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Am J Physiol Lung Cell Mol Physiol 284: L1037-L1044, 2003. First published January 31, 2003; doi:10.1152/ajplung.00308.2002
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Vol. 284, Issue 6, L1037-L1044, June 2003

Classical isoforms of PKC as regulators of CAT-1 transporter activity in pulmonary artery endothelial cells

Karina Y. Krotova, Sergey I. Zharikov, and Edward R. Block

Department of Medicine, University of Florida College of Medicine; and Research Service, Malcom Randall VA Medical Center, Gainesville, Florida 32610

We examined which isoforms of protein kinase C (PKC) may be involved in the regulation of cationic amino acid transporter-1 (CAT-1) transport activity in cultured pulmonary artery endothelial cells (PAEC). An activator of classical and novel isoforms of PKC, phorbol 12-myristate-13-acetate (PMA; 100 nM), inhibited CAT-1-mediated L-arginine transport in PAEC after a 1-h treatment and activated L-arginine uptake after an 18-h treatment of cells. These changes in L-arginine transport were not related to the changes in the expression of the CAT-1 transporter. The inhibitory effect of PMA on L-arginine transport was accompanied by a translocation of PKCalpha (a classical PKC isoform) from the cytosol to the membrane fraction, whereas the activating effect of PMA on L-arginine transport was accompanied by full depletion of the expression of PKCalpha in PAEC. A selective activator of Ca2+-dependent classical isoforms of PKC, thymeleatoxin (Thy; 100 nM; 1-h and 18-h treatments), induced the same changes in L-arginine uptake and PKCalpha translocation and depletion as PMA. The effects of PMA and Thy on L-arginine transport in PAEC were attenuated by a selective inhibitor of classical PKC isoforms Go 6976 (1 µM). Phosphatidylinositol-3,4,5-triphosphate-dipalmitoyl (PIP; 5 µM), which activates novel PKC isoforms, did not affect L-arginine transport in PAEC after 1-h and 18-h treatment of cells. PIP (5 µM; 1 h) induced the translocation of PKCepsilon (a novel PKC isoform) from the cytosolic to the particulate fraction and did not affect the translocation of PKCalpha . These results demonstrate that classical isoforms of PKC are involved in the regulation of CAT-1 transport activity in PAEC. We suggest that translocation of PKCalpha to the plasma membrane induces phosphorylation of the CAT-1 transporter, which leads to inhibition of its transport activity in PAEC. In contrast, depletion of PKCalpha after long-term treatment with PMA or Thy promotes dephosphorylation of the CAT-1 transporter and activation of its activity.

cationic amino acid transporter; L-arginine transport


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