| Autor: |
Sanchez-Dominguez CN; Department of Biochemistry and Molecular Medicine, Faculty of Medicine, Autonomous University of Nuevo Leon, Monterrey, Nuevo Leon 64460, Mexico., Gallardo-Blanco HL; Department of Genetics, Faculty of Medicine, Autonomous University of Nuevo Leon, Monterrey, Nuevo Leon 64460, Mexico., Salinas-Santander MA; Saltillo Unit, Autonomous University of Coahuila, Faculty of Medicine, Saltillo, Coahuila 25000, Mexico., Ortiz-Lopez R; Tecnologico de Monterrey, Medical School and Health Sciences, Monterrey, Nuevo Leon 64710, Mexico. |
| Abstrakt: |
Biotransformation is an enzyme-catalyzed process in which the body converts endogenous compounds, xenobiotics and toxic substances into harmless or easily excreted metabolites. The biotransformation reactions are classified as phase I and II reactions. Uridine 5'-diphospho (UDP)-glucuronosyltransferases (UGTs) are a superfamily of phase II enzymes which have roles in the conjugation of xenobiotics or endogenous compounds, including drugs and bilirubin, with glucuronic acid to make them easier to excrete. The method the human body uses to achieve glucuronidation may be affected by a large interindividual variation due to changes in the sequences of the genes encoding these enzymes. In the last five years, the study of the genetic variants of the UGTs at a molecular level has become important due to its association with several diseases and the ability to predict adverse events due to drug metabolism. In the present review, the structure and the prominent genetic variants of the UGT1A subfamily and their metabolic and clinical implications are described. |
