Kinetic analysis of transcellular passage of the cobalamin-transcobalamin complex in Caco-2 monolayers.

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 [⁵⁷Co]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 as

SUBMITTER: Juul CB 

PROVIDER: S-EPMC6594447 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature