pubmed-article:7595536 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0007765 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0010837 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
pubmed-article:7595536 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:7595536 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:7595536 | pubmed:dateCreated | 1995-12-15 | lld:pubmed |
pubmed-article:7595536 | pubmed:abstractText | Cultured cerebellar granule neurons maintained in depolarizing concentrations of K+ (25 mM) and then switched to physiological concentrations of K+ (5 mM) undergo apoptosis. We now report that activation of specific G proteins robustly and bidirectionally affects apotosis of cultured rat cerebellar granule neurons. Stimulation of Gs with cholera toxin completely blocks apoptosis induced by nondepolarizing concentrations of K+, whereas stimulation of Go/Gi with the wasp venom peptide mastoparan induces apoptosis of cerebellar granule neurons even in high (depolarizing) concentrations of K+. Moreover, pretreatment of cerebellar granule neurons with cholera toxin attenuates neuronal death induced by mastoparan. By contrast, pertussis toxin, cell-permeable analogues of cyclic AMP, and activators of protein kinase A do not affect apoptosis of cultured cerebellar granule neurons. These data suggest that G proteins may function as key switches for controlling the programmed death of mammalian neurons, especially in the developing CNS. | lld:pubmed |
pubmed-article:7595536 | pubmed:language | eng | lld:pubmed |
pubmed-article:7595536 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7595536 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7595536 | pubmed:month | Dec | lld:pubmed |
pubmed-article:7595536 | pubmed:issn | 0022-3042 | lld:pubmed |
pubmed-article:7595536 | pubmed:author | pubmed-author:PaulS MSM | lld:pubmed |
pubmed-article:7595536 | pubmed:author | pubmed-author:LiuS QSQ | lld:pubmed |
pubmed-article:7595536 | pubmed:author | pubmed-author:IrwinR PRP | lld:pubmed |
pubmed-article:7595536 | pubmed:author | pubmed-author:YanG MGM | lld:pubmed |
pubmed-article:7595536 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7595536 | pubmed:volume | 65 | lld:pubmed |
pubmed-article:7595536 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7595536 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7595536 | pubmed:pagination | 2425-31 | lld:pubmed |
pubmed-article:7595536 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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pubmed-article:7595536 | pubmed:meshHeading | pubmed-meshheading:7595536-... | lld:pubmed |
pubmed-article:7595536 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7595536 | pubmed:articleTitle | Activation of G proteins bidirectionally affects apoptosis of cultured cerebellar granule neurons. | lld:pubmed |
pubmed-article:7595536 | pubmed:affiliation | Department of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, USA. | lld:pubmed |
pubmed-article:7595536 | pubmed:publicationType | Journal Article | lld:pubmed |
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