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• W2904344181 endingPage "477" @default.
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• W2904344181 abstract "We suggest a novel kinetic approach to quantifying receptor–ligand interactions via the cellular transport and/or accumulation of the ligand. The system of cobalamin (Cbl, vitamin B12) transport was used as a model, because Cbl is an obligatory cofactor, taken up by animal cells with the help of a transport protein and a membrane receptor. Bovine transcobalamin (bTC) stimulated the cellular accumulation and transcytosis of radioactive [ 57 Co]Cbl in polarized monolayers of Caco-2 cells. The bovine protein was much more efficient than human TC. The transport was inhibited in a dose-dependent manner by the unlabeled bTC-Cbl complex, the ligand-free bTC, and the receptor-associated protein (RAP). This inhibition pattern implied the presence of a megalin-like receptor. Quantitative assessment of kinetic records by the suggested method revealed the apparent concentration of receptors in vitro (≈15 nM), as well as the dissociation constants of bTC–Cbl ( K d = 13 nM) and RAP ( K d = 1.3 nM). The data were used to estimate the effective luminal concentrations of TC-specific receptors in kidneys (3.8 µM) and intestine (50 nM), the tissues resembling polarized Caco-2 cells." @default.
• W2904344181 created "2018-12-22" @default.
• W2904344181 creator A5037799908 @default.
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• W2904344181 date "2019-02-15" @default.
• W2904344181 modified "2023-10-05" @default.
• W2904344181 title "Kinetic analysis of transcellular passage of the cobalamin–transcobalamin complex in Caco-2 monolayers" @default.
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• W2904344181 doi "https://doi.org/10.1091/mbc.e18-09-0571" @default.
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