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Down‐Regulation of c‐ neu Receptors by Nerve Growth Factor in PC12 Cells
Author(s) -
Oshima Mari,
Weiss Linnea,
Dougall William C.,
Greene Mark I.,
Guroff Gordon
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.65010427.x
Subject(s) - nerve growth factor , phosphorylation , receptor , tyrosine phosphorylation , endocrinology , medicine , trk receptor , epidermal growth factor , tyrosine , biology , microbiology and biotechnology , serine , growth factor , chemistry , biochemistry
A small number of p185 c‐ neu receptors have been found on PC12 cells. These receptors show some basal phosphorylation in quiescent cells. When the cells are treated with nerve growth factor (NGF) for a short time, some increase in phosphorylation is seen, mainly on serine and threonine residues, and this is accompanied by a slight shift in the apparent molecular weight. Epidermal growth factor (EGF) also increases the phosphorylation of p185 c‐ neu , in this case on tyrosine residues. Neither heregulin‐β1 nor gp30 stimulates the tyrosine phosphorylation of p185 c‐ neu , and neither has a proliferative effect on the cells. Treatment of the cells with NGF for 5 days produces a 70–80% reduction in the number of p185 c‐ neu receptors. This down‐regulation does not occur when PC12nnr5 cells, which lack the high‐affinity NGF receptor, p140 trk , are treated with NGF.The level of p185 c‐ neu mRNA is not altered by NGF treatment, suggesting that the down‐regulation is due to either a translational or a posttranslational alteration.