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

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Phospholipase C-β3 mediates the thrombin-induced Ca2+ response in glial cells

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dc.contributor.author Suh, Pann-Ghill ko
dc.contributor.author Hwang, Jong-Ik ko
dc.contributor.author Choi, Jung-Woong ko
dc.contributor.author Kim, Daesoo ko
dc.contributor.author Ryu, Sung Ho ko
dc.contributor.author Shin, Kum-Joo ko
dc.contributor.author Oh, Yong-Seok ko
dc.contributor.author Lee, Zee-Won ko
dc.contributor.author Ha, Kwon-Soo ko
dc.contributor.author Shin, Hee-Sup ko
dc.date.available 2015-03-09T00:33:59Z -
dc.date.created 2015-01-16 ko
dc.date.issued 2005-06 ko
dc.identifier.citation MOLECULES AND CELLS, v.19, no.3, pp.375 - 381 ko
dc.identifier.issn 1016-8478 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/10827 -
dc.description.abstract Phospholipase C-β (PLC-β) hydrolyses phosphatidylinositol 4,5-bisphosphate and generates inositol 1,4,5-trisphosphate in response to activation of various G protein-coupled receptors (GPCRs). Using glial cells from knock-out mice lacking either PLC-β1 [PLC-β1 (-/-)] or PLC-β3 [PLC-β3 (-/-)], we examined which isotype of PLC- participated in the cellular signaling events triggered by thrombin. Generation of inositol phosphates (IPs) was enhanced by thrombin in PLC-β1 (-/-) cells, but was negligible in PLC-β3 (-/-) cells. Expression of PLC-β in PLC-β(-/-) cells resulted in an increase in pertussis toxin (PTx)-sensitive IPs in response to thrombin as well as to PARI-specific peptide, while expression of PLC-β1 in PLC-β1 (-/-) cells did not have any effect on IP generation. The thrombin-induced [Ca2+]i increase was delayed and attenuated in PLC-β3 (-/-) cells, but normal in PLC-β1 (-/-) cells. Pertussis toxin evoked a delayed [Ca2+], increase in PLC-β3 (-/-) cells as well as in PLC-β1 (-/-) cells. These results suggest that activation of PLC-β3 by pertussis toxin-sensitive G proteins is responsible for the transient [Ca2+], increase in response to thrombin, whereas the delayed [Ca2+], increase may be due to activation of some other PLC, such as PLC-β4, acting via PTx-insensitive G proteins. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher KOREAN SOC MOLECULAR & CELLULAR BIOLOGY ko
dc.title Phospholipase C-β3 mediates the thrombin-induced Ca2+ response in glial cells ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-27244445213 ko
dc.identifier.wosid 000231331100020 ko
dc.type.rims ART ko
dc.description.scopustc 11 *
dc.date.scptcdate 2015-11-04 *
dc.identifier.doi 10.1016/j.atherosclerosis.2004.12.046 ko
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