Phosphatidylethanolaminebinding protein is not involved in µopioid receptor-mediated regulation of extracellular signalregulated kinase

Author：

Publisher： Spandidos Publications

E-ISSN： 1791-3004|11|5|3368-3374

ISSN： 1791-2997

Source： Molecular Medicine Reports, Vol.11, Iss.5, 2015-01, pp. : 3368-3374

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Abstract

Stimulation of the µopioid receptor activates extracellular signalregulated kinase (ERK), however, the mechanism by which this occurs remains to be elucidated. Phosphatidylethanolaminebinding protein (PEBP) has been reported to act as a negative regulator of the ERK cascade (RafMEKERK) by binding to Raf1 kinase. In the present study, the role of PEBP in µopioid receptormediated ERK activation was investigated in Chinese hamster ovary/µ cells and SHSY5Y cells, as well as in human embryonic kidney 293 cells expressing other types of G proteincoupled receptors. The acute activation of µopioid receptors by morphine or (DAla2, MePhe4, Gly5ol) enkephalin induced a rapid activation of ERK. Prolonged morphine treatment did not affect the phosphorylation level of ERK compared with control cells, but the phosphorylation level of ERK decreased markedly when cells were precipitated with naloxone following chronic morphine treatment. For the phosphorylation of PEBP, no change was identified under the designated drug treatment and exposure duration. A total of two other types of G proteincoupled receptors, including Gscoupled dopamine D1 receptors and Gqcoupled adrenergic α1A receptors were also investigated and only the activation of adrenergic α1A receptors induced an upregulated phosphorylation of PEBP, which was protein kinase C activity dependent. Thus, PEBP did not have a significant role in µopioid receptormediated regulation of ERK.