pubmed-article:10579584 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C1120843 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C1708528 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C0332206 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:10579584 | lifeskim:mentions | umls-concept:C0070750 | lld:lifeskim |
pubmed-article:10579584 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:10579584 | pubmed:dateCreated | 1999-12-17 | lld:pubmed |
pubmed-article:10579584 | pubmed:abstractText | Consistent with previous studies on cell lines and non-neuronal cells, specific inhibitors of protein kinase C induced mouse primary cultured neocortical neurons to undergo apoptosis. To examine the complementary hypothesis that activating protein kinase C would attenuate neuronal apoptosis, the cultures were exposed for 1 h to phorbol-12-myristate-13-acetate, which activated protein kinase C as evidenced by downstream enhancement of the mitogen-activated protein kinase pathway. Exposure to phorbol-12-myristate-13-acetate, or another active phorbol ester, phorbol-12,13-didecanoate, but not to the inactive ester, 4alpha-phorbol-12,13-didecanoate, markedly attenuated neuronal apoptosis induced by serum deprivation. Phorbol-12-myristate-13-acetate also attenuated neuronal apoptosis induced by exposure to beta-amyloid peptide 1-42, or oxygen-glucose deprivation in the presence of glutamate receptor antagonists. The neuroprotective effects of phorbol-12-myristate-13-acetate were blocked by brief (non-toxic) concurrent exposure to the specific protein kinase C inhibitors, but not by a specific mitogen-activated protein kinase 1 inhibitor. Phorbol-12-myristate-13-acetate blocked the induction of p38 mitogen-activated protein kinase activity and specific inhibition of this kinase by SB 203580 attenuated serum deprivation-induced apoptosis. c-Jun N-terminal kinase 1 activity was high at rest and not modified by phorbol-12-myristate-13-acetate treatment. These data strengthen the idea that protein kinase C is a key modulator of several forms of central neuronal apoptosis, in part acting through inhibition of p38 mitogen-activated protein kinase regulated pathways. | lld:pubmed |
pubmed-article:10579584 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10579584 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10579584 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10579584 | pubmed:issn | 0306-4522 | lld:pubmed |
pubmed-article:10579584 | pubmed:author | pubmed-author:BehrensM MMM | lld:pubmed |
pubmed-article:10579584 | pubmed:author | pubmed-author:CohnN HNH | lld:pubmed |
pubmed-article:10579584 | pubmed:author | pubmed-author:StrasserUU | lld:pubmed |
pubmed-article:10579584 | pubmed:author | pubmed-author:KohJ YJY | lld:pubmed |
pubmed-article:10579584 | pubmed:author | pubmed-author:GwagB JBJ | lld:pubmed |
pubmed-article:10579584 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10579584 | pubmed:volume | 94 | lld:pubmed |
pubmed-article:10579584 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10579584 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10579584 | pubmed:pagination | 917-27 | lld:pubmed |
pubmed-article:10579584 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:10579584 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10579584 | pubmed:articleTitle | Prevention of neuronal apoptosis by phorbol ester-induced activation of protein kinase C: blockade of p38 mitogen-activated protein kinase. | lld:pubmed |
pubmed-article:10579584 | pubmed:affiliation | Department of Neurology and Center for the Study of the Nervous System Injury, Washington University School of Medicine, St Louis, MO 63110, USA. behrensm@neuro.wustl.edu | lld:pubmed |
pubmed-article:10579584 | pubmed:publicationType | Journal Article | lld:pubmed |
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