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Title 

S100A6 (calcyclin) enhances the sensitivity to apoptosis via the upregulation of caspase-3 activity in Hep3B cells

Authors 

J H JooS Y YoonJ H KimS G PaikSung Ran MinJ S LimIn Seong ChoeIn Pyo ChoiJae Wha Kim

Publisher 

Wiley-Blackwell

Issue Date 

2008

Citation 

Journal of Cellular Biochemistry, vol. 103, no. 4, pp. 1183-1197

Keywords 

A23187apoptosiscaspase-3EF-handHep3BS100A6

Abstract 

S100A6 (calcyclin) is a small calcium-binding protein which has been implicated in several cellular processes such as cell cycle progression, cytoskeleton rearrangement, and exocytosis. Also the upregulation of S100A6 has been reported in a variety of tumors and linked to metastasis. However, exact intracellular roles of S100A6 related with apoptosis have not been clarified yet. Here we demonstrated that the upregulation of S100A6 enhances the cell death rate compared to the control under the apoptotic conditions. In exogenously S100A6 induced Hep3B cells, cell viability was significantly decreased compared with mock and S100A6-knockdown cells under calcium ionophore A23187 treatment. The exogenously introduced S100A6 significantly affected the caspase-3-like activity in programmed cell death through the enhanced caspase-3 expression, which was verified by promoter assay in wild or mutant S100A6-transfected Hep3B cells. Next, the promoter activity of caspase-3 was increased by 2.5-folds in wild-type S100A6-transfected cells compared to mutant 2 (E67K, mutant of EF-hand motif) or control. Our results suggest that S100A6 might be involved in the processing of apoptosis by modulating the transcriptional regulation of caspase-3.

ISSN 

0730-2312

Link 

http://dx.doi.org/10.1002/jcb.21496

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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