Tau and GSK3beta dephosphorylations are required for regulating Pin1 phosphorylation
| Autor: | Jae H. Oh, Seok H. Lee, Seung Wan Jee, Dae Y. Hwang, Sun B. Shim, Su H. Lee, Jung S. Cho, Yhun Yhong Sheen, Hwa J. Lim, Yong K. Kim, Min Y. Kim, Sae H. Min |
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| Rok vydání: | 2005 |
| Předmět: |
endocrine system
Enolase tau Proteins Transfection Biochemistry Fusion gene Dephosphorylation Animals Genetically Modified Cellular and Molecular Neuroscience Amyloid beta-Protein Precursor Glycogen Synthase Kinase 3 Animals splice Gene DNA Primers Glycogen Synthase Kinase 3 beta Base Sequence Chemistry General Medicine Peptidylprolyl Isomerase Molecular biology Rats NIMA-Interacting Peptidylprolyl Isomerase nervous system PIN1 Phosphorylation |
| Zdroj: | Neurochemical research. 30(8) |
| ISSN: | 0364-3190 |
| Popis: | Pin1 binds mitotically phosphorylated Thr231-Pro232 and Thr212-Pro213 sites on tau, and a Pin1 deficiency in mice leads to tau hyperphosphorylation. The aim of this study was to determine if the dephosphorylation or inhibition of tau and GSK3beta phosphorylation induces the Pin1 phosphorylation. To test this, human SK-N-MC cells were stably transfected with a fusion gene containing neuron-specific enolase (NSE)-controlled APPsw gene(NSE/APPsw), to induce Abeta-42. The stable transfectants were then transiently transfected with NSE/Splice, lacking human tau (NSE/Splice), or NSE/hTau, containing human tau, into the cells. The NSE/Splice- and NSE/hTau-cells were then treated with lithium. We concluded that (i) there was more C99-beta APP accumulation than C83-betaAPP in APPsw-tansfectant and thereby promoted Abeta-42 production in transfectants. (ii) the inhibition of tau and GSK3beta phosphorylations correlated with increase in Pin1 activation in NSE/hTau- cells. Thus, these observations suggest that Pin1 might have an inhibitive role in phosphorylating tau and GSK3beta for protecting against Alzheimer's disease. |
| Databáze: | OpenAIRE |
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