Inhibition by R(+) or S(–) pramipexole of caspase activation and cell death induced by methylpyridinium ion or beta amyloid peptide in SH‐SY5Y neuroblastoma
Identifieur interne : 001881 ( Main/Exploration ); précédent : 001880; suivant : 001882Inhibition by R(+) or S(–) pramipexole of caspase activation and cell death induced by methylpyridinium ion or beta amyloid peptide in SH‐SY5Y neuroblastoma
Auteurs : Nicole A. Abramova [États-Unis] ; David S. Cassarino [États-Unis] ; Shaharyar M. Khan [États-Unis] ; Terry W. Painter [États-Unis] ; James P. Bennett Jr. [États-Unis]Source :
- Journal of Neuroscience Research [ 0360-4012 ] ; 2002-02-15.
English descriptors
Abstract
Cell models of neurodegenerative diseases (NDD) can involve expression of mutant nuclear genes associated with Mendelian forms of the diseases or effects of toxins believed to replicate essential disease features. Death produced by exposing neural cells to methylpyridinium ion (MPP+) or neurotoxic beta amyloid (BA) peptides is frequently used to study features of the sporadic, most prevalent forms of Parkinson's disease (PD) and Alzheimer's disease (AD), respectively. We examined in replicating SH‐SY5Y human neuroblastoma cells the release of cytochrome C into cytoplasm, activation of caspases 9 and 3, and loss of calcein retention as markers of the “mitochondrial” pathway of cell death. Exposure to 5 mM MPP+, which induces apoptotic cell death within 18–24 hr, released cytochrome C within 4 hr, activated caspases 9 and 3, and reduced calcein accumulation. BA 25–35 peptide produced more rapid and greater elevations of caspase 3 activity; no effects were observed with the nontoxic BA 35–25 reverse sequence. The dependence on mitochondrial transition pore (MTP) activity of MPP+‐induced caspase activations was demonstrated by preincubation with bongkreckic acid, which blocked elevations of caspases 9 and 3. Stereoisomers of pramipexole (PPX), a free radical scavenger and inhibitor of MTP opening, inhibited caspase activation (MPP+ and BA) and restored calcein accumulation (MPP+). Our results demonstrate that MPP+ and BA can induce cell death through MTP‐dependent activation of caspase cascades. PPX stereoisomers interfere with activation of these cell death pathways and may be useful clinically as neuroprotectants in PD and AD and related diseases. © 2002 Wiley‐Liss, Inc.
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DOI: 10.1002/jnr.10127
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Death produced by exposing neural cells to methylpyridinium ion (MPP+) or neurotoxic beta amyloid (BA) peptides is frequently used to study features of the sporadic, most prevalent forms of Parkinson's disease (PD) and Alzheimer's disease (AD), respectively. We examined in replicating SH‐SY5Y human neuroblastoma cells the release of cytochrome C into cytoplasm, activation of caspases 9 and 3, and loss of calcein retention as markers of the “mitochondrial” pathway of cell death. Exposure to 5 mM MPP+, which induces apoptotic cell death within 18–24 hr, released cytochrome C within 4 hr, activated caspases 9 and 3, and reduced calcein accumulation. BA 25–35 peptide produced more rapid and greater elevations of caspase 3 activity; no effects were observed with the nontoxic BA 35–25 reverse sequence. The dependence on mitochondrial transition pore (MTP) activity of MPP+‐induced caspase activations was demonstrated by preincubation with bongkreckic acid, which blocked elevations of caspases 9 and 3. Stereoisomers of pramipexole (PPX), a free radical scavenger and inhibitor of MTP opening, inhibited caspase activation (MPP+ and BA) and restored calcein accumulation (MPP+). Our results demonstrate that MPP+ and BA can induce cell death through MTP‐dependent activation of caspase cascades. PPX stereoisomers interfere with activation of these cell death pathways and may be useful clinically as neuroprotectants in PD and AD and related diseases. © 2002 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li><li>Virginie</li></region></list><tree><country name="États-Unis"><region name="Virginie"><name sortKey="Abramova, Nicole A" sort="Abramova, Nicole A" uniqKey="Abramova N" first="Nicole A." last="Abramova">Nicole A. Abramova</name></region><name sortKey="Bennett Jr, James P" sort="Bennett Jr, James P" uniqKey="Bennett Jr J" first="James P." last="Bennett Jr.">James P. Bennett Jr.</name><name sortKey="Cassarino, David S" sort="Cassarino, David S" uniqKey="Cassarino D" first="David S." last="Cassarino">David S. Cassarino</name><name sortKey="Khan, Shaharyar M" sort="Khan, Shaharyar M" uniqKey="Khan S" first="Shaharyar M." last="Khan">Shaharyar M. Khan</name><name sortKey="Painter, Terry W" sort="Painter, Terry W" uniqKey="Painter T" first="Terry W." last="Painter">Terry W. Painter</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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