Truncated Tau with the Fyn‐binding domain and without the microtubule‐binding domain hinders the myelinating capacity of an oligodendrocyte cell line

Belkadi, Abdelmadjid; LoPresti, Patrizia

doi:10.1111/j.1471-4159.2008.05600.x

Cited by 31 publications

(34 citation statements)

References 49 publications

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“…Thus, overexpression of Tau fragments lacking the repeat domain, which stay in the cell body because they cannot be sorted into the axon, also leads to a local accumulation of Fyn , and presumably other SH3-domain proteins. A role for Tau -Fyn interactions has been postulated for oligodendrocytes where the complex is transported into cell processes in a MT-dependent manner and is required for myelination (Belkadi and LoPresti 2008;Klein et al 2002). In neurons, the Tau-Fyn complex becomes enriched in lipid rafts upon exposure to Ab (Williamson et al 2008).…”

Section: Fkbp52mentioning

confidence: 99%

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

Mandelkow

2012

Cold Spring Harbor Perspectives in Medicine

705

636

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Tau represents the subunit protein of one of the major hallmarks of Alzheimer disease (AD), the neurofibrillary tangles, and is therefore of major interest as an indicator of disease mechanisms. Many of the unusual properties of Tau can be explained by its nature as a natively unfolded protein. Examples are the large number of structural conformations and biochemical modifications ( phosphorylation, proteolysis, glycosylation, and others), the multitude of interaction partners (mainly microtubules, but also other cytoskeletal proteins, kinases, and phosphatases, motor proteins, chaperones, and membrane proteins). The pathological aggregation of Tau is counterintuitive, given its high solubility, but can be rationalized by short hydrophobic motifs forming b structures. The aggregation of Tau is toxic in cell and animal models, but can be reversed by suppressing expression or by aggregation inhibitors. This review summarizes some of the structural, biochemical, and cell biological properties of Tau and Tau fibers. Further aspects of Tau as a diagnostic marker and therapeutic target, its involvement in other Tau-based diseases, and its histopathology are covered by other chapters in this volume.

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Section: Fkbp52mentioning

confidence: 99%

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

Mandelkow

2012

Cold Spring Harbor Perspectives in Medicine

705

636

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“…Other very early (pre-fibrillar) disease-associated changes include lysosomal hypertrophy [84,85] as well as the colocalization of a variety of development-associated regulatory proteins, including GSK3β, CDK5, MARK kinases, CRMP2, and GAP43 [86][87][88][89][90]. Additional abnormalities associated with pre-fibrillar neurons include evidence for the reactivation of developmental programs normally associated with tau, especially those associated with axonal identity [91,92], and other aspects of axonogenesis [93][94][95][96]. Moreover, it emerged that the primary genetic and environmental risk factors for developing LOAD were (respectively) the ApoE4 allele [27], and severe or repeated head trauma [97][98][99].…”

Section: Translational Neurosciencementioning

confidence: 99%

Untangling the role of tau in Alzheimer’s disease: A unifying hypothesis

Bhatia

Hall

2013

Translational Neuroscience

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Recent investigations into the etiology and pathogenesis of Alzheimer's disease (AD) in the past few years have expanded to include previously unexplored and/or disconnected aspects of AD and related conditions at both the cellular and systemic levels of organization. These include how AD-associated abnormalities affect the cell cycle and neuronal differentiation state and how they recruit signal transduction, membrane trafficking and protein transcytosis mechanisms to produce a neurotoxic syndrome capable of spreading itself throughout the brain. The recent expansion of AD research into intercellular and new aspects of cellular degenerative mechanisms is causing a systemic re-evaluation of AD pathogenesis, including the roles played by well-studied elements, such as the generation of Aβ and tau protein aggregates. It is also changing our view of neurodegenerative diseases as a whole. Here we propose a conceptual framework to account for some of the emerging aspects of the role of tau in AD pathogenesis.

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“…11 During axonal regeneration, tau mRNA is widely expressed, but tau proteins are only present in those axons that regenerate the quickest. 10, 24 Although tau protein is not necessary for nerve regeneration, axons that show an embryonic pattern of MAP gene expression grow more dynamically. 10, 25 The present study exploited autologous facial nerves to analyse the effect of exogenous rhBMP-2 on axon regeneration after nerve injury.…”

Section: G Wu L Zhu T Jin Et Al Rhbmp-2 Increases Axonal Regenerationmentioning

confidence: 99%

Local Delivery of Recombinant Human Bone Morphogenetic Protein-2 Increases Axonal Regeneration and the Expression of Tau Protein after Facial Nerve Injury

Zhu

Jin

et al. 2010

J Int Med Res

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This study explored the function and possible mechanism of bone morphogenetic protein-2 (BMP-2) in the healing of injured peripheral nerves in vivo. Rabbit facial nerves were injured by clamping and then treated with recombinant human BMP-2 (rhBMP-2) or phosphate-buffered saline (control) by injecting once during surgery and twice a day post-injury for 7 days. Facial nerve fragments within 5 mm of the clamping point were examined at different times post-surgery. Axon structures visualized by Bielschowsky staining were similar in experimental and control nerves 2 and 6 weeks post-injury. At 4 weeks post-injury, cross-section images of facial nerves showed that axons treated with rhBMP-2 were denser and thicker, and levels of tau protein were increased. It is concluded from these data that rhBMP-2 may affect injured facial nerve regeneration by inducing more neurons to return to embryonic patterns of tau gene expression.

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Truncated Tau with the Fyn‐binding domain and without the microtubule‐binding domain hinders the myelinating capacity of an oligodendrocyte cell line

Abstract: The mechanisms underlying developmental myelination have therapeutic potential following CNS injury and degeneration. We report that transplanted central glial (

Cited by 31 publications

References 49 publications

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

Untangling the role of tau in Alzheimer’s disease: A unifying hypothesis

Local Delivery of Recombinant Human Bone Morphogenetic Protein-2 Increases Axonal Regeneration and the Expression of Tau Protein after Facial Nerve Injury

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