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The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two regulatory motifs
Author(s) -
Bardot Olivier,
Clemencet Marie Claude,
Passilly Patricia,
Latruffe Norbert
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00097-s
Subject(s) - peroxisome , peroxisome proliferator , transfection , chemistry , enzyme , phosphofructokinase 2 , bifunctional , biochemistry , microbiology and biotechnology , biology , gene , catalysis
Peroxisome proliferators (PPs) are non‐genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator‐activated receptor (PPAR) and the 9‐ cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT‐related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.