| pubmed-article:9648865 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9648865 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:9648865 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:9648865 | lifeskim:mentions | umls-concept:C0242184 | lld:lifeskim |
| pubmed-article:9648865 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9648865 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:9648865 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9648865 | pubmed:dateCreated | 1998-7-9 | lld:pubmed |
| pubmed-article:9648865 | pubmed:abstractText | Caspase activation has been shown to be a critical step in several models of neuronal apoptosis such as staurosporine treatment of human neuroblastoma SH-SY5Y cells and potassium deprivation of rat cerebellar granule neurons. One common event is the appearance of caspase-mediated 120-kDa nonerythroid alpha-spectrin breakdown product (SBDP120). Second, inhibitors of the caspase family are effective blockers of such neuronal death. In this study, we report the appearance of caspase-mediated SBDP120 in excitotoxin-challenged fetal rat cerebrocortical neurons [N-methyl-D-aspartate (NMDA), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid, and kainate] and rat cerebellar granule neurons (NMDA and kainate). A general caspase inhibitor, carbobenzoxy-Asp-CH2OC(O)-2,6-dichlorobenzene (Z-D-DCB), blocked the formation of SBDP120 under these conditions and attenuated the observed NMDA-induced lactate dehydrogenase (LDH) release in both cell types. Furthermore, hydrolytic activity toward a caspase-3-preferred synthetic peptide substrate, acetyl-DEVD-7-amido-4-methylcoumarin, was significantly elevated in NMDA-treated granule neurons. Lastly, oxygen-glucose deprivation (OGD)-challenged cerebrocortical cultures also showed the appearance of SBDP120. Again, Z-D-DCB blocked the SBDP120 formation as well as attenuated the LDH release from the OGD-challenged neurons. Taken together, the presence of caspase-specific SBDP120 and the neuroprotective effects of Z-D-DCB strongly suggest that caspase activation contributes at least in part to excitotoxin- and OGD-induced neuronal death. | lld:pubmed |
| pubmed-article:9648865 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9648865 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9648865 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9648865 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9648865 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:9648865 | pubmed:author | pubmed-author:NathRR | lld:pubmed |
| pubmed-article:9648865 | pubmed:author | pubmed-author:WannK TKT | lld:pubmed |
| pubmed-article:9648865 | pubmed:author | pubmed-author:McGinnisK MKM | lld:pubmed |
| pubmed-article:9648865 | pubmed:author | pubmed-author:ProbertAAJr | lld:pubmed |
| pubmed-article:9648865 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9648865 | pubmed:volume | 71 | lld:pubmed |
| pubmed-article:9648865 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9648865 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9648865 | pubmed:pagination | 186-95 | lld:pubmed |
| pubmed-article:9648865 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9648865 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9648865 | pubmed:articleTitle | Evidence for activation of caspase-3-like protease in excitotoxin- and hypoxia/hypoglycemia-injured neurons. | lld:pubmed |
| pubmed-article:9648865 | pubmed:affiliation | Department of Neuroscience Therapeutics, Parke-Davis Pharmaceutical Research, Warner-Lambert Company, Ann Arbor, Michigan 48105, USA. | lld:pubmed |
| pubmed-article:9648865 | pubmed:publicationType | Journal Article | lld:pubmed |
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