Protein disulfide isomerase knockdown-induced cell death is cell-line-dependent and involves apoptosis in MCF-7 cells
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- Hashida Tomoyo
- Graduate School of Biomedical Sciences, Hiroshima University
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- Kotake Yaichiro
- Graduate School of Biomedical Sciences, Hiroshima University
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- Ohta Shigeru
- Graduate School of Biomedical Sciences, Hiroshima University
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Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes disulfide bond formation and assists protein folding, as well as being a structural subunit of microsomal triglyceride transfer protein (MTP) and prolyl 4-hydroxylase (P4HD), and an estrogen and thyroid hormone-binding protein. Previous reports indicate that some endocrine-disrupting chemicals (EDCs) bind to PDI and disturb its functions, and we executed PDI-knockdown to examine the effects of dysfunction of PDI. In this study, the effects of PDI-knockdown were compared among three cell lines: MCF-7, SH-SY5Y and HeLa. PDI-knockdown induced different levels of cytotoxicity among these cell lines. In MCF-7 cells, PDI-knockdown activated apoptotic signaling, causing cytochrome c release from mitochondria and activation of caspase-9, caspase-6, caspase-7 and poly[ADP-ribose]polymerase-1, and the cytotoxicity induced by PDI-knockdown was suppressed by a pan-caspase inhibitor, z-VAD-fmk. These data suggest that cell death induced by PDI-knockdown is caspase-dependent apoptosis in MCF-7 cells.
収録刊行物
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- Ｔｈｅ Ｊｏｕｒｎａｌ ｏｆ Ｔｏｘｉｃｏｌｏｇｉｃａｌ Ｓｃｉｅｎｃｅｓ
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Ｔｈｅ Ｊｏｕｒｎａｌ ｏｆ Ｔｏｘｉｃｏｌｏｇｉｃａｌ Ｓｃｉｅｎｃｅｓ 36 (1), 1-7, 2011
一般社団法人 日本毒性学会
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詳細情報 詳細情報について
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- CRID
- 1390282679878348800
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- NII論文ID
- 10027420192
- 20001046901
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- NII書誌ID
- AN00002808
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- DOI
- 10.2131/jts.36.1
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- ISSN
- 18803989
- 03881350
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- NDL書誌ID
- 10999449
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 使用不可