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Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/6243
Title: Multiple Gi proteins participate in nerve growth factor-induced activation of c-Jun N-terminal kinases in PC12 cells
Authors: Tso, Ha
Morris, Christina J.
Yung, Lisa Y.
Ip, Nancy Y.
Wong, Yung-Hou
Keywords: Nerve growth factor
c-Jun N-terminal kinase
Gi/o proteins
PC12 pheochromocytoma cells
Neurite outgrowth
Trk-A receptor
Issue Date: Jun-2009
Citation: Neurochemical research, v. 34, no. 6, 2009
Abstract: Nerve growth factor (NGF)-mediated activation of mitogen-activated protein kinases (MAPK) is critical for differentiation and apoptosis of PC12 cells. Since NGF employs stress-activated c-Jun N-terminal kinase (JNK) to regulate both programmed cell death and neurite outgrowth of PC12 cells, we examined NGF-regulated JNK activity and the role of Gi/o proteins. Induction of JNK phosphorylation by NGF occurred in a time- and dose-dependent manner and was partially inhibited by pertussis toxin (PTX). To discern the participation of various signaling intermediates, PC12 cells were treated with specific inhibitors prior to NGF challenge. NGF-elevated JNK activity was abolished by inhibitors of JNK, p38 MAPK, Src, JAK3 and MEK1/2. NGF-dependent JNK phosphorylation became insensitive to PTX treatment upon transient expressions of Gαz or the PTX-resistant mutants of Gαi1-3 and GαoA. Collectively, these studies indicate that NGF-dependent JNK activity may be mediated via Gi1-3 proteins, JAK3, Src, p38 MAPK and the MEK/ERK cascade.
Rights: The original publication is available at http://www.springerlink.com/
URI: http://hdl.handle.net/1783.1/6243
Appears in Collections:BICH Journal/Magazine Articles

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