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XB-ART-19125
J Biol Chem 1995 Oct 27;27043:25591-5.
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Stable inducible expression of a functional rat liver organic anion transport protein in HeLa cells.

Shi X , Bai S , Ford AC , Burk RD , Jacquemin E , Hagenbuch B , Meier PJ , Wolkoff AW .


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Recently we expression cloned a rat liver organic anion transport protein in Xenopus laevis oocytes (Jacquemin, E. Hagenbuch, B, Stieger, B., Wolkoff, A.W., and Meier, P.J.,(1994) Proc. Natl. Acad. Sci. U.S.A. 91, 133-137). In the present study, we have stably transfected the cDNA encoding this protein into HeLa cells by using a vector containing a zinc-inducible promoter. The parent cells have virtually no baseline transport of [35S]sulfobromophthalein, whereas the induced transfected cells express a novel 74-kDa protein and avidly transport this ligand. Transport by these cells is saturable (Km = 3.3 microM, Vmax = 257 pmol/min/mg protein), bidirectional, and highly temperature-dependent. In the presence of albumin, uptake of [35S]sulfobromophthalein requires the presence of extracellular Cl, whereas in the absence of albumin, this C1- dependence is not seen. These studies indicate that cellular uptake of sulfobromophthalein does not result from direct interaction with the plasma membrane lipid bilayer but rather requires the presence of a specific plasma membrane transporter.

???displayArticle.pubmedLink??? 7592731
???displayArticle.link??? J Biol Chem
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