Title : Inhibition of the all-trans Retinoic Acid (atRA) Hydroxylases CYP26A1 and CYP26B1 Results in Dynamic, Tissue-Specific Changes in Endogenous atRA Signaling.

Pub. Date : 2017 Jul

PMID : 28446509






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Inhibition of the all-trans Retinoic Acid (atRA) Hydroxylases CYP26A1 and CYP26B1 Results in Dynamic, Tissue-Specific Changes in Endogenous atRA Signaling. Tretinoin cytochrome P450, family 26, subfamily a, polypeptide 1 Mus musculus
2 The cytochrome P450 family 26 (CYP26) enzymes are responsible for atRA clearance, and are potential drug targets to increase concentrations of endogenous atRA in a tissue-specific manner. Tretinoin cytochrome P450, family 26, subfamily a, polypeptide 1 Mus musculus
3 The cytochrome P450 family 26 (CYP26) enzymes are responsible for atRA clearance, and are potential drug targets to increase concentrations of endogenous atRA in a tissue-specific manner. Tretinoin cytochrome P450, family 26, subfamily a, polypeptide 1 Mus musculus
4 Following a single 2.5-mg/kg dose of talarozole to mice, atRA concentrations increased up to 5.7-, 2.7-, and 2.5-fold in serum, liver, and testis, respectively, resulting in induction of Cyp26a1 in the liver and testis and Rar beta and Pgc 1beta in liver. Tretinoin cytochrome P450, family 26, subfamily a, polypeptide 1 Mus musculus
5 The increase in atRA concentrations was well predicted from talarozole pharmacokinetics and in vitro data of CYP26 inhibition. Tretinoin cytochrome P450, family 26, subfamily a, polypeptide 1 Mus musculus