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|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.
|Keywords: ||Nerve growth factor|
c-Jun N-terminal kinase
PC12 pheochromocytoma cells
|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/|
|Appears in Collections:||BICH Journal/Magazine Articles|
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