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Ochratoxin A secretion by ATP-dependent membrane transporters in Caco-2 cells

Jan Schrickx1, Yuri Lektarau, J Fink-Gremmels

  • 1Department of Veterinary Pharmacology, Pharmacy and Toxicology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 16, 3584 CM, Utrecht, The Netherlands, J.A.Schrickx@vet.uu.nl

Archives of Toxicology
|October 26, 2005
PubMed

Insights

The mycotoxin ochratoxin A (OTA) is secreted by Caco-2 cells via MRP2 and BCRP transporters. This research clarifies OTA

Area of Science:

  • Toxicology
  • Cell Biology
  • Pharmacology

Background:

  • ATP-dependent membrane transporters like P-gp, MRP2, and BCRP are crucial for xenobiotic and drug excretion.
  • The mycotoxin ochratoxin A (OTA) has been previously suggested to be a substrate for these transporters.

Purpose of the Study:

  • To investigate the absorption and secretion mechanisms of ochratoxin A (OTA) in a Caco-2 cell model.
  • To determine if OTA is a substrate for specific ATP-dependent transporters, namely MRP2 and BCRP.

Main Methods:

  • Caco-2 cells were cultured as confluent monolayers in bicameral inserts.
  • Transepithelial transport of OTA was assessed.
  • The effects of MRP2, BCRP, and P-gp inhibitors (MK571, GF120918, Ko143) and other modulators (Cyclosporine A, PSC833) on OTA transport were evaluated.

Main Results:

  • Caco-2 cells demonstrated concentration-dependent secretion of OTA to the luminal side, with higher secretory than absorptive permeability.
  • Inhibitors of MRP2 (MK571) and BCRP (GF120918, Ko143) significantly decreased OTA secretion and increased absorption.
  • Cyclosporine A reduced secretory permeability, while PSC833 had no effect, further implicating MRP2 and BCRP in OTA transport.

Conclusions:

  • Ochratoxin A (OTA) is confirmed to be a substrate for both MRP2 and BCRP transporters.
  • These findings are significant for understanding mycotoxin absorption, tissue distribution, and excretion pathways (renal, biliary, mammary).
  • The study highlights the role of efflux transporters in the disposition of ochratoxin A.

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