Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9426584 | Neuroscience | 2005 | 14 Pages |
Abstract
These findings demonstrate increased immunoreactivity against phosphorylated adducin at the myristoylated alanine-rich C kinase substrate domain in a murine model of amyotrophic lateral sclerosis. As adducin is a substrate for protein kinase C at the myristoylated alanine-rich C kinase substrate domain, the increased phospho-adducin immunoreactivity is likely a consequence of protein kinase C activation in neurons and astrocytes of the spinal cord and evidence for aberrant phosphorylation events in mutant human superoxide dismutase mice that may affect neuron survival.
Keywords
PKCNMDAmotoneuronTPLSMdiaminobenzidine tetrahydrochloridePFAN-methyl-d-aspartatePBSTMAP-2ROINGSGFAPMARCKSDABPBSAdducinmyristoylated alanine-rich C kinase substrateamyotrophic lateral sclerosisALSmotor neuron diseaseTyrSODSer/Thrnormal goat serumSerine/threonineSuperoxide dismutaseSpinal cordPhosphate-buffered salineregion of interestparaformaldehydeGlial fibrillary acidic proteinmicrotubule-associated protein-2Protein kinase C
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Authors
X. Shan, J.H. Hu, F.S. Cayabyab, C. Krieger,