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J. Biochem, 1990, Vol. 107, No. 5 749-754
© 1990 Japanese Biochemical Society

research-article

Hepatic Uptake of Bilirubin Diglucuronide: Analysis by Using Sinusoidal Plasma Membrane Vesicles1

Yukihiko Adachi*,2, Jayanta Roy-Chowdhury**, Namita Roy-Chowdhury**, Rolf Kinne***,3, Thao Tran**, Hiroaki Kobayashi* and Irwin M. Arias****

*Second Department of Internal Medicine, Kinki University School of Medicine Osakasayama, Osaka 589
**Departments of Medicine, Albert Einstein College of Medicine 1300 Morris Park Avenue, Bronx, New York, NY 10461, U.S.A.
***Departments of Physiology, Albert Einstein College of Medicine 1300 Morris Park Avenue, Bronx, New York, NY 10461, U.S.A.
****Department of Physiology, Tufts University School of Medicine 136 Harrison Avenue, Boston, MA 02111, U.S.A.

To whom correspondence should be addressed.

In order to characterize the mechanism for bilirubin transport in the liver, the uptake of bilirubin diglucuronide (BDG) into purified sinusoidal plasma membrane vesicles was investigated. BDG uptake was saturable, and was inhibited by sulfobromophthalein and unconjugated bilirubin, but was not affected by sodium taurocholate. BDG uptake was sodium-independent and was stimulated by intravesicular bilirubin or BDG (trans-stimulation). BDG transport showed strong potential sensitivity; vesicle inside-negative membrane potential created by different anion gradients inhibited BDG uptake whereas vesicle inside-positive membrane potential generated by potassium gradients and valino-mycin markedly stimulated BDG transport. These data suggest that BDG, sulfobromophthalein, and probably unconjugated bilirubin share a common transporter in liver cells which is sodium independent, membrane-potential-dependent and capable of exchange. The direction of transport in vivo may be governed by the intracellular concentration of BDG and of other yet unidentified organic an ions sharing this transporter.

1This work was partly supported by the U.S. National Institutes of Health grants DK 39137 (to NRC), DK 34357 (to JRC), and DK 35652 (to IMA).

3Present address: Max-Planck-Institut fur Systemphysiologie, Rheinlanddam 201, 4600 Dortmund 1, F.R.G.


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