Cited 0 times in
Ca2+-mediated activation of c-Jun N-terminal kinase and nuclear factor kappa B by NMDA in cortical cell cultures.
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ko, HW | - |
dc.contributor.author | Park, KY | - |
dc.contributor.author | Kim, H | - |
dc.contributor.author | Han, PL | - |
dc.contributor.author | Kim, YU | - |
dc.contributor.author | Gwag, BJ | - |
dc.contributor.author | Choi, EJ | - |
dc.date.accessioned | 2011-08-22T05:56:14Z | - |
dc.date.available | 2011-08-22T05:56:14Z | - |
dc.date.issued | 1998 | - |
dc.identifier.issn | 0022-3042 | - |
dc.identifier.uri | http://repository.ajou.ac.kr/handle/201003/3885 | - |
dc.description.abstract | We examined the possibility that c-Jun N-terminal kinase (JNK) and nuclear factor kappaB (NF-kappaB) might be involved in intracellular signaling cascades that mediate NMDA-initiated neuronal events. Exposure of cortical neurons to 100 microM NMDA induced activation of JNK within 1 min. Activity of JNK was further increased over the next 5 min and then declined by 30 min. Similarly, ionomycin, a selective Ca2+ ionophore, induced activation of JNK. The NMDA-induced activation of JNK was abrogated in the absence of extracellular Ca2+, suggesting that Ca2+ entry is necessary and sufficient for the JNK activation. Immunohistochemistry with anti-NF-kappaB antibody demonstrated nuclear translocation of NF-kappaB within 5 min following NMDA treatment. NMDA treatment also enhanced the DNA binding activity of nuclear NF-kappaB in a Ca2+-dependent manner. Treatment with 3 mM aspirin blocked the NMDA-induced activation of JNK and NF-kappaB. Neuronal death following a brief exposure to 100 microM NMDA was Ca2+ dependent and attenuated by addition of aspirin or sodium salicylate. The present study suggests that Ca2+ influx is required for NMDA-induced activation of JNK and NF-kappaB as well as NMDA neurotoxicity. This study also implies that aspirin may exert its neuroprotective action against NMDA through blocking the NMDA-induced activation of NF-kappaB and JNK. | - |
dc.language.iso | en | - |
dc.subject.MESH | Animals | - |
dc.subject.MESH | Aspirin | - |
dc.subject.MESH | Calcium | - |
dc.subject.MESH | Calcium-Calmodulin-Dependent Protein Kinases | - |
dc.subject.MESH | Cells, Cultured | - |
dc.subject.MESH | Cerebral Cortex | - |
dc.subject.MESH | Enzyme Activation | - |
dc.subject.MESH | Fetus | - |
dc.subject.MESH | JNK Mitogen-Activated Protein Kinases | - |
dc.subject.MESH | Mice | - |
dc.subject.MESH | Mitogen-Activated Protein Kinases | - |
dc.subject.MESH | N-Methylaspartate | - |
dc.subject.MESH | NF-kappa B | - |
dc.title | Ca2+-mediated activation of c-Jun N-terminal kinase and nuclear factor kappa B by NMDA in cortical cell cultures. | - |
dc.type | Article | - |
dc.identifier.pmid | 9751169 | - |
dc.identifier.url | http://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0022-3042&date=1998&volume=71&issue=4&spage=1390 | - |
dc.contributor.affiliatedAuthor | 곽, 병주 | - |
dc.type.local | Journal Papers | - |
dc.citation.title | Journal of neurochemistry | - |
dc.citation.volume | 71 | - |
dc.citation.number | 4 | - |
dc.citation.date | 1998 | - |
dc.citation.startPage | 1390 | - |
dc.citation.endPage | 1395 | - |
dc.identifier.bibliographicCitation | Journal of neurochemistry, 71(4). : 1390-1395, 1998 | - |
dc.identifier.eissn | 1471-4159 | - |
dc.relation.journalid | J000223042 | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.