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J Biol Chem, Vol. 274, Issue 11, 7067-7071, March 12, 1999

Up-regulation of the Pit-2 Phosphate Transporter/Retrovirus Receptor by Protein Kinase C

Zsolt Jobbagy, Zoltan Olah, Gyorgy Petrovics, Maribeth V. Eiden^¶, Betsy D. Leverett, Nicholas M. Dean^**, and Wayne B. Anderson

From the  Laboratory of Cellular Oncology, National Cancer Institute, and ^¶ Laboratory of Cellular and Molecular Regulation, National Institute of Mental Health, National Institutes of Health Bethesda, Maryland 20892,  Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892, and ^** Department of Pharmacology, ISIS Pharmaceuticals, Carlsbad Research Center, Carlsbad, California 92008

The membrane receptors for the gibbon ape leukemia retrovirus and the amphotropic murine retrovirus serve normal cellular functions as sodium-dependent phosphate transporters (Pit-1 and Pit-2, respectively). Our earlier studies established that activation of protein kinase C (PKC) by treatment of cells with phorbol 12-myristate 13-acetate (PMA) enhanced sodium-dependent phosphate (Na/P_i) uptake. Studies now have been carried out to determine which type of Na/P_i transporter (Pit-1 or Pit-2) is regulated by PKC and which PKC isotypes are involved in the up-regulation of Na/P_i uptake by the Na/P_i transporter/viral receptor. It was found that the activation of short term (2-min) Na/P_i uptake by PMA is abolished when cells are infected with amphotropic murine retrovirus (binds Pit-2 receptor) but not with gibbon ape leukemia retrovirus (binds Pit-1 receptor), indicating that Pit-2 is the form of Na/P_i transporter/viral receptor regulated by PKC. The PKC-mediated activation of Pit-2 was blocked by pretreating cells with the pan-PKC inhibitor bisindolylmaleimide but not with the conventional PKC isotype inhibitor Gö 6976, suggesting that a novel PKC isotype is required to regulate Pit-2. Overexpression of PKC, but not of PKC, -, or -, was found to mimic the activation of Na/P_i uptake. To further establish that PKC is involved in the regulation of Pit-2, cells were treated with PKC-selective antisense oligonucleotides. Treatment with PKC antisense oligonucleotides decreased the PMA-induced activation of Na/P_i uptake. These results indicate that PMA-induced stimulation of Na/P_i uptake by Pit-2 is specifically mediated through activation of PKC.

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