DC Field | Value | Language |
---|---|---|
dc.contributor.author | Bae, SS | - |
dc.contributor.author | Lee, YH | - |
dc.contributor.author | Chang, JS | - |
dc.contributor.author | Galadari, SH | - |
dc.contributor.author | Kim, YS | - |
dc.contributor.author | Ryu, SH | - |
dc.contributor.author | Suh, PG | - |
dc.contributor.author | 서판길 | - |
dc.date.accessioned | 2016-03-31T13:52:38Z | - |
dc.date.available | 2016-03-31T13:52:38Z | - |
dc.date.issued | 1998-01 | - |
dc.identifier.citation | JOURNAL OF NEUROCHEMISTRY | - |
dc.identifier.citation | v.71 | - |
dc.identifier.citation | no.1 | - |
dc.identifier.citation | pp.178-185 | - |
dc.identifier.issn | 0022-3042 | - |
dc.identifier.other | 1998-OAK-0000000259 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/20750 | - |
dc.description.abstract | Phospholipase C gamma 1 (PLC-gamma 1) is phosphorylated on treatment of cells with nerve growth factor (NGF).To assess the role of PLC-gamma 1 in mediating the neuronal differentiation induced by NGF treatment, we established PC12 cells that overexpress whole PLC-gamma 1 (PLC-gamma 1PC12), the SH2-SH2-SH3 domain (PLC-gamma 1SH223PC12), SH2-SH2-deleted mutants (PLC-gamma 1 Delta SH22PC12), and SH3-deleted mutants (PLC-gamma 1 Delta SH3PC12). Overexpressed whole PLC-yl or the SH2-SH2-SH3 domain of PLC-gamma 1 stimulated cell growth and inhibited NGF-induced neurite outgrowth of PC12 cells. However, cells expressing PLC-yl lacking the SH2-SH2 domain or the SH3 domain had no effect on NGF-induced neuronal differentiation. Overexpression of intact PLC-gamma 1 resulted in a threefold increase in total inositol phosphate accumulation on treatment with NGF. However, overexpression of the SH2-SH2-SH3 domain of PLC-gamma 1 did not alter total inositol phosphate accumulation. To investigate whether the SH2-SH2-SH3 domain of PLC-gamma 1 can mediate the NGF-induced signal, tyrosine phosphorylation of the SH2-SH2-SH3 domain of PLC-gamma 1 on NGF treatment was examined. The SH2-SH2-SH3 domain of PLC-gamma 1 as well as intact PLC-gamma 1 could be tyrosine-phosphorylated on NGF treatment. These results indicate that the overexpressed SH2-SH2-SH3 domain of PLC-gamma 1 can block the differentiation of PC12 cells induced by NGF and that the inhibition appears not to be related to the lipase activity of PLC-gamma 1 but to the SH2-SH2-SH3 domain of PLC-gamma 1. | - |
dc.description.statementofresponsibility | X | - |
dc.publisher | LIPPINCOTT WILLIAMS & WILKINS | - |
dc.subject | nerve growth factor | - |
dc.subject | signal transduction | - |
dc.subject | PC12 cells | - |
dc.subject | phospholipase C gamma 1 | - |
dc.subject | differentiation | - |
dc.subject | proliferation | - |
dc.subject | SIGNAL-TRANSDUCTION | - |
dc.subject | NEURONAL DIFFERENTIATION | - |
dc.subject | DNA-SYNTHESIS | - |
dc.subject | C-GAMMA-1 | - |
dc.subject | PROTEIN | - |
dc.subject | KINASE | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | HYDROLYSIS | - |
dc.subject | ACTIVATION | - |
dc.subject | BINDING | - |
dc.title | Src homology domains of phospholipase C gamma 1 inhibit nerve growth factor-induced differentiation of PC12 cells | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.author.google | Bae, SS | - |
dc.author.google | Lee, YH | - |
dc.author.google | Chang, JS | - |
dc.author.google | Galadari, SH | - |
dc.author.google | Kim, YS | - |
dc.author.google | Ryu, SH | - |
dc.author.google | Suh, PG | - |
dc.relation.volume | 71 | - |
dc.relation.issue | 1 | - |
dc.relation.startpage | 178 | - |
dc.relation.lastpage | 185 | - |
dc.contributor.id | 10052640 | - |
dc.publisher.location | US | - |
dc.relation.journal | JOURNAL OF NEUROCHEMISTRY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.docType | MEETING ABSTRACT | - |
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