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. 2017 Aug 22;11:253. doi: 10.3389/fncel.2017.00253

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Copyright © 2017 Mortensen, Larsen and Amara.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Protein kinase C (PKC)-mediated down regulation of norepinephrine transporter (NET) activity in PC12 cells is not dependent on phosphorylation of residues 258 and 259. Naïve PC12 cells were transiently transfected for 48 h with cDNAs for WT-NET or T258A/S259A-NET. Radiolabeled uptake was measured following 30 min incubation with PKC activator phorbol 12-myristate 13-acetate (PMA; 1 μM) subtracting mock-transfected cells. All experiments were performed in triplicate in three independent experiments. Both cDNAs were significantly affected by PKC activation (*p < 0.05) but no significant difference (N.S.) in the magnitude of the PKC-mediated downregulation of uptake was observed between the two cDNAs (two-way ANOVA with Bonferroni post hoc analysis).