Cited 99 times in
Inhibition of apoptosis signal-regulating kinase 1 by nitric oxide through a thiol redox mechanism
DC Field | Value | Language |
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dc.contributor.author | 유제욱 | - |
dc.date.accessioned | 2015-07-14T17:30:00Z | - |
dc.date.available | 2015-07-14T17:30:00Z | - |
dc.date.issued | 2004 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/113006 | - |
dc.description.abstract | Nitric oxide is an endogenous thiol-reactive molecule that modulates the functions of many regulatory proteins by a thiol-redox mechanism. NO has now been shown to inhibit the activation of apoptosis signal-regulating kinase 1 (ASK1) in murine fibrosarcoma L929 cells through such a mechanism. Exposure of L929 cells to interferon-gamma resulted in the endogenous production of NO and in inhibition of the activation of ASK1 by hydrogen peroxide. The interferon-gamma-induced inhibition of ASK1 activity was blocked by N(G)-nitro-l-arginine, an inhibitor of NO synthase. Furthermore, the NO donor S-nitro-N-acetyl-dl-penicillamine (SNAP) inhibited ASK1 activity in vitro, and this inhibition was reversed by thiol-reducing agents such as dithiothreitol and beta-mercaptoethanol. SNAP did not inhibit the kinase activities of MKK3, MKK6, or p38 in vitro. The inhibition of ASK1 by interferon-gamma was not changed by 1H- (1,2,4)oxadiazolo[4,3-alpha]quinoxalin-1-one, an inhibitor of guanylyl cyclase nor was it mimicked by 8-bromo-cyclic GMP. Site-directed mutagenesis revealed that replacement of cysteine 869 of ASK1 by serine rendered this protein resistant to the inhibitory effects both of interferon-gamma in intact cells and of SNAP in vitro. Co-immunoprecipitation data showed that NO production inhibited a binding of ASK1, but not ASK1(C869S), to MKK3 or MKK6. Moreover, interferon-gamma induced the S-nitrosylation of endogenous ASK1 in L929 cells. Together, these results suggest that NO mediates the interferon-gamma-induced inhibition of ASK1 in L929 cells through a thiolredox mechanism. | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 7584~7590 | - |
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 | Animals | - |
dc.subject.MESH | Cell Line | - |
dc.subject.MESH | Cysteine | - |
dc.subject.MESH | Enzyme Activation/drug effects | - |
dc.subject.MESH | Enzyme Inhibitors/pharmacology* | - |
dc.subject.MESH | Fibrosarcoma | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Hydrogen Peroxide/pharmacology | - |
dc.subject.MESH | Interferon-gamma/pharmacology | - |
dc.subject.MESH | MAP Kinase Kinase Kinase 5 | - |
dc.subject.MESH | MAP Kinase Kinase Kinases/antagonists & inhibitors* | - |
dc.subject.MESH | MAP Kinase Kinase Kinases/chemistry | - |
dc.subject.MESH | MAP Kinase Kinase Kinases/genetics | - |
dc.subject.MESH | Mice | - |
dc.subject.MESH | Mutagenesis, Site-Directed | - |
dc.subject.MESH | Nitric Oxide/pharmacology* | - |
dc.subject.MESH | Nitric Oxide Donors/pharmacology | - |
dc.subject.MESH | Nitric Oxide Synthase/antagonists & inhibitors | - |
dc.subject.MESH | Nitroarginine/pharmacology | - |
dc.subject.MESH | Oxidation-Reduction | - |
dc.subject.MESH | Penicillamine/analogs & derivatives* | - |
dc.subject.MESH | Penicillamine/pharmacology | - |
dc.subject.MESH | Structure-Activity Relationship | - |
dc.subject.MESH | Sulfhydryl Compounds/metabolism* | - |
dc.subject.MESH | Transfection | - |
dc.subject.MESH | Tumor Cells, Cultured | - |
dc.title | Inhibition of apoptosis signal-regulating kinase 1 by nitric oxide through a thiol redox mechanism | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Microbiology (미생물학) | - |
dc.contributor.googleauthor | Hee-Sae Park | - |
dc.contributor.googleauthor | Je-Wook Yu | - |
dc.contributor.googleauthor | Eui-Ju Choi | - |
dc.contributor.googleauthor | Kanghyun Ryoo | - |
dc.contributor.googleauthor | Sung-Ho Huh | - |
dc.contributor.googleauthor | Mi-Sung Kim | - |
dc.contributor.googleauthor | Jun-Ho Cho | - |
dc.identifier.doi | 10.1074/jbc.M304183200 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A02508 | - |
dc.relation.journalcode | J01258 | - |
dc.identifier.eissn | 1083-351X | - |
dc.identifier.pmid | 14668338 | - |
dc.contributor.alternativeName | Yu, Je Wook | - |
dc.contributor.affiliatedAuthor | Yu, Je Wook | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 279 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 7584 | - |
dc.citation.endPage | 7590 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.279(9) : 7584-7590, 2004 | - |
dc.identifier.rimsid | 36850 | - |
dc.type.rims | ART | - |
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