Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-4-2
pubmed:abstractText
We recently isolated mutant PC12 cell clones (PC84 cells) by transfection of PC12 cells with nerve growth factor (NGF) cDNA. These cells secreted active NGF and extended short processes, but proliferated faster than the parental PC12 cells. Because the expression level of p75, a low-affinity receptor for NGF, was significantly low, we suspected that NGF signaling via p75 was necessary for the growth arrest of the PC12 cells, and this was shown to be the case by repressing p75 function in PC12 cells. In this study, we examined the downstream signaling of p75, which would ultimately evoke the growth arrest. NGF is known to induce rapid phosphorylation of MAP kinase and Akt in PC12 cells, whereas in PC84 cells, MAP kinase was phosphorylated but the phosphorylation level of Akt was very low under the serum-free condition. This finding suggested that the low expression level of p75 in PC84 cells was the reason for the low Akt activation. Because Akt is known to be activated via phosphatidylinositol (PI) 3-kinase, we treated PC12 cells with a PI3-kinase inhibitor, Wortmannin, and found these cells did not cease proliferation in the presence of NGF. Furthermore, anti-p75 neutralizing antibody reduced NGF-induced phosphorylation of Akt in PC12 cells under the serum-free condition. Because we had already shown that PC12 cells treated with anti-p75 neutralizing antibody did not cease proliferation in the presence of NGF, these results suggest that NGF activates Akt via p75, which is necessary for the NGF-induced growth arrest of PC12 cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Akt1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Nerve Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, trkA, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nerve Growth Factor, http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0360-4012
pubmed:author
pubmed:copyrightInfo
Copyright 2003 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12671996-Androstadienes, pubmed-meshheading:12671996-Animals, pubmed-meshheading:12671996-Cell Division, pubmed-meshheading:12671996-Enzyme Inhibitors, pubmed-meshheading:12671996-Intracellular Fluid, pubmed-meshheading:12671996-Nerve Growth Factor, pubmed-meshheading:12671996-PC12 Cells, pubmed-meshheading:12671996-Phosphatidylinositol 3-Kinases, pubmed-meshheading:12671996-Phosphorylation, pubmed-meshheading:12671996-Protein-Serine-Threonine Kinases, pubmed-meshheading:12671996-Proto-Oncogene Proteins, pubmed-meshheading:12671996-Proto-Oncogene Proteins c-akt, pubmed-meshheading:12671996-Rats, pubmed-meshheading:12671996-Receptor, Nerve Growth Factor, pubmed-meshheading:12671996-Receptor, trkA, pubmed-meshheading:12671996-Receptors, Nerve Growth Factor, pubmed-meshheading:12671996-Signal Transduction, pubmed-meshheading:12671996-Tumor Cells, Cultured
pubmed:year
2003
pubmed:articleTitle
Growth arrest of PC12 cells by nerve growth factor is dependent on the phosphatidylinositol 3-kinase/Akt pathway via p75 neurotrophin receptor.
pubmed:affiliation
Laboratory of Molecular Biology, Gifu Pharmaceutical University, Gifu, Japan.
pubmed:publicationType
Journal Article