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- W2364761434 abstract "Objective To investigate the alterations in uptake function of liver specific transporter OATP-C (organic anion transporting polypeptide C) by mutating positive charge consensus lysine K490T (Lys to Thr) localized on this polypeptide extracellular loop. Methods Wild type OATP-C full length cDNA was amplified from human liver mRNA by RT-PCR. Mutation of positive charge to neutral amino acid K490T (Lys to Thr) was made by site-direct mutagenesis technique. The recombinant constructs of wild type and mutated OATP-C cDNA with GFP fusion gene at its C-terminal were generated by subcloning and transfected into HEK293 cells, then cell plasma membrane targeting expression and substrate uptake function were observed. Results Both the wild type and mutated OATP-C proteins were highly expressed on HEK293 cell plasma membrane. The uptake of[3H] estrone sulfat substrates of mutated OATP-C markedly reduced in 5 min by 38.66% as compared with wild type. Analysis of concentration-dependent uptake kinetics demonstrated that the mutants possessed a significantly higher Km value and lower Vmax value than those of wild type. Conclusion The conserved positive charge Lys-490 on extracellular loop of OATP-C may be a determinant amino acid in the uptake of organic anion substrates." @default.
- W2364761434 created "2016-06-24" @default.
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- W2364761434 date "2007-01-01" @default.
- W2364761434 modified "2023-09-23" @default.
- W2364761434 title "Effect of its Lysine-490 mutation on uptake function of organic anion transporting polypeptide C" @default.
- W2364761434 hasPublicationYear "2007" @default.
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