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008			200702b xxu||||| |||| 00| 0 eng d
040			_cH12O
041			_aeng
100			_92678 _aMarín Buera, Lorena _eInstituto de Investigación i+12
100			_92679 _aGarcía Bartolomé, Alberto _eInstituto de Investigación i+12
100			_91013 _aMorán Jiménez, María Josefa _eInstituto de Investigación i+12
100			_91007 _aArenas Barbero, Joaquín _eInstituto de Investigación
100			_92680 _aHidalgo, Beatriz _eBioquímica
100			_92412 _aMartín, Miguel A. _eInstituto de Investigación i+12
100			_92361 _aUgalde Bilbao, Cristina _eInstituto de Investigación i+12
100			_92247 _aSánchez Pérez, Ricardo _eInstituto de Investigación i+12
245	0	0	_aDifferential proteomic profiling unveils new molecular mechanisms associated with mitochondrial complex III deficiency. _h[artículo]
260			_bJournal of proteomics, _c2015
300			_a113:38-56.
500			_aFormato Vancouver: Marín-Buera L, García-Bartolomé A, Morán M, López-Bernardo E, Cadenas S, Hidalgo B et al. Differential proteomic profiling unveils new molecular mechanisms associated with mitochondrial complex III deficiency. J Proteomics. 2015 Jan 15;113:38-56.
501			_aPMID: 25239759 PMC4259860
504			_aContiene 64 referencias
520			_aWe have analyzed the cellular pathways and metabolic adaptations that take place in primary skin fibroblasts from patients with mutations in BCS1L, a major genetic cause of mitochondrial complex III enzyme deficiency. Mutant fibroblasts exhibited low oxygen consumption rates and intracellular ATP levels, indicating that the main altered molecular event probably is a limited respiration-coupled ATP production through the OXPHOS system. Two-dimensional DIGE and MALDI-TOF/TOF mass spectrometry analyses unambiguously identified 39 proteins whose expression was significantly altered in complex III-deficient fibroblasts. Extensive statistical and cluster analyses revealed a protein profile characteristic for the BCS1L mutant fibroblasts that included alterations in energy metabolism, cell signaling and gene expression regulation, cytoskeleton formation and maintenance, and intracellular stress responses. The physiological validation of the predicted functional adaptations of human cultured fibroblasts to complex III deficiency confirmed the up-regulation of glycolytic enzyme activities and the accumulation of branched-chain among other amino acids, suggesting the activation of anaerobic glycolysis and cellular catabolic states, in particular protein catabolism, together with autophagy as adaptive responses to mitochondrial respiratory chain dysfunction and ATP deficiency. Our data point to an overall metabolic and genetic reprogramming that could contribute to explain the clinical manifestations of complex III deficiency in patients.
710			_9625 _aInstituto de Investigación imas12
710			_9317 _aServicio de Bioquímica Clínica
856			_uhttp://europepmc.org/article/MED/25239759 _yAcceso libre
942			_2ddc _cART _n0