The Involvement of Post-Translational Modifications in Alzheimer’s Disease

E-ISSN： 1875-5828|15|4|313-335

ISSN： 1567-2050

Source： Current Alzheimer Research, Vol.15, Iss.4, 2018-02, pp. : 313-335

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Abstract

Background: Alzheimer#39;s disease (AD) is a neurodegenerative disorder recognized as the mostcommon cause of chronic dementia among the ageing population. AD is histopathologically characterized byprogressive loss of neurons and deposits of insoluble proteins, primarily composed of amyloid-#946; pelaques andneurofibrillary tangles (NFTs).

Methods: Several molecular processes contribute to the formation of AD cellular hallmarks. Among them,post-translational modifications (PTMs) represent an attractive mechanism underlying the formation of covalentbonds between chemical groups/peptides to target proteins, which ultimately result modified in their function.Most of the proteins related to AD undergo PTMs. Several recent studies show that AD-related proteinslike APP, A#946;, tau, BACE1 undergo post-translational modifications. The effect of PTMs contributes to thenormal function of cells, although aberrant protein modification, which may depend on many factors, candrive the onset or support the development of AD.

Results: Here we will discuss the effect of several PTMs on the functionality of AD-related proteins potentiallycontributing to the development of AD pathology.

Conclusion: We will consider the role of Ubiquitination, Phosphorylation, SUMOylation, Acetylation andNitrosylation on specific AD-related proteins and, more interestingly, the possible interactions that may occurbetween such different PTMs.