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The involvement of calpain in homocysteine‐induced apoptosis in SH‐SY5Y cells
Author(s) -
Jang Yumi,
Kim HyunJung,
Kwon Young Hye
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.877.3
Subject(s) - calpain , sh sy5y , apoptosis , homocysteine , programmed cell death , mitochondrion , microbiology and biotechnology , intracellular , caspase , chemistry , neurotoxicity , biology , cell culture , biochemistry , neuroblastoma , toxicity , enzyme , genetics , organic chemistry
Apoptotic neuronal cell death is the important feature of aging and neurodegenerative disease, but its mechanisms are not clear. In the previous study, we reported that caspase‐9 activity was significantly increased when cells were treated with homocysteine along with activation of caspase‐4. The expression of Bax was also increased by homocysteine, suggesting homocysteine may cause activation of mitochondrial apoptotic pathway. The transfer of Ca 2+ from the ER to the mitochondria is required for initiation of programmed cell death by some apoptotic signals. Therefore, in the present study, we investigated the roles of Ca 2+ and calpain in homocysteine‐mediated apoptotic pathway in SH‐SY5Y human neuroblastoma cells. Homocysteine significantly increased intracellular Ca 2+ level. Neurotoxicity induced by homocysteine was significantly attenuated when cells were co‐treated with calpain inhibitor, PD150606. The increase in caspase‐3 activity by ER stress inducers was significantly decreased when cells were treated with calpain inhibitor. Therefore, our data indicate that homocysteine induces programmed cell death through crosstalk between mitochondria and ER and that calpain may play an important physiological role in the pathogenesis of neurodegenerative disorders. This study was supported by a grant from Korea Research Foundation.