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KMID : 0613820070170081129
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Journal of Life Science
2007 Volume.17 No. 8 p.1129 ~ p.1134
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Bombyx mori Protein Disulfide Isomerase (bPDI) Protects Sf9 Cells from Endoplasmic Reticulum (ER) Stress
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Goo Tae-Won
Yun Eun-Young
Kim Seong-Wan
Choi Kwang-Ho
Kang Seok-Woo
Kwon Ki-Sang
Kwon O-Yu
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Abstract
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In the previous our study, a cDNA that encodes protein disulfide isomerase from Bombyx mori (bPDI) was isolated and characterized. bPDI has an open reading frame of 494 amino acids contained two PDI-typical thioredoxin active site of WCGHCK and ER (endoplasmic reticulum) retention signal of the KDEL motif at its C-terminal. Recent studies have demonstrated that misfolded proteins are accumulated in many diseases including Alzheimer’s, goiter, emphysema, and prion infections. bPDI was over-expressed or knock-downed in Sf9 cells to study the relationship between bPDI expression and protections against protein misfolding. bPDI gene was cloned in insect expression vector pIZT/V5-His for over-expression and bPDI double-stranded RNA (dsRNA) was generated for knock-down. Over-expression of bPDI significantly improved survival rate, but bPDI dsRNA transfection significantly reduced survival rate after 48 hours exposure. In mock-transfected or wild-type cells had no significant effect. The results support the view that bPDI is one of the important intracellular components for cell protect mechanism, especially, against ER stress such as protein misfolding.
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KEYWORD
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Bombyx mori, protein disulfide isomerase, endoplamic reticulum, misfolding
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