Induction of apoptosis by vitamin D-3 analogue EB1089 in NCI-H929 myeloma cells via activation of caspase 3 and p38 MAP kinase
- Authors
- Park, WH; Seol, JG; Kim, ES; Hyun, JM; Jung, CW; Lee, CC; Binderup, L; Koeffler, HP; Kim, BK; Lee, YY
- Issue Date
- Jun-2000
- Publisher
- BLACKWELL SCIENCE LTD
- Keywords
- vitamin D-3 analogue; myeloma; apoptosis; caspase; MAP kinase
- Citation
- BRITISH JOURNAL OF HAEMATOLOGY, v.109, no.3, pp 576 - 583
- Pages
- 8
- Journal Title
- BRITISH JOURNAL OF HAEMATOLOGY
- Volume
- 109
- Number
- 3
- Start Page
- 576
- End Page
- 583
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/47360
- DOI
- 10.1046/j.1365-2141.2000.02046.x
- ISSN
- 0007-1048
1365-2141
- Abstract
- EB1089, a novel 1,25-dihydroxyvitamin D-3 analogue, has been known to have potent antiproliferative properties in a variety of malignant cells both in vitro and in vivo. In the present study we analysed the effect of EB1089 on NCI-H929 human myeloma cells. EB1089 inhibited cell growth of NCI-H929 and efficiently induced the G(1) phase arrest of the cell cycle in a dose-dependent manner. We could also detect apoptosis in NCI-H929 cells exposed to EB1089 (1 x 10(-7) M for 72 h) using the sub-G(1) group of the cell cycle by FAGS and annexin V binding assays. Induction of apoptosis by EB1089 was associated with down-regulation of the Bcl-2 protein without change of the Bar protein. Regarding caspase activity, which plays a crucial role in apoptosis, EB1089-treated NCI-H929 cells revealed an increased activity of caspase 3 protease accompanied by degradation of the PARP protein in a dose- and time-dependent manner, In addition, EB1089 caused the down-regulation of p44 extracellular signal-related kinase (ERK) activity and up-regulation of the p38 kinase activity during apoptosis of NCI-H929 cells, These results suggest that EB1089 inhibits growth of NCI-H929 cells via G(1) cell cycle arrest as well as apoptosis by activating p38 kinase and suppressing ERK activity.
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