There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 1092 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 1083 | - |
dc.citation.title | FASEB JOURNAL | - |
dc.citation.volume | 14 | - |
dc.contributor.author | Bae, SS | - |
dc.contributor.author | Perry, DK | - |
dc.contributor.author | Oh, YS | - |
dc.contributor.author | Choi, Jang Hyun | - |
dc.contributor.author | Galadari, SH | - |
dc.contributor.author | Ghayur, T | - |
dc.contributor.author | Ryu, SH | - |
dc.contributor.author | Hannun, YA | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T12:07:37Z | - |
dc.date.available | 2023-12-22T12:07:37Z | - |
dc.date.created | 2014-10-14 | - |
dc.date.issued | 2000-06 | - |
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-γ1 (PLC-γ1), 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-γ1 was fragmented when Molt- 4 cells were treated with several apoptotic stimuli such as etoposide, ceramides, and tumor necrosis factor α. Cleavage of PLC-γ1 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-γ1 in vitro and generated a cleavage product of the same size as that observed in vivo, suggesting that PLC-γ1 is cleaved by group II caspases in vivo. From point mutagenesis studies, Ala-Glu-Pro-Asp770 was identified to be a cleavage site within PLC-γ1. Epidermal growth factor receptor (EGFR) -induced tyrosine phosphorylation of PLC-γ1 resulted in resistance to cleavage by caspase-3 in vitro. Furthermore, cleaved PLC-γ1 could not be tyrosine-phosphorylated by EGFR in vitro. In addition, tyrosine- phosphorylated PLC-γ1 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- γ1. We provide evidence for the biochemical relationship between PLC-γ1- mediated signal pathway and apoptotic signal pathway, indicating that the defect of PLC-γ1-mediated signaling pathway can facilitate an apoptotic progression. | - |
dc.identifier.bibliographicCitation | FASEB JOURNAL, v.14, no.9, pp.1083 - 1092 | - |
dc.identifier.issn | 0892-6638 | - |
dc.identifier.scopusid | 2-s2.0-0001455392 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/7296 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0001455392 | - |
dc.identifier.wosid | 000087427300004 | - |
dc.language | 영어 | - |
dc.publisher | FEDERATION AMER SOC EXP BIOL | - |
dc.title | Proteolytic cleavage of phospholipase C-gamma 1 during apoptosis in Molt-4 cells | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.