Transduced HSP27 protein protects neuronal cell death by enhancing FALS-associated SOD1 mutant activity.
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.
An
Jae Jin
JJ
Department of Biomedical Science and Research Institute for Bioscience and Biotechnology, Hallym University, Chunchon 200-702, Korea.
Lee
Yeom Pyo
YP
Kim
Dae Won
DW
Sohn
Eun Joung
EJ
Jeong
Hoon Jae
HJ
Kang
Hye Won
HW
Shin
Min Jae
MJ
Kim
Mi Jin
MJ
Ahn
Eun Hee
EH
Jang
Sang Ho
SH
Kang
Jung Hoon
JH
Kang
Tae-Cheon
TC
Won
Moo Ho
MH
Kwon
Oh-Shin
OS
Cho
Sung-Woo
SW
Lee
Kil Soo
KS
Park
Jinseu
J
Eum
Won Sik
WS
Choi
Soo Young
SY