| http://purl.uniprot.org/citations/15459207 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15459207 | http://www.w3.org/2000/01/rdf-schema#comment | "Extracellular signal-regulated kinase 1/2 (ERK1/2) is known to function in cell survival in response to various stresses; however, the mechanism of cell survival by ERK1/2 remains poorly elucidated in ischemic heart. Here we applied functional proteomics by two-dimensional electrophoresis to identify a cellular target of ERK1/2 in response to ischemic hypoxia. Approximately 1500 spots were detected by Coomassie Brilliant Blue staining of a sample from unstimulated cells. The staining intensities of at least 50 spots increased at 6-h reoxygenation after 2-h ischemic hypoxia. Of the 50 spots that increased, at least 4 spots were inhibited in the presence of PD98059, a MEK inhibitor. A protein with a molecular mass of 52 kDa that is strongly induced by ERK1/2 activation in response to ischemic hypoxia and reoxygenation was identified as alpha-enolase, a rate-limiting enzyme in the glycolytic pathway, by liquid chromatography-mass spectrometry and amino acid sequencing. The expressions of the alpha-enolase mRNA and protein are inhibited during reoxygenation after ischemic hypoxia in the cells containing a dominant negative mutant of MEK1 and treated with a MEK inhibitor, PD98059, leading to a decrease in ATP levels. alpha-Enolase expression is also observed in rat heart subjected to ischemia-reperfusion. The induction of alpha-enolase by ERK1/2 appears to be mediated by c-Myc. The introduction of the alpha-enolase protein into the cells restores ATP levels and prevents cell death during ischemic hypoxia and reoxygenation in these cells. These results show that alpha-enolase expression by ERK1/2 participates in the production of ATP during reoxygenation after ischemic hypoxia, and a decrease in ATP induces apoptotic cell death. Furthermore, alpha-enolase improves the contractility of cardiomyocytes impaired by ischemic hypoxia. Our results reveal that ERK1/2 plays a role in the contractility of cardiomyocytes and cell survival through alpha-enolase expression during ischemic hypoxia and reoxygenation."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m402299200"xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Matsuzaki M."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Kimura M."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Iwamatsu A."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Nakamura K."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Mizukami Y."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Kobayashi S."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Yoshida K."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Aki T."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Nao T."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/author | "Okusa T."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/pages | "50120-50131"xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/title | "ERK1/2 regulates intracellular ATP levels through alpha-enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation."xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15459207 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15459207 |
| http://purl.uniprot.org/citations/15459207 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15459207 |
| http://purl.uniprot.org/uniprot/P06733#attribution-0CE5CFDE50D694E83D9678B00537C4FD | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15459207 |
| http://purl.uniprot.org/uniprot/P06733#attribution-4560708EB4595A3792D6936AF972A7B4 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15459207 |
| http://purl.uniprot.org/uniprot/P04764#attribution-4560708EB4595A3792D6936AF972A7B4 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15459207 |
| http://purl.uniprot.org/uniprot/Q16665#attribution-4560708EB4595A3792D6936AF972A7B4 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15459207 |
| http://purl.uniprot.org/uniprot/Q01986#attribution-FA680A0BEAEA8A8E8D2B42A16F96E669 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15459207 |