| pubmed-article:19941067 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19941067 | lifeskim:mentions | umls-concept:C2754100 | lld:lifeskim |
| pubmed-article:19941067 | lifeskim:mentions | umls-concept:C1412055 | lld:lifeskim |
| pubmed-article:19941067 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19941067 | pubmed:dateCreated | 2010-3-10 | lld:pubmed |
| pubmed-article:19941067 | pubmed:abstractText | Apoptosis-associated tyrosine kinase (AATYK) is up-regulated by phosphorylation in cultured cerebellar granule neurons (CGN) undergoing apoptosis upon switch to low KCl-containing medium. However, the underlying signaling pathways remain to be fully characterized. When CGN at culture day 7 were switched from 25 mM KCl (K25) to 5 mM (K5) medium, AATYK band migration on SDS-PAGE shifted to a more slowly migrating position expected for the hyperphosphorylated protein. The apoptosis-inducing agent C(2)-ceramide also caused a mobility shift of the AATYK protein. Exposing CGN (K25) to L-type voltage-dependent Ca(2+) channel antagonists shifted the AATYK band to the K5-induced position, while the Ca(2+) channel activator FPL-64176 had the contrary effect. FK-506, a calcineurin inhibitor caused AATYK hyperphosphorylation under high KCl conditions. CGN death in K5 medium is linked to inhibition of the PI 3-kinase/Akt survival pathway and concomitant activation of the pro-apoptotic downstream target glycogen synthase kinase-3 (GSK-3). GSK-3 inhibitors blocked the K5-induced mobility shift of AATYK. Moreover, CGN cultured from AATYK-deficient mice remained sensitive to death in K5 medium. Thus, AATYK activation may not be a physiologically relevant principal regulatory target of the GSK-3 death pathway in KCl-deprived CGN. | lld:pubmed |
| pubmed-article:19941067 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19941067 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19941067 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19941067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19941067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19941067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19941067 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19941067 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19941067 | pubmed:issn | 1573-6903 | lld:pubmed |
| pubmed-article:19941067 | pubmed:author | pubmed-author:SkaperStephen... | lld:pubmed |
| pubmed-article:19941067 | pubmed:author | pubmed-author:HughesJane... | lld:pubmed |
| pubmed-article:19941067 | pubmed:author | pubmed-author:FacciLauraL | lld:pubmed |
| pubmed-article:19941067 | pubmed:author | pubmed-author:RichardsonJil... | lld:pubmed |
| pubmed-article:19941067 | pubmed:author | pubmed-author:WardDaniel... | lld:pubmed |
| pubmed-article:19941067 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19941067 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:19941067 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19941067 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19941067 | pubmed:pagination | 588-97 | lld:pubmed |
| pubmed-article:19941067 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:meshHeading | pubmed-meshheading:19941067... | lld:pubmed |
| pubmed-article:19941067 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19941067 | pubmed:articleTitle | Apoptosis-associated tyrosine kinase and neuronal cell death. | lld:pubmed |
| pubmed-article:19941067 | pubmed:affiliation | Neurosciences Centre of Excellence for Drug Discovery, GlaxoSmithKline Research and Development Limited, New Frontiers Science Park, Harlow, UK. | lld:pubmed |
| pubmed-article:19941067 | pubmed:publicationType | Journal Article | lld:pubmed |
