daniel DSenescence, Muscle Tissues, muscles set, muscle system, musculi, Women's Group, set of muscles, Tissues, musculature system, motor system, Women's Groups, Tissue, Women Groups., muscles, set of skeletal muscles, muscle, Aging, Muscle, Woman, Girl, muscle element, muscule system, ageing, Biological Aging, Biological, musculus, AGING BIOL, Girls, musculature, BIOL AGING, Muscle Tissue, muscle groupIGF-I, data, steel factor, muscle system, cou, musculi, Women's Group, Slf, set of muscles, hematopoietic growth factor KL, adult stage, Women Groups, musculature system, Proteins, Muscle Protein, Somatomedin-C, somatomedin, muscles, set of skeletal muscles, Gene, FPH2, Muscle, Tl3, Tl2, Woman, Girl, sKITLG, polypeptide, Electrophoreses, Lr, mechano growth factor, Osmolality, Girls, Protein, Gene Products, Osmolarities, Low, Igf-1, Adults, Ionic, adult, Osmolalities, SHEP7, Muscle Tissues, me75, muscles set, adults, mast cell growth factor, Osmolar, Tissues, Stem cell factor, Ionic Strengths, motor system, Women's Groups, Tissue, somatomedin-C, SF, Kitl, proteins, muscle, Muscle., STAT5, Mast cell growth factor, D17Mit170, T1, muscle element, muscule system, Protein Gene Products, Gene Proteins, stem cell factor, Osmolarity, Strengths, KL-1, IGF1, Concentration, MGF, musculus, Concentrations, c-Kit ligand, Mechano growth factor, Bra, KITLG, musculature, Soluble KIT ligand, Osmolar Concentrations, SCF, Sl, Muscle Tissue, Ionic Strength, muscle group, StrengthSenescence, Muscle Tissues, muscles set, muscle system, musculi, Women's Group, set of muscles, Tissues, musculature system, motor system, Women's Groups, Tissue, Women Groups., muscles, set of skeletal muscles, muscle, Aging, Muscle, Woman, Girl, muscle element, muscule system, ageing, Biological Aging, Biological, musculus, AGING BIOL, Girls, musculature, BIOL AGING, Muscle Tissue, muscle groupMorbidities, Viral Marker, Biological Markers, human being, Viral, muscle system, Surrogate Endpoints, Surrogate Endpoint, musculi, Clinical Markers, Laboratory, set of muscles, Clinical Marker, musculature system, Serum Markers, Biochemical, muscles, set of skeletal muscles, End Point, Endpoint, Biochemical Markers, Aging, Homo sapiense, Serum, Muscle, Biologic Marker, supernumerary, Immune Marker, Surrogate End Points, Surrogate Markers, Homo spaiens, Laboratory Markers, Homo sapien, Biological, Homo sapian, Marker, Surrogate End Point, Homo sapians, AGING BIOL, Homo sapeins, BIOL AGING, Viral., Biologic Markers, Senescence, increased, Muscle Tissues, Serum Marker, muscles set, Homo sapients, Clinical, End Points, Tissues, Surrogate, increased number, Biological Marker, motor system, Endpoints, Tissue, Humo sapiens, muscle, Immunologic, Laboratory Marker, man, Homo sapines, human, Surrogate Marker, muscle element, muscule system, loss of, ageing, present in greater numbers in organism, Biological Aging, Homo spiens, Immunologic Markers, "human" EXACT genbank_common_name [], Immune, Markers, Homo sapience, Biochemical Marker, Homo sampiens, Viral Markers, musculus, musculature, Muscle Tissue, Home sapiens, Immunologic Marker, accessory, Biologic, muscle group, Immune Markers2005http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310006844dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0pubmed~1identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~2lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0061690314620604570.01.0falseProteomics of muscle chronological ageing in post-menopausal women.Data from ProteomeXchange, PXD ID: PXD001527. File: E-PP-proteolyse-682(1179).mgf Published as part of BMC Genomics. 2014 15:1165 . From the Abstract: {{i}} Muscle samples were compared between adult (56 years) and old (78 years) post-menopausal women. In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins. Two-dimensional gel electrophoreses with overlapping IPGs were used to improve the separation of muscle proteins. {{/i}}2015-02-19GPM3231000684425532418PXD001527PXD001527