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    <subfield code="a">10.1016/j.jprot.2012.07.001</subfield>
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    <subfield code="2">sideral</subfield>
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    <subfield code="a">Ramírez-Torres, A</subfield>
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    <subfield code="a">Proteomics and gene expression analyses of squalene-supplemented mice identify microsomal thioredoxin domain-containing protein 5 changes associated with hepatic steatosis</subfield>
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    <subfield code="c">2012</subfield>
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    <subfield code="a">Squalene is an abundant hydrocarbon present in virgin olive oil. Previous studies showed that its administration decreased atherosclerosis and steatosis in male apoE-knock-out mice. To study its effects on microsomal proteins, 1 g/kg/day of squalene was administered to those mice. After 10 weeks, hepatic fat content was assessed and protein extracts of microsomal enriched fractions from control and squalene-treated animals were analyzed by 2D-DIGE. Spots exhibiting significant differences were identified by peptide fingerprinting and MSMS analysis. Squalene administration modified the expression of thirty-one proteins involved in different metabolic functions and increased the levels of those involved in vesicle transport, protein folding and redox status. Only mRNA levels of 9 genes (Arg1, Atp5b, Cat, Hyou1, Nipsnap1, Pcca, Pcx, Pyroxd2, and Txndc5) paralleled these findings. No such mRNA changes were observed in wild-type mice receiving squalene. Thioredoxin domain-containing protein 5 (TXNDC5) protein and mRNA levels were significantly associated with hepatic fat content in apoE-ko mice. These results suggest that squalene action may be executed through a complex regulation of microsomal proteins, both at the mRNA and post-transcriptional levels and the presence of apoE may change the outcome. Txndc5 reflects the anti-steatotic properties of squalene and the sensitivity to lipid accumulation.</subfield>
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    <subfield code="9">info:eu-repo/grantAgreement/ES/DGA-FSE/B69</subfield>
    <subfield code="9">info:eu-repo/grantAgreement/ES/DGA/PI025-08</subfield>
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    <subfield code="9">info:eu-repo/semantics/openAccess</subfield>
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    <subfield code="a">BIOCHEMICAL RESEARCH METHODS</subfield>
    <subfield code="b">15 / 74 = 0.203</subfield>
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    <subfield code="a">Barceló-Batllori, S</subfield>
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    <subfield code="a">Martínez-Beamonte, R</subfield>
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    <subfield code="a">Surra, JC</subfield>
    <subfield code="u">Universidad de Zaragoza</subfield>
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    <subfield code="a">Arnal, C</subfield>
    <subfield code="u">Universidad de Zaragoza</subfield>
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    <subfield code="a">Guillén, N</subfield>
    <subfield code="u">Universidad de Zaragoza</subfield>
    <subfield code="0">(orcid)0000-0001-6627-298X</subfield>
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    <subfield code="a">Acín, S</subfield>
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    <subfield code="a">Osada, J</subfield>
    <subfield code="u">Universidad de Zaragoza</subfield>
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    <subfield code="a">Universidad de Zaragoza</subfield>
    <subfield code="b">Dpto. Patología Animal</subfield>
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    <subfield code="1">1002</subfield>
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    <subfield code="a">Universidad de Zaragoza</subfield>
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    <subfield code="a">Universidad de Zaragoza</subfield>
    <subfield code="b">Dpto. Anat.Pat.Med.Leg.For.To.</subfield>
    <subfield code="c">Area Toxicología</subfield>
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    <subfield code="g">77 (2012), 27-39</subfield>
    <subfield code="p">J. proteomics</subfield>
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