MRP4 is responsible for the efflux transport of mycophenolic acid β-d glucuronide (MPAG) from hepatocytes to blood.
MPA
MPAG
MRP4
drug–drug interactions
molecular docking
Journal
Xenobiotica; the fate of foreign compounds in biological systems
ISSN: 1366-5928
Titre abrégé: Xenobiotica
Pays: England
ID NLM: 1306665
Informations de publication
Date de publication:
Jan 2021
Jan 2021
Historique:
pubmed:
22
8
2020
medline:
15
12
2020
entrez:
22
8
2020
Statut:
ppublish
Résumé
Mycophenolic acid (MPA) has become a cornerstone of immunosuppressive therapy, in particular for transplant patients. In the gastrointestinal tract, the liver and the kidney, MPA is mainly metabolized into phenyl-β-d glucuronide (MPAG). Knowledge about the interactions between MPA/MPAG and membrane transporters is still fragmented. The aim of the present study was to explore these interactions with the basolateral hepatic MRP4 transporter. The inhibition of the MRP4-driven transport by various drugs which can be concomitantly prescribed was also evaluated. In vitro experiments using vesicles overexpressing MRP4 showed an ATP-dependent transport of MPAG driven by MRP4 (Michaelis-Menten constant of 233.9 ± 32.8 µM). MPA was not effluxed by MRP4. MRP4-mediated transport of MPAG was inhibited (from -43% to -84%) by ibuprofen, cefazolin, cefotaxime and micafungin. An in silico approach based on molecular docking and molecular dynamics simulations rationalized the mode of binding of MPAG to MRP4. The presence of the glucuronide moiety in MPAG was highlighted as key, being prone to make electrostatic and H-bond interactions with specific residues of the MRP4 protein chamber. This explains why MPAG is a substrate of MRP4 whereas MPA is not.
Identifiants
pubmed: 32820679
doi: 10.1080/00498254.2020.1813352
doi:
Substances chimiques
Glucuronides
0
Membrane Transport Proteins
0
Multidrug Resistance-Associated Proteins
0
mycophenolic acid glucuronide
54TS5J9T0K
Mycophenolic Acid
HU9DX48N0T
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM