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PPARα regulates the expression of the amino acid degrading enzyme histidase
Author(s) -
Aleman Gabriela,
Quiroz Gabriela,
Torres Nimbe,
Tovar Armando R
Publication year - 2006
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.20.5.a1043-b
Subject(s) - electrophoretic mobility shift assay , catabolism , microbiology and biotechnology , luciferase , gene expression , transcription factor , transfection , amino acid , enzyme , messenger rna , gene , biochemistry , biology , transcription (linguistics) , chemistry , histidine , linguistics , philosophy
Histidase (Hal) is the first enzyme in the catabolism of histidine. Two putative PPAR responsive elements (PPARE) have been identified in the rat Hal gene promoter, however their functionality has not been assessed. Thus, the purpose of the present work was to establish if the transcription factor PPARα can regulate Hal gene expression. The results showed that the addition of the PPARα agonist Wy 14 643 to the diet decreased hepatic Hal activity and mRNA expression, and increased CPT‐1 mRNA concentration. Transfection of HepG2 cells with a plasmid (pGL3 basic) containing the Hal gene promoter and incubated with Wy 14 643 decreased luciferase activity by 60%. Furthermore electrophoretic mobility shift assay showed protein binding to the PPARE of the Hal promoter located at position −487 from the TSS. When this PPRE site was mutated the binding of the PPARα present in nuclear extracts was lost. These results suggest that PPARα may have an important role in preventing amino acid catabolism during stress conditions in the rat. Supported by CONACYT (grant 41799‐M)