Cited 83 times in
Death induction by recombinant native TRAIL and its prevention by a caspase 9 inhibitor in primary human esophageal epithelial cells
DC Field | Value | Language |
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dc.contributor.author | 김건홍 | - |
dc.date.accessioned | 2015-07-14T17:23:11Z | - |
dc.date.available | 2015-07-14T17:23:11Z | - |
dc.date.issued | 2004 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/112777 | - |
dc.description.abstract | The cytotoxic death ligand TRAIL (tumor necrosis factor-related apoptosis-inducing ligand) is a tumor-specific agent under development as a novel anticancer therapeutic agent. However, some reports have demonstrated toxicity of certain TRAIL preparations toward human hepatocytes and keratinocytes through a caspase-dependent mechanism that involves activation of the extrinsic death pathway and Type II signaling through the mitochondria. We have isolated and purified both His-tagged protein and three versions of native recombinant human TRAIL protein from Escherichia coli. We found that 5 mm dithiothreitol in the purification process enhanced oligomerization of TRAIL and resulted in the formation of hyper-oligomerized TRAILs, including hexamers and nonomers with an extremely high potency in apoptosis induction. Although death-inducing signaling complex formation was much more efficient in cells treated with hyper-oligomerized TRAILs, this did not convert TRAIL-sensitive Type II HCT116 colon tumor cells to a Type I death pattern as judged by their continued sensitivity to a caspase 9 inhibitor. Moreover, TRAIL-resistant Type II Bax-null colon carcinoma cells were not converted to a TRAIL-sensitive Type I state by hyper-oligomerized TRAIL. Primary human esophageal epithelial 2 cells were found to be sensitive to all TRAIL preparations used, including trimer TRAIL. TRAIL-induced death in esophageal epithelial 2 cells was prevented by caspase 9 inhibition for up to 4 h after TRAIL exposure. This result suggests a possible therapeutic application of caspase 9 inhibition as a strategy to reverse TRAIL toxicity. Hyper-oligomerized TRAIL may be considered as an alternative agent for testing in clinical trials. | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 40044~40052 | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Adenocarcinoma | - |
dc.subject.MESH | Antineoplastic Agents/pharmacology* | - |
dc.subject.MESH | Caspase 9 | - |
dc.subject.MESH | Caspase Inhibitors* | - |
dc.subject.MESH | Caspases/metabolism | - |
dc.subject.MESH | Cell Death/drug effects | - |
dc.subject.MESH | Cell Line, Tumor/drug effects | - |
dc.subject.MESH | Epithelial Cells/cytology | - |
dc.subject.MESH | Epithelial Cells/drug effects* | - |
dc.subject.MESH | Esophagus/cytology | - |
dc.subject.MESH | GPI-Linked Proteins | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Lung Neoplasms | - |
dc.subject.MESH | Receptors, TNF-Related Apoptosis-Inducing Ligand | - |
dc.subject.MESH | Receptors, Tumor Necrosis Factor/genetics* | - |
dc.subject.MESH | Receptors, Tumor Necrosis Factor/therapeutic use | - |
dc.subject.MESH | Receptors, Tumor Necrosis Factor, Member 10c | - |
dc.subject.MESH | Recombinant Proteins/genetics | - |
dc.subject.MESH | Recombinant Proteins/toxicity* | - |
dc.subject.MESH | Tumor Necrosis Factor Decoy Receptors | - |
dc.title | Death induction by recombinant native TRAIL and its prevention by a caspase 9 inhibitor in primary human esophageal epithelial cells | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Biochemistry & Molecular Biology (생화학,분자생물학) | - |
dc.contributor.googleauthor | Seok-Hyun Kim | - |
dc.contributor.googleauthor | Kunhong Kim | - |
dc.contributor.googleauthor | Wafik S. El-Deiry | - |
dc.contributor.googleauthor | Youhai Chen | - |
dc.contributor.googleauthor | Anil K. Rustgi | - |
dc.contributor.googleauthor | Meenhard Herlyn | - |
dc.contributor.googleauthor | David T. Dicker | - |
dc.contributor.googleauthor | Jae G. Kwagh | - |
dc.identifier.doi | 10.1074/jbc.M404541200 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A00289 | - |
dc.relation.journalcode | J01258 | - |
dc.identifier.eissn | 1083-351X | - |
dc.identifier.pmid | 15226295 | - |
dc.contributor.alternativeName | Kim, Kun Hong | - |
dc.contributor.affiliatedAuthor | Kim, Kun Hong | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 279 | - |
dc.citation.number | 38 | - |
dc.citation.startPage | 40044 | - |
dc.citation.endPage | 40052 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.279(38) : 40044-40052, 2004 | - |
dc.identifier.rimsid | 44499 | - |
dc.type.rims | ART | - |
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