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http://purl.uniprot.org/citations/26227811http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26227811http://www.w3.org/2000/01/rdf-schema#comment"

Background

Tau hyperphosphorylation plays a critical role in neurodegenerative diseases [EMBO Mol Med. 6:1142-60, 2014; Annu Rev Neurosci. 24:1121-59, 2001]. Recent evidence has shown that Akt is down-regulated in AD [J Pathol. 225:54-62, 2011]. However, it remained unknown which pathological process, e.g. tau pathology or neuron death, Akt may contribute to. In this study, Cre-loxP technique was employed to generate a viable Akt three isoforms conditional knockout (Akt cTKO) mouse in which total Akt levels were dramatically reduced in the adult brain.

Results

Significantly increased levels of tau phosphorylated (p-tau) at various sites were observed in Akt cTKO mice as compared to age-matched littermate controls. Increased levels for phosphorylated GSK3α and phosphorylated PKA substrates were detected in Akt cTKO brains. In contrast, no significant changes on p-tau levels were found in Akt1(-/-), Akt2(-/-) or Akt3(-/-) mice.

Conclusions

Akt may regulate tau phosphorylation in the adult brain by affecting activities for PKA and GSK3α."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.org/dc/terms/identifier"doi:10.1186/s13024-015-0030-y"xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Chen G."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Lu S."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Zhu X."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Wang L."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Yang Z."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Xu C."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Xu Y."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Cheng S."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Hou J."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Peng Y."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Yin Z."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Zou X."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/author"Yu T."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/name"Mol Neurodegener"xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/pages"33"xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/title"Conditional inactivation of Akt three isoforms causes tau hyperphosphorylation in the brain."xsd:string
http://purl.uniprot.org/citations/26227811http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/26227811http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26227811
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http://purl.uniprot.org/uniprot/#_D3Z783-mappedCitation-26227811http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26227811
http://purl.uniprot.org/uniprot/#_A0A0A0MQC7-mappedCitation-26227811http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26227811
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