dc.citation.conferencePlace |
KO |
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dc.citation.conferencePlace |
Seoul, Korea |
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dc.citation.title |
Asian-Pacific Society for Neurochemistry 4th Meeting |
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dc.contributor.author |
Lee, YH |
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dc.contributor.author |
Bae, SS |
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dc.contributor.author |
Seo, JK |
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dc.contributor.author |
Choi, I |
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dc.contributor.author |
Ryu, SH |
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dc.contributor.author |
Suh, Pann-Ghill |
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dc.date.accessioned |
2023-12-20T06:39:56Z |
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dc.date.available |
2023-12-20T06:39:56Z |
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dc.date.created |
2014-12-23 |
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dc.date.issued |
1998-06-24 |
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dc.description.abstract |
Phospholipase C (PLC)-gamma1 plays a pivotal role in the signal transduction pathway mediated by growth factors. In this study, we found that neurite outgrowth of pheochromocytoma (PC12) cells was significantly induced by interleukin-6 (IL-6). Stimulation of PC12 cells with IL-6 led to tyrosine phosphorylation of PLC-gamma1 in a dose- and time-dependent manner. IL-6 stimulation also increased the hydrolysis of phosphatidylinositol 4,5-bisphosphate. Accumulation of total inositol phosphate as well as tyrosine phosphorylation of PLC-gamma1 was inhibited by the pretreatment of protein kinase inhibitors such as genistein and staurosporine. These results suggest that PLC-gamma1 may be involved in the signal transduction pathway of IL-6-induced PC12 cell differentiation |
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dc.identifier.bibliographicCitation |
Asian-Pacific Society for Neurochemistry 4th Meeting |
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dc.identifier.uri |
https://scholarworks.unist.ac.kr/handle/201301/52339 |
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dc.publisher |
J. Neurochem. Suppl. 2, S38D, |
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dc.title |
Interleukin-6-induced tyrosine phosphorylation of phospholipase C-gamma1 in PC12 cells |
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dc.type |
Conference Paper |
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dc.date.conferenceDate |
1998-06-24 |
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