Protein kinase C-mediated phosphorylation of Kv beta 2 in adult rat brain.
Protein kinase C-mediated phosphorylation of Kv beta 2 in adult rat brain.
复制标题
成年大鼠脑中蛋白激酶 C 介导的 Kv beta 2 磷酸化。
DOI:
10.1023/b:nere.0000042215.92952.3d
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发表时间:
2004
影响因子:
4.4
通讯作者:
Prystowsky,MichaelB
中科院分区:
文献类型:
--
作者:
Wang,Xintao;Zhang,Jie;Berkowski,StanM;Knowleg,Heather;Chandramouly,AB;Downens,Martha;Prystowsky,MichaelB
The phosphorylation of Kvβ2 was investigated by different protein kinases. Protein kinase A catalytic subunit (PKA-CS) yielded the greatest phosphorylation of recombinant Kvβ2 (rKvβ2), with limited phosphorylation by protein kinase C catalytic subunit (PKC-CS) and no detectable phosphorylation by casein kinase II (CKII). Protein kinase(s) from adult rat brain lysate phosphorylated both rKvβ2 and endogenous Kvβ. The PKA inhibitor, PKI 6-22, fully inhibited PKA-mediated phophorylation of rKvβ2 yet showed minimal inhibition of kinase activity present in rat brain. The inhibitor Gö 6983, that blocks PKCα, PKCβ, PKCγ, PKCδ and PKCζ activities, inhibited rKvβ2 phosphorylation by rat brain kinases, with no inhibition by Gö 6976 which blocks PKCα and PKCβΙ activities. Dose-response analysis of Gö 6983 inhibitory activity indicates that at least two PKC isozymes account for the kinase activity present in rat brain. Τhus, while PKA was the most active protein kinase to phosphorylate rKvβ2 in vitro, Kvβ2 phosphorylation in the rat brain is mainly mediated by PKC isozymes.