DC Field | Value | Language |
---|---|---|
dc.contributor.author | Bae, SS | - |
dc.contributor.author | Perry, DK | - |
dc.contributor.author | Oh, YS | - |
dc.contributor.author | Choi, JH | - |
dc.contributor.author | Galadari, SH | - |
dc.contributor.author | Ghayur, T | - |
dc.contributor.author | Ryu, SH | - |
dc.contributor.author | Hannun, YA | - |
dc.contributor.author | Suh, PG | - |
dc.date.accessioned | 2016-03-31T13:30:38Z | - |
dc.date.available | 2016-03-31T13:30:38Z | - |
dc.date.created | 2009-08-12 | - |
dc.date.issued | 2000-06 | - |
dc.identifier.issn | 0892-6638 | - |
dc.identifier.other | 2000-OAK-0000001350 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/19987 | - |
dc.description.abstract | Apoptosis is a cell suicide mechanism that requires the activation of cellular death proteases for its induction. We examined whether the progress of apoptosis involves cleavage of phospholipase C-gamma 1 (PLC-gamma 1), which plays a pivotal role in mitogenic signaling pathway. Pretreatment of T leukemic Molt-4 cells with PLC inhibitors such as U-73122 or ET-18-OCH3 potentiated etoposide-induced apoptosis in these cells. PLC-gamma 1 was fragmented when Molt-4 cells were treated with several apoptotic stimuli such as etoposide, ceramides, and tumor necrosis factor alpha. Cleavage of PLC-gamma 1 was blocked by overexpression of Bcl-2 and by specific inhibitors of caspases such as Z-DEVD-CH2F and YVAD-cmk. Purified caspase-3 and caspase-7, group II caspases, cleaved PLC-gamma 1 in vitro and generated a cleavage product of the same size as that observed in vivo, suggesting that PLC-gamma 1 is cleaved by group II caspases in vivo. From point mutagenesis studies, Ala-Glu-Pro-Asp(770) was identified to be a cleavage site within PLC-gamma 1. Epidermal growth factor receptor (EGFR) -induced tyrosine phosphorylation of PLC-gamma 1 resulted in resistance to cleavage by caspase-3 in vitro. Furthermore, cleaved PLC-gamma 1 could not be tyrosine-phosphorylated by EGFR in vitro. In addition, tyrosine-phosphorylated PLC-gamma 1 was not significantly cleaved during etoposide-induced apoptosis in Molt-4 cells. This suggests that the growth factor-induced tyrosine phosphorylation may suppress apoptosis-induced fragmentation of PLC-gamma 1. We provide evidence for the biochemical relationship between PLC-gamma 1-mediated signal pathway and apoptotic signal pathway, indicating that the defect of PLC-gamma 1-mediated signaling pathway can facilitate an apoptotic progression.-Bae, S. S., Ferry, D. K., Oh, Y. S., Choi, J. H., Galadari, S. H., Ghayur, T., Ryu, S. H., Hannun, Y. A., Suh, P.-G. Proteolytic cleavage of phospholipase C-gamma 1 during apoptosis in Molt-4 cells. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | FEDERATION AMER SOC EXP BIOL | - |
dc.relation.isPartOf | FASEB JOURNAL | - |
dc.subject | PLC-gamma 1 | - |
dc.subject | proteolysis | - |
dc.subject | tyrosine phosphorylation | - |
dc.subject | CYTOCHROME-C | - |
dc.subject | FOCAL ADHESION | - |
dc.subject | CASPASE FAMILY | - |
dc.subject | SH3 DOMAIN | - |
dc.subject | DEATH | - |
dc.subject | PROTEIN | - |
dc.subject | ACTIVATION | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | BCL-2 | - |
dc.subject | ELEGANS | - |
dc.title | Proteolytic cleavage of phospholipase C-gamma 1 during apoptosis in Molt-4 cells | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1096/fasebj.14.9.1083 | - |
dc.author.google | Bae, SS | - |
dc.author.google | Perry, DK | - |
dc.author.google | Oh, YS | - |
dc.author.google | Choi, JH | - |
dc.author.google | Galadari, SH | - |
dc.author.google | Ghayur, T | - |
dc.author.google | Ryu, SH | - |
dc.author.google | Hannun, YA | - |
dc.author.google | Suh, PG | - |
dc.relation.volume | 14 | - |
dc.relation.issue | 9 | - |
dc.relation.startpage | 1083 | - |
dc.relation.lastpage | 1092 | - |
dc.contributor.id | 10052640 | - |
dc.relation.journal | FASEB JOURNAL | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | FASEB JOURNAL, v.14, no.9, pp.1083 - 1092 | - |
dc.identifier.wosid | 000087427300004 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 1092 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 1083 | - |
dc.citation.title | FASEB JOURNAL | - |
dc.citation.volume | 14 | - |
dc.contributor.affiliatedAuthor | Ryu, SH | - |
dc.contributor.affiliatedAuthor | Suh, PG | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 62 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | CYTOCHROME-C | - |
dc.subject.keywordPlus | FOCAL ADHESION | - |
dc.subject.keywordPlus | CASPASE FAMILY | - |
dc.subject.keywordPlus | SH3 DOMAIN | - |
dc.subject.keywordPlus | DEATH | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | BCL-2 | - |
dc.subject.keywordPlus | ELEGANS | - |
dc.subject.keywordAuthor | PLC-gamma 1 | - |
dc.subject.keywordAuthor | proteolysis | - |
dc.subject.keywordAuthor | tyrosine phosphorylation | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Life Sciences & Biomedicine - Other Topics | - |
dc.relation.journalResearchArea | Cell Biology | - |
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