Quantitative Proteomic Analysis Reveals Metabolic Alterations, Calcium Dysregulation, And Increased Expression Of Extracellular Matrix Proteins In Laminin α2 Chain-deficient Muscle

dc.creatorDe Oliveira B.M.
dc.creatorMatsumura C.Y.
dc.creatorFontes-Oliveira C.C.
dc.creatorGawlik K.I.
dc.creatorAcosta H.
dc.creatorWernhoff P.
dc.creatorDurbeej M.
dc.date2014
dc.date2015-06-25T17:53:09Z
dc.date2015-11-26T14:21:57Z
dc.date2015-06-25T17:53:09Z
dc.date2015-11-26T14:21:57Z
dc.date.accessioned2018-03-28T21:23:47Z
dc.date.available2018-03-28T21:23:47Z
dc.identifier
dc.identifierMolecular And Cellular Proteomics. American Society For Biochemistry And Molecular Biology Inc., v. 13, n. 11, p. 3001 - 3013, 2014.
dc.identifier15359476
dc.identifier10.1074/mcp.M113.032276
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84910684594&partnerID=40&md5=2e15e53d812e1848bd583738e3651c6b
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/86396
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/86396
dc.identifier2-s2.0-84910684594
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1244686
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionCongenital muscular dystrophy with laminin α2 chain deficiency (MDC1A) is one of the most severe forms of muscular disease and is characterized by severe muscle weakness and delayed motor milestones. The genetic basis of MDC1A is well known, yet the secondary mechanisms ultimately leading to muscle degeneration and subsequent connective tissue infiltration are not fully understood. In order to obtain new insights into the molecular mechanisms underlying MDC1A, we performed a comparative proteomic analysis of affected muscles (diaphragm and gastrocnemius) from laminin α2 chain-deficient dy3K/dy3K mice, using multidimensional protein identification technology combined with tandem mass tags. Out of the approximately 700 identified proteins, 113 and 101 proteins, respectively, were differentially expressed in the diseased gastrocnemius and diaphragm muscles compared with normal muscles. A large portion of these proteins are involved in different metabolic processes, bind calcium, or are expressed in the extracellular matrix. Our findings suggest that metabolic alterations and calcium dysregulation could be novel mechanisms that underlie MDC1A and might be targets that should be explored for therapy. Also, detailed knowledge of the composition of fibrotic tissue, rich in extracellular matrix proteins, in laminin α2 chain-deficient muscle might help in the design of future anti-fibrotic treatments. All MS data have been deposited in the ProteomeXchange with identifier PXD000978 (http://proteomecentral.proteomexchange. org/dataset/PXD000978).
dc.description13
dc.description11
dc.description3001
dc.description3013
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior; 2014-10-6; CAPES; Coordenação de Aperfeiçoamento de Pessoal de Nível Superior; KAW2007.0118; Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
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dc.languageen
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc.
dc.relationMolecular and Cellular Proteomics
dc.rightsfechado
dc.sourceScopus
dc.titleQuantitative Proteomic Analysis Reveals Metabolic Alterations, Calcium Dysregulation, And Increased Expression Of Extracellular Matrix Proteins In Laminin α2 Chain-deficient Muscle
dc.typeArtículos de revistas


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