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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Krane, Gregory A.
• Braddock, Katie C.

Colaboradores

• McConkey, Marie
• Gillin, Cory

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-121404-130336

Advisor

• Adams, David S.

Year

• 2004

Date created

• 2004-12-14

Resource type

• Major Qualifying Project

Major

• Biochemistry
• Biology & Biotechnology

Rights statement

• In Copyright