S-allyl- l-cysteine selectively protects cultured rat hippocampal neurons from amyloid β-protein- and tunicamycin-induced neuronal death

S-allyl- l-cysteine (SAC), one of the organosulfur compounds found in aged garlic extract, has been shown to possess various biological effects including neurotrophic activity. In our previous experiments, we found that SAC could protect against amyloid β-protein (Aβ)- and tunicamycin-induced cell d...

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Bibliographic Details
Published in:	Neuroscience Vol. 122; no. 4; pp. 885 - 895
Main Authors:	Kosuge, Y, Koen, Y, Ishige, K, Minami, K, Urasawa, H, Saito, H, Ito, Y
Format:	Journal Article
Language:	English
Published:	Oxford Elsevier Ltd 2003 Elsevier
Subjects:	4-hydroxynonenal Amyloid beta-Peptides - toxicity Animals Biological and medical sciences caspase-12 Cell Death - drug effects Cell Death - physiology Cell Survival - drug effects Cells, Cultured Cysteine - analogs & derivatives Cysteine - pharmacology Dose-Response Relationship, Drug ER stress Hippocampus - drug effects Hippocampus - physiology Medical sciences neuronal death Neurons - drug effects Neurons - physiology Neuropharmacology Neuroprotective agent Neuroprotective Agents - pharmacology organosulfur compound Pharmacology. Drug treatments Rats Rats, Wistar Tunicamycin - toxicity HRP ALS caspase-12 organosulfur compound MTT Aβ mBBr BME GSH AGE PBS AD SDS IN DCF ER stress ER 4-hydroxynonenal ECL SAC TEAC neuronal death ROS PI HNE Rat Enzyme Rodentia Central nervous system Caspase Extract Neuroprotective agent In vitro Encephalon Peptidases Vertebrata Mammalia Cell death β Amyloid protein Animal Plant origin Hydrolases Garlic Hippocampus
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Summary:	S-allyl- l-cysteine (SAC), one of the organosulfur compounds found in aged garlic extract, has been shown to possess various biological effects including neurotrophic activity. In our previous experiments, we found that SAC could protect against amyloid β-protein (Aβ)- and tunicamycin-induced cell death in differentiated PC12 cells. In the study described here, we characterized the neuronal death induced by Aβ, 4-hydroxynonenal (HNE), tunicamycin, and trophic factor deprivation, and investigated whether and how SAC could prevent this in cultured rat hippocampal neurons. Treatment with SAC protected these cells against Aβ- and tunicamycin-induced neuronal death, which is mediated predominantly through caspase-12-dependent pathway in a concentration-dependent manner. In contrast, it afforded no protection against HNE- and trophic factor-deprivation-induced cell death, which has been shown to be mediated by caspase-3-dependent pathway. SAC also attenuated the Aβ-induced increase of intracellular reactive oxygen species in hippocampal neurons. SAC had no effect on Aβ-induced cell death in cultured cerebellar granule neurons, which was prevented by a caspase-3 inhibitor. These results suggest that SAC could protect against the neuronal cell death that is triggered by ER dysfunction in the hippocampus, and that it has no effect on neuronal cell death that is dependent upon the caspase-3 mediated pathway.
ISSN:	0306-4522 1873-7544
DOI:	10.1016/j.neuroscience.2003.08.026