PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity

M S Qui; S H Green

doi:10.1016/0896-6273(92)90033-a

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PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity

Journal article

Peer reviewed

PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity

M S Qui and S H Green

Neuron (Cambridge, Mass.), Vol.9(4), pp.705-717

10/1992

DOI: 10.1016/0896-6273(92)90033-a

PMID: 1382473

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Abstract

Expression of oncogenic ras in PC12 cells causes neuronal differentiation and sustained protein tyrosine phosphorylation and activity of extracellular signal-regulated kinases (ERKs), p42erk2 and p44erk1. Oncogenic N-ras-induced neuronal differentiation is inhibited by compounds that block ERK protein tyrosine phosphorylation or ERK activity, indicating that ERKs are not only activated by p21ras but serve as the primary downstream effectors of p21ras. Treatment of PC12 cells with nerve growth factor or fibroblast growth factor results in neuronal differentiation and in a sustained elevation of p21ras activity, of ERK activity, and of ERK tyrosine phosphorylation. Epidermal growth factor, which does not cause neuronal differentiation, stimulates only transient (< 1 hr) activation of p21ras and ERKs. These data indicate that transient activation of p21ras and, consequently, ERKs is not sufficient for induction of neuronal differentiation. Prolonged ERK activity is required: a consequence of sustained activation of p21ras by the growth factor receptor protein tyrosine kinase.

Neurites - physiology

Protein-Tyrosine Kinases - metabolism

Proto-Oncogene Proteins p21(ras) - genetics

Phosphotyrosine

Type C Phospholipases - metabolism

Immunoblotting

Neurons - cytology

Guanosine Triphosphate - metabolism

PC12 Cells

Tyrosine - analogs & derivatives

Nerve Growth Factors - pharmacology

Protein-Tyrosine Kinases - genetics

Time Factors

Isoenzymes - metabolism

Neurites - ultrastructure

Neurons - physiology

Guanosine Diphosphate - metabolism

Neurons - drug effects

Cell Differentiation - physiology

Proto-Oncogene Proteins p21(ras) - metabolism

Signal Transduction

Tyrosine - analysis

Calcium-Calmodulin-Dependent Protein Kinases

Proteins - genetics

Animals

Proteins - metabolism

Cell Differentiation - drug effects

Protein Binding

Epidermal Growth Factor - pharmacology

Kinetics

Genes, ras

Details

Title: Subtitle: PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity
Creators: M S Qui - Department of Biology, University of Iowa, Iowa City 52242
S H Green
Resource Type: Journal article
Publication Details: Neuron (Cambridge, Mass.), Vol.9(4), pp.705-717
DOI: 10.1016/0896-6273(92)90033-a
PMID: 1382473
NLM abbreviation: Neuron
ISSN: 0896-6273
eISSN: 1097-4199
Publisher: United States
Grant note: NS26538 / NINDS NIH HHS
Language: English
Date published: 10/1992
Academic Unit: Biology; Otolaryngology
Record Identifier: 9983991953002771

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