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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Src homology domains of phospholipase C gamma 1 inhibit nerve growth factor-induced differentiation of PC12 cells

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dc.contributor.author Bae, Sun Sik ko
dc.contributor.author Lee, Young Han ko
dc.contributor.author Chang, Jong-Soo ko
dc.contributor.author Galadari, Sehamuddin H. ko
dc.contributor.author Kim, Yong Sik ko
dc.contributor.author Ryu, Sung Ho ko
dc.contributor.author Suh, Pann-Ghill ko
dc.date.available 2015-09-01T07:25:19Z -
dc.date.created 2015-08-20 ko
dc.date.issued 1998-07 ko
dc.identifier.citation JOURNAL OF NEUROCHEMISTRY, v.71, no.1, pp.178 - 185 ko
dc.identifier.issn 0022-3042 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/16457 -
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 ko
dc.description.statementofresponsibility open -
dc.language 영어 ko
dc.publisher WILEY-BLACKWELL ko
dc.title Src homology domains of phospholipase C gamma 1 inhibit nerve growth factor-induced differentiation of PC12 cells ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-0346629933 ko
dc.identifier.wosid 000074283600019 ko
dc.type.rims ART ko
dc.description.wostc 38 *
dc.description.scopustc 41 *
dc.date.tcdate 2015-12-28 *
dc.date.scptcdate 2015-11-04 *
dc.identifier.doi 10.1046/j.1471-4159.1998.71010178.x ko
dc.identifier.url http://onlinelibrary.wiley.com/doi/10.1046/j.1471-4159.1998.71010178.x/abstract ko
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