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S100A6 (calcyclin) enhances the sensitivity to apoptosis via the upregulation of caspase-3 activity in Hep3B cells
Journal of cellular biochemistry, 2008-03, Vol.103 (4), p.1183-1197
Joo, Joung Hyuck
Yoon, Sun Young
Kim, Joo Heon
Paik, Sang-Gi
Min, Sung Ran
Lim, Jong-Seok
Choe, In Seong
Choi, Inpyo
Kim, Jae Wha
2008
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Joo, Joung Hyuck
Yoon, Sun Young
Kim, Joo Heon
Paik, Sang-Gi
Min, Sung Ran
Lim, Jong-Seok
Choe, In Seong
Choi, Inpyo
Kim, Jae Wha
Titel
S100A6 (calcyclin) enhances the sensitivity to apoptosis via the upregulation of caspase-3 activity in Hep3B cells
Ist Teil von
Journal of cellular biochemistry, 2008-03, Vol.103 (4), p.1183-1197
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2008
Quelle
MEDLINE
Beschreibungen/Notizen
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. J. Cell. Biochem. 103: 1183–1197, 2008. © 2007 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0730-2312
eISSN: 1097-4644
DOI: 10.1002/jcb.21496
Titel-ID: cdi_proquest_miscellaneous_70326794
Format
–
Schlagworte
A23187
,
apoptosis
,
Apoptosis - physiology
,
Calcimycin - pharmacology
,
Calcium - metabolism
,
Caspase 3 - biosynthesis
,
caspase-3
,
Cell Cycle Proteins - genetics
,
Cell Cycle Proteins - physiology
,
Cell Line, Tumor
,
EF-hand
,
Enzyme Activation
,
Hep3B
,
Humans
,
Ionophores - pharmacology
,
Mutation
,
Promoter Regions, Genetic
,
S100 Calcium Binding Protein A6
,
S100 Proteins - genetics
,
S100 Proteins - physiology
,
S100A6
,
Up-Regulation
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