http://purl.uniprot.org/citations/12441106 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12441106 | http://www.w3.org/2000/01/rdf-schema#comment | "The role of c-Jun in apoptosis evoked by human amylin was investigated using human and rat insulinoma beta-cell lines. Two transient increases in the levels of c-jun mRNA were detected at 30 minutes and eight hours after treatment with human amylin. The level of c-Jun protein was also up-regulated in a time-dependent manner, reaching maximal levels after eight hours of exposure. However, no c-Jun induction was detected in cells treated with vehicle only or with rat amylin, indicating that the amyloidogenic feature of the human peptide may be important for c-Jun induction. We found that c-Jun was activated by phosphorylation specifically at Ser63 at four hours, but not at Ser73, after treatment with human amylin, preceding increased c-Jun protein. Furthermore, expression of an antisense c-jun (AS-c-jun), which suppressed protein levels of both c-Jun and phosphorylated-c-Jun, caused a marked reduction in apoptotic cell death, whereas the corresponding sense c-jun (S-c-jun) had no effect on changes of either c-Jun production or apoptosis. This indicated that increased expression and activation of c-Jun is required for human amylin-induced apoptosis. Immunocytochemical studies showed a significant increase in nuclear staining for c-Jun, phosphorylated-c-Jun (Ser63) and phosphorylated-JNK, suggesting that c-Jun may be activated through activation of JNK. In addition, electrophoretic mobility-shift assays showed that the increase in expression and phosphorylation of c-Jun was associated with increased AP-1 DNA binding activity. Supershift assays demonstrated that c-Jun, c-Fos and ATF-2 are part of the AP-1 complex, indicating that activated c-Jun is dimerized with c-Fos or ATF-2 for control of its target gene expression. Finally, we showed that human amylin triggers AP-1-mediated transcriptional activation. Our results suggest strongly that human amylin induces apoptosis through stimulation of expression and activation of c-Jun, and that co-expression and dimerization of c-Jun and c-fos or ATF-2 may be important for activation of the downstream apoptotic process."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0022-2836(02)01044-6"xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/author | "Zhang S."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/author | "Dragunow M."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/author | "Cooper G.J."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/author | "MacGibbon G."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/name | "J Mol Biol"xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/pages | "271-285"xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/title | "Increased expression and activation of c-Jun contributes to human amylin-induced apoptosis in pancreatic islet beta-cells."xsd:string |
http://purl.uniprot.org/citations/12441106 | http://purl.uniprot.org/core/volume | "324"xsd:string |
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