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Updated: Nov 28, 2025

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
Published on: August 6, 2018
Analysis of the interaction between tryptophan-related compounds and ATP-binding cassette transporter G2 (ABCG2)
Alba M Garcia-Lino1, Alex Gomez-Gomez2, Dafne Garcia-Mateos1
1Department of Biomedical Sciences-Physiology, Faculty of Veterinary Medicine, Animal Health Institute (INDEGSAL), University of Leon, Campus de Vegazana, 24071 Leon, Spain.
Abstract:
ATP-binding cassette transporter G2 (ABCG2) is involved in the secretion of several compounds in milk. The in vitro and in vivo interactions between tryptophan-related compounds and ABCG2 were investigated. The tryptophan metabolome was determined by liquid chromatography-tandem mass spectrometry in milk and plasma from wild-type and Abcg2-/- mice as well as dairy cows carrying the ABCG2 Y581S polymorphism (Y/S) and noncarrier animals (Y/Y). The milk-to-plasma ratios of tryptophan, kynurenic acid, kynurenine, anthranilic acid, and xanthurenic acid were higher in wild-type mice than in Abcg2-/- mice. The ratio was 2-fold higher in Y/S than in Y/Y cows for kynurenine. In vitro transport assays confirmed that some of these compounds were in vitro substrates of the transporter and validated the differences observed between the two variants of the bovine protein. These findings show that the secretion of metabolites belonging to the kynurenine pathway into milk is mediated by ABCG2.
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