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KMID : 0624620090420030136
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BMB Reports
2009 Volume.42 No. 3 p.136 ~ p.141
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Transduced HSP27 protein protects neuronal cell death by enhancing FALS-associated SOD1 mutant activity
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An Jae-Jin
Lee Yeom-Pyo
Kim Dae-Won
Sohn Eun-Joung
Jeong Hoon-Jae
Kang Jung-Hoon
Kwon Oh-Shin
Lee Kil-Soo
Park Jin-Seu
Eum Won-Sik
Kang Hye-Won
Shin Min-Jae
Kim Mi-Jin
Ahn Eun-Hee
Jang Sang-Ho
Kang Tae-Cheon
Won Moo-Ho
Cho Sung-Woo
Choi Soo-Young
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Abstract
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Familial Amyotrophic lateral sclerosis (FALS) is a progressive neurodegenetative disorder induced by mutations of the SOD1 gene. Heat shock protein 27 (HSP27) is well-defined as a stress-inducible protein, however the its role in ALS protection has not yet been established. To investigate the role HSP27 may have in SOD1 mutant-mediated apoptosis, human SOD1 or HSP27 genes were fused with a PEP-1 peptide in a bacterial expression vector to produce a genetic in-frame fusion protein, which was then transduced into cells. We found the purified PEP-1-HSP27 fusion proteins can be transduced efficiently into neuronal cells and protect against cell death by enhancing mutant SOD1 activity. Moreover, transduced PEP-1-HSP27 efficiently prevents protein aggregation produced by oxidative stress. These results suggest that transduced HSP27 fusion protein may be explored as a potential therapeutic agent for FALS patients
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KEYWORD
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Amyotrophic lateral sclerosis (ALS), Cu, Zn-superoxide dismutase (SOD1), Heat shock protein 27 (HSP27), PEP-1 peptide, Protein transduction
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