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Abstract
Microtubule-associated Tau proteins belong to a family of factors that polymerize tubulin dimers and stabilize microtubules. Tau is strongly expressed in neurons, localized in the axon and is essential for neuronal plasticity and network. From the very beginning of Tau discovery, proteomics methods have been essential to the knowledge of Tau biochemistry and biology. In this review, we have summarized the main contributions of several proteomic methods in the understanding of Tau, including expression, post-translational modifications and structure, in both physiological and pathophysiological aspects. Finally, recent advances in proteomics technology are essential to develop further therapeutic targets and early predictive and discriminative diagnostic assays for Alzheimer’s disease and related disorders.
Financial & competing interests disclosure
This work was supported by Inserm, CNRS, IMPRT, University of Lille 2, Lille County Hospital (CHR-Lille), Région Nord/Pas-de-Calais, FEDER, and grants from Association Française contre les Myopathies (AFM2006-1579 and AFM2007-1043), GIP ANR-05-BLANC-0320-01, GIS-Longévité, and Fédération pour la Recherche sur le Cerveau and from the European Community: APOPIS (contract LSHM-CT-2003-503330) and cNEUPRO (contract LSHM-CT-2007-037950).
Alexis Brettville is a recipient from a scholarship co-sponsored by both Région Nord/Pas-de-Calais and CHR-Lille. Eugeen Vanmechelen and Pierre Grognet are both employees from Innogenetics NV, Gent, Belgium.
The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.