Nerve Growth Factor Induces Protein-Tyrosine Phosphorylation

When the sympathetic nerve-like cell line PC12 is exposed to nerve growth factor (NGF), there is a rapid and transient phosphorylation of tyrosine residues in cellular proteins, as demonstrated by immunoblotting of cell extracts with high-affinity polyclonal antibodies specific for phosphotyrosine r...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-09, Vol.85 (18), p.6788-6791
Main Author: Maher, Pamela A.
Format: Article
Language:English
Subjects:
Adrenal Gland Neoplasms - enzymology
Animals
Antibodies
Bucladesine - pharmacology
Cell growth
Cell Line
Cell lines
Epidermal Growth Factor - pharmacology
Immunosorbent Techniques
Insulin
Nerve Growth Factors - metabolism
Nerves
Neurons
PC12 cells
Pheochromocytoma - enzymology
Phosphorylation
Phosphotyrosine
Protein-Tyrosine Kinases - metabolism
Rats
Receptors
Tyrosine - analogs & derivatives
Tyrosine - metabolism
Viruses
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:When the sympathetic nerve-like cell line PC12 is exposed to nerve growth factor (NGF), there is a rapid and transient phosphorylation of tyrosine residues in cellular proteins, as demonstrated by immunoblotting of cell extracts with high-affinity polyclonal antibodies specific for phosphotyrosine residues. Epidermal growth factor (EGF), which does not cause the morphological differentiation of PC12 cells that is produced by NGF, also induces protein-tyrosine phosphorylation. The methyltransferase inhibitor, 5′-methylthioadenosine, which is known to block the NGF-mediated morphological differentiation of PC12 cells, also inhibits the induction of protein-tyrosine phosphorylation by NGF. 5′-Methylthioadenosine has no effect, however, on EGF-stimulated phosphorylation of tyrosine residues in cellular proteins. In addition, low temperature markedly slows the rate of protein-tyrosine phosphorylation stimulated by NGF, but it has no effect on the time course of protein-tyrosine phosphorylation induced by EGF. These data suggest that NGF and EGF induce protein-tyrosine phosphorylation in PC12 cells by different mechanisms.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.18.6788