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    Protein kinase Cdelta mediates cyclic adenosine monophosphate-stimulated translocation of sodium taurocholate cotransporting polypeptide and multidrug resistant associated protein 2 in rat hepatocytes

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    Authors
    Schonhoff, Christopher M.
    Gillin, Henry
    Webster, Cynthia R. L.
    Anwer, M. Sawkat
    UMass Chan Affiliations
    Department of Biomedical Sciences
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2008-02-15
    Keywords
    1-Phosphatidylinositol 3-Kinase; ATP-Binding Cassette Transporters; Acetamides; Acetophenones; Animals; Benzopyrans; Cyclic AMP; Hepatocytes; Male; Organic Anion Transporters, Sodium-Dependent; Phosphorylation; Protein Kinase C-delta; Pyrans; Rats; Rats, Wistar; Spiro Compounds; Symporters; Taurocholic Acid
    Life Sciences
    Medicine and Health Sciences
    
    Metadata
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    Link to Full Text
    http://dx.doi.org/10.1002/hep.22162
    Abstract
    Cyclic adenosine monophosphate (cAMP) stimulates translocation of Na(+)-taurocholate (TC) cotransporting polypeptide (Ntcp) and multidrug resistant associated protein 2 (Mrp2) to the plasma membrane. Because cAMP activates phosphoinositide-3-kinase (PI3K) and protein kinase C (PKC) activation is PI3K-dependent, the aim of the current study was to determine whether cAMP activates conventional and novel PKCs in hepatocytes and whether such activation plays a role in cAMP-stimulated Ntcp and Mrp2 translocation. The effect of cAMP on PKCs, TC uptake, and Ntcp and Mrp2 translocation was studied in isolated rat hepatocytes using a cell-permeable cAMP analog, CPT-cAMP. The activity of PKCs was assessed from membrane translocation of individual PKCs, and phospho-specific antibodies were used to determine PKCdelta phosphorylation. TC uptake was determined from time-dependent uptake of (14)C-TC, and a cell surface biotinylation method was used to determine Ntcp and Mrp2 translocation. CPT-cAMP stimulated nPKCdelta but not cPKCalpha or nPKCepsilon, and induced PI3K-dependent phosphorylation of nPKCdelta at Thr(505). Rottlerin, an inhibitor of nPKCdelta, inhibited cAMP-induced nPKCdelta translocation, TC uptake, and Ntcp and Mrp2 translocation. Bistratene A, an activator of nPKCdelta, stimulated nPKCdelta translocation, TC uptake, and Ntcp and Mrp2 translocation. The effects of cAMP and bistratene A on TC uptake and Ntcp and Mrp2 translocation were not additive. Conclusion: These results suggest that cAMP stimulates Ntcp and Mrp2 translocation, at least in part, by activating nPKCdelta via PI3K-dependent phosphorylation at Thr(505).
    Source
    Hepatology. 2008 Apr;47(4):1309-16. Link to article on publisher's site
    DOI
    10.1002/hep.22162
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32900
    PubMed ID
    18273864
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1002/hep.22162
    Scopus Count
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    Morningside GSBS Scholarly Publications

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