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Dietary protein regulates gene expression of amino acid‐degrading enzymes through PPARα
Author(s) -
Contreras Alejandra,
Rangel Claudia,
Ortiz Victor,
Aleman Gabriela,
PalaciosGonzalez Berenice,
Tejero Elizabeth,
Torres Nimbe,
Tovar Armando
Publication year - 2013
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.27.1_supplement.631.23
Subject(s) - gene expression , catabolism , gene , biology , peroxisome proliferator activated receptor , biochemistry , amino acid , fatty acid , enzyme , beta oxidation , microarray , regulation of gene expression , dna microarray , transcription factor , gene expression profiling
The effects of PPARα ligands, such as fatty acids, have been demonstrated in several tissues, particularly in liver, modulating the expression of enzymes for fatty acid oxidation, but recent evidence also suggest that PPARα regulates amino acid oxidation. The amino acid catabolism is regulated by hepatic amino acid‐degrading enzymes (AADE); therefore the aim of this work was to study whether PPARα regulates the expression of AADE. Male PPARα null mice were used and age‐matched with C57BL6 mice (Wild type, WT) as control group, and were fed diets containing increased amounts of dietary protein (6, 20 or 50 %). RNA was extracted from liver to assess the whole genome expression using microarrays (Mouse Gene 1.0 ST Array, Affymetrix). We found that in WT mice, the gene expression of AADE, such as Hal, Got1, Ass1, Sdh and Uroc1, was proportional to the increase in dietary protein concentration. In contrast, in PPARα null mice this effect was absent, even more, we did not observe significant differential gene expression between groups fed with 6 and 50% of protein. Moreover, some AADE such as Kynu, Oat and Acmsd, as well as the transcription factor Hnf4α showed higher gene expression in KO than WT. Network analysis suggest that PPARα regulates the expression of AADE genes through Hnf4α interaction. Thus, PPARα functions as a metabolic sensor to preserve amino acids by stimulating fatty oxidation. Grant Funding Source : CONACYT