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The expression of genes involved in amino acid oxidation and gluconeogenesis is down‐regulated by cold exposure in rat liver
Author(s) -
Castro Ana Laura,
Palacios Berenice,
Torres Nimbe,
Tovar Armando R,
Aleman Gabriela
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.869.12
Subject(s) - gluconeogenesis , catabolism , phosphoenolpyruvate carboxykinase , peroxisome , beta oxidation , peroxisome proliferator activated receptor , amino acid , alpha (finance) , gene expression , tyrosine aminotransferase , biochemistry , coactivator , chemistry , peroxisome proliferator activated receptor alpha , enzyme , gene , biology , lipid metabolism , tyrosine , histidine , nuclear receptor , enzyme inducer , transcription factor , medicine , construct validity , nursing , patient satisfaction
We have demonstrated that PPAR‐alpha down‐regulates the expression of the histidine degrading enzyme, histidase (HAL), while it up‐regulates enzymes involved in lipid oxidation. PGC‐1 is a well‐known PPAR‐alpha coactivator, that is over‐expressed during cold exposure (CE). The aim of the present work was to study whether the induction of PGC‐1 by CE regulates the expression of genes involved in amino acid catabolism (HAL, tyrosine aminotransferase (TAT)), as well as of genes involved in lipid oxidation and gluconeogenesis (CPT‐1, PEPCK, PPAR?, PGC‐1 alpha and ‐1 beta) in rat liver. Our results show a decreased expression in HAL, TAT and PEPCK after 12 h CE when compared with those rats mantained at room temperature. PGC‐1 alpha, ‐1?, and CPT‐1 expression was increased after CE, with no change in PPAR‐alpha mRNA abundance. Our data suggest that an induction of PGC‐1 alpha and ‐1 beta by CE activates PPAR?, that in turn increased the expression of genes involved in fatty acid oxidation, and at the same time decreased amino acid catabolism for body protein sparing.