Biochemical and Biophysical Research Communications
Regular ArticleThe Levels of cdk5 and p35 Proteins and Tau Phosphorylation Are Reduced during Neuronal Apoptosis
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Cited by (31)
Free D-aspartate triggers NMDA receptor-dependent cell death in primary cortical neurons and perturbs JNK activation, Tau phosphorylation, and protein SUMOylation in the cerebral cortex of mice lacking D-aspartate oxidase activity
2019, Experimental NeurologyCitation Excerpt :Further studies will be required to investigate the involvement of calcineurin and of other phosphatases such as PP2A and PP1 in regulating Tau phosphorylation in Ddo−/− mouse brain. Tau dephosphorylation has been reported to be associated with neuronal apoptosis (Amadoro et al., 2004; Canu et al., 1998; Kerokoski et al., 2001; Liu et al., 2010; Mills et al., 1998; Pristera et al., 2013; Rametti et al., 2004), oxidative stress (Ko et al., 1997) and glutamate-induced cell death (Lorio et al., 2001). In this latter case, Tau is also cleaved to a fragment (Lorio et al., 2001) like that seen in 100 μM D-Asp-treated primary cortical neurons.
Cdk5 protein inhibition and Aβ42 increase BACE1 protein level in primary neurons by a post-transcriptional mechanism: Implications of CDK5 as a therapeutic target for Alzheimer disease
2012, Journal of Biological ChemistryCitation Excerpt :The decrease in Cdk5 protein was unexpected. It has been shown that various apoptotic agents decrease Cdk5 and p35 levels (57), and we observed caspase 3 cleavage, suggesting that Cdk5 inhibition reduces Cdk5 levels through a caspase 3/apoptosis-dependent mechanism. Because our results with CP681301 and roscovitine treatment allowed us to exclude our first hypothesis that inhibition of Cdk5 activity would attenuate the Aβ42-induced BACE1 increase, we tested the possibility that inhibition of caspase 3 could block the BACE1 elevation.
Post-translational modifications of tau protein: Implications for Alzheimer's disease
2011, Neurochemistry InternationalCitation Excerpt :A role of CDK5 in tau phosphorylation and NFT formation has been clearly established in transgenic mice (Cruz et al., 2003; Noble et al., 2003). Although CDK5 regulates APP (amyloid precursor protein) processing and tau hyperphosphorylation, its involvement in AD remains controversial (Iqbal et al., 2009; Kerokoski et al., 2001; Lopes et al., 2010; Van den Haute et al., 2001). MAPKs also phosphorylate tau (Feijoo et al., 2005; Sergeant et al., 2008) and are found in NFTs of AD brains (Zhu et al., 2000).
Suppression of calpain-dependent cleavage of the CDK5 activator p35 to p25 by site-specific phosphorylation
2007, Journal of Biological ChemistryCitation Excerpt :On the other hand, calpain has also been thought to be a signaling protease, which generates limited proteolysed fragments that possess altered properties in comparison to their parent molecules (18). Cdk5-p25 is different from Cdk5-p35 with regard to solubility, cellular localization, stability, and kinase activity (6–9, 38). Thus, it is important to understand how proteolytic cleavage of p35 to p25 is regulated.
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To whom correspondence should be addressed at University of Kuopio, Dept. of Neuroscience and Neurology, P.O. Box 1627, 70211 Kuopio, Finland. Fax: +358-17-162048. E-mail: [email protected].