Faculty Advisor

Adams, David S.

Abstract

Mrp2 is an organic anion and bile salt export pump that must be translocated from the cytoplasm to the hepatocyte tubule canalicular membrane to transport its substrate. Although cAMP has been shown to induce both Mrp2 translocation and PKC-delta activation, the interdependency of those two events has not been established. Hepatocytes were treated with a cAMP analogue and/or bistratene A (a known activator of PKC-delta) at varying concentrations, followed by biotinylation of cell surface protein, preparation of cell lysates, immunoprecipitation by streptavidin, and western analysis of Mrp2 levels. Like cAMP, bistratene A also induced Mrp2 translocation, and the combined effects were not additive, indicating that cAMP translocates Mrp2 by activating PKC-delta.

Publisher

Worcester Polytechnic Institute

Date Accepted

December 2004

Major

Biology and Biotechnology

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

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