Conventional protein kinase C isoforms regulate human dopamine transporter activity in Xenopus oocytes
Conventional protein kinase C isoforms regulate human dopamine transporter activity in Xenopus oocytes
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DOI：
10.1016/s0014-5793(02)02554-1
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发表时间：
2002-04-10
期刊：
影响因子：
3.5
通讯作者：
Zahniser, NR
中科院分区：
文献类型：
--
作者：
Doolen, S;Zahniser, NR
在表达人(h)DAT的非洲爪蟾卵母细胞中，验证了特异性蛋白激酶C （PKC）亚型调节多巴胺转运蛋白（DAT）功能的假设。使用10 nM phorbol 12-肉豆蔻酸13-醋酸酯（PMA）激活传统PKCs （cPKCs）和新型PKCs (nPKCs)，可显著抑制dat相关的运输电流。这种效应被同型非选择性PKC抑制剂、cPKCs和deltaPKC的选择性抑制剂以及Ca2+螯合逆转。相比之下，epsilonPKC易位抑制剂肽对pma诱导的hDAT转运相关电流的抑制没有影响。因此，PMA调节hDAT在卵母细胞中的表达的主要机制似乎是通过激活cPKC。(C) 2002年欧洲生化学会联合会。Elsevier Science B.V.版权所有。
The hypothesis that specific protein kinase C (PKC) isoforms regulate dopamine transporter (DAT) function was tested in Xenopus laevis oocytes expressing human (h)DAT. Activation of conventional PKCs (cPKCs) and novel PKCs (nPKCs) using 10 nM phorbol 12-myristate 13-acetate (PMA) significantly inhibited DAT-associated transport currents. This effect was reversed by isoform-non-selective PKC inhibitors, selective inhibitors of cPKCs and deltaPKC, and by Ca2+ chelation. By contrast, the epsilonPKC translocation inhibitor peptide had no effect on PMA-induced inhibition of hDAT transport-associated currents. Thus, the primary mechanism by which PMA regulates hDAT expressed in oocytes appears to be by activating cPKC(s). (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.