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Beta-Catenin and Leukemic Cell Apoptosis
Hwang,Sang Gu,Trepel,Jane B.,Lee,Hyung Chul,Moon,Ja Young 한국생명과학회 2000 한국생명과학회 학술발표회 Vol.27 No.-
Beta-catenin, which plays a critical role in both the cytoskeleton and in transcriptional regulation in various adherent cell types, undergoes degradation during adherent cell apoptosis. Although beta-catenin has been reported to be present in Jurkat T-acute lymphoblastic leukemia cells, the role of beta-catenin and its regulation in hematologic malignancies have not been examined. The data presented here demonstrate that treatment of the T cell leukemia Jurkat with the apoptosis inducers anti-Fas, TRAIL, staurosporin, and etoposide induced proteolytic cleavage of beta-catenin, as did TRAIL and staurosporin in U937 myeloblastic leukemia cells. In Jurkat cells, beta-catenin was cleaved at both the N- and C-terminus after anti-Fas. We observed strongly enhanced association of truncated beat-catenin with alpha-catenin and the actin cytoskeleton, in contrast to apoptotic adherent cells, in which beta-catenin association with alpha-catenin and actin is down-regulated during apoptosis. In Jurkat cells the interaction of beta-catenin with adenomatous polyposis coli protein and tubulin was down-regulated in response to Fas, further demonstrating a dramatic rearrangement of the T cell cytoskeleton. Down-regulation of beta-catenin-associated transcription was also an early event in response to anti-Fas. The data demonstrate that the organization of the cytoskeleton and its reorganization during apoptosis markedly differ in Jurkat cells and previously studied adherent cells. Furthermore, the data suggest that beta-catenin, which is not expressed in normal mature T cells, is integrally involved in organization of the Jurkat cytoskeleton, and that beta-catenin may play a role in promoting Jurkat survival.