149096 20260202145620.0 doi 10.1016/j.jprot.2012.02.025 sideral 99976 ART-2012-99976 eng Ramírez-Torres, A. Universidad de Zaragoza Proteomics and gene expression analyses of mitochondria from squalene-treated apoE-deficient mice identify short-chain specific acyl-CoA dehydrogenase changes associated with fatty liver amelioration 2012 Access copy available to the general public Unrestricted Squalene, a hydrocarbon involved in cholesterol biosynthesis, is an abundant component in virgin olive oil. Previous studies showed that its administration decreased atherosclerosis and steatosis in male apoE knock-out mice. To study the effect of squalene on mitochondrial proteins in fatty liver, 1. g/kg/day of this isoprenoid was administered to those mice. After 10. weeks, hepatic fat was assessed and protein extracts from mitochondria enriched fractions from control and squalene-treated animals were analyzed by 2D-DIGE. Spots exhibiting significant differences were identified by MS analysis. Squalene administration modified the expression of eighteen proteins involved in different metabolic processes, 12 associated with hepatic fat content. Methionine adenosyltransferase I alpha (Mat1a) and short-chain specific acyl-CoA dehydrogenase (Acads) showed significant increased and decreased transcripts, respectively, consistent with their protein changes. These mRNAs were also studied in wild-type mice receiving squalene, where Mat1a was found increased and Acads decreased. However, this mRNA was significantly increased in the absence of apolipoprotein E. These results suggest that squalene action may be executed through a complex regulation of mitochondrial protein expression, including changes in Mat1a and Acads levels. Indeed, Mat1a is a target of squalene administration while Acads reflects the anti-steatotic properties of squalene. info:eu-repo/grantAgreement/ES/CICYT-FEDER/SAF 2010-14958 info:eu-repo/grantAgreement/ES/DGA/PI025-08 info:eu-repo/semantics/openAccess by-nc-nd https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es 4.088 2012 BIOCHEMICAL RESEARCH METHODS 15 / 74 = 0.203 2012 Q1 T1 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Barceló-Batllori, S. Fernández-Vizarra, E. (orcid)0000-0002-2469-142X Navarro, M. A. Universidad de Zaragoza (orcid)0000-0002-0108-1004 Arnal, C. Universidad de Zaragoza (orcid)0000-0003-1197-4276 Guillén, N. Universidad de Zaragoza (orcid)0000-0001-6627-298X Acín, S. Osada, J. Universidad de Zaragoza (orcid)0000-0002-8251-8457 1009 773 Universidad de Zaragoza Dpto. Patología Animal Área Sanidad Animal 1002 X Universidad de Zaragoza Dpto. Bioq.Biolog.Mol. Celular Proy. investigación DEA 1002 060 Universidad de Zaragoza Dpto. Bioq.Biolog.Mol. Celular Área Bioquímica y Biolog.Mole. 1000 807 Universidad de Zaragoza Dpto. Anat.Pat.Med.Leg.For.To. Area Toxicología 75, 9 (2012), 2563-2575 J. proteomics JOURNAL OF PROTEOMICS 1874-3919 504161 http://zaguan.unizar.es/record/149096/files/texto_completo.pdf Versión publicada 1124354 http://zaguan.unizar.es/record/149096/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:149096 articulos driver 2026-02-02-14:49:02 ARTICLE