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|Title: ||Nerve growth factor-induced stimulation of p38 mitogen-activated protein kinase in PC12 cells is partially mediated via Gi/o proteins|
|Authors: ||Yung, Lisa Y.|
Wu, H. T.
Yu, C. H.
Ip, Nancy Y.
Nerve growth factor
|Issue Date: ||Aug-2008 |
|Citation: ||Cellular signalling, v. 20, iss. 8, August 2008, p. 1538-1544|
|Abstract: ||Differentiation of PC12 cells by nerve growth factor (NGF) requires the activation of various mitogen-activated protein kinases (MAPKs) including p38 MAPK. Accumulating evidence has suggested cross-talk regulation of NGF-induced responses by G protein-coupled receptors, thus we examined whether NGF utilizes Gi/o proteins to regulate p38 MAPK in PC12 cells. Induction of p38 MAPK phosphorylation by NGF occurred in a time- and dose-dependent manner and was partially inhibited by pertussis toxin (PTX). NGF-dependent p38 MAPK phosphorylation became insensitive to PTX treatment upon transient expressions of Gαz or the PTX-resistant mutants of Gαi2 and GαoA. Moreover, Gαi2 was co-immunoprecipitated with the TrkA receptor from PC12 cell lysates. To discern the participation of various signaling intermediates, PC12 cells were treated with a panel of specific inhibitors prior to the NGF challenge. NGF-induced p38 MAPK phosphorylation was abolished by inhibitors of Src (PP1, PP2, and SU6656) and MEK1/2 (U0126). Inhibition of the p38 MAPK pathway also suppressed NGF-induced PC12 cell differentiation. In contrast, inhibitors of JAK2, phospholipase C, protein kinase C and Ca2+/calmodulin-dependent kinase II did not affect the ability of NGF to activate p38 MAPK. Collectively, these studies indicate that NGF-dependent p38 MAPK activity may be mediated via Gαi2 protein, Src, and the MEK/ERK cascade.|
|Rights: ||Cellular signalling © copyright 2008 Elsevier. The Journal's web site is located at http://www.sciencedirect.com/|
|Appears in Collections:||BICH Journal/Magazine Articles|
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|NGFp38FigsCelllularSign.ppt||pre-published version||12938Kb||Microsoft Powerpoint||View/Open|
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