Open AccessThe Essentials of Biochemistry of the Proteins as Related to Alzheimer’s Disease: A Review
Author(s) -
Atul Prasad
Publication year - 2020
Publication title -
international journal of biochemistry research and review
Language(s) - English
Resource type - Journals
ISSN - 2231-086X
DOI - 10.9734/ijbcrr/2020/v29i130163
Subject(s) - tangle , hyperphosphorylation , intracellular , tau protein , neurofibrillary tangle , amyloid precursor protein , neuroscience , extracellular , alzheimer's disease , phosphatase , senile plaques , amyloid (mycology) , disease , microbiology and biotechnology , biology , chemistry , biochemistry , kinase , medicine , enzyme , pathology , mathematics , pure mathematics
Amyloid plaques and Tau tangles, constitute the pathological hallmarks of the brains of the patients suffering from Alzheimer’s disease. They are identified as far back as 1996 by Alois Alzheimer, a German psychiatrist and neuropathologist, but till this date, how they produce neuronal death remained an enigma. The amyloid cascade theory held its sway until recent times until the emphasis is shifted to the metabolites of amyloid Beta precursor protein (APP). Several metabolites of APP are formed depending on by which pathway, the APP is metabolized, either by the non -amyloidogenic pathway (forming α-C terminal fragment -CTFα / C83 and the N-terminal fragment sAPPα / P3 and the APP intracellular domain AICD). Or amyloidogenic pathways. (Forming extracellular Aβ and APP intracellular domain -AICD). The hyperphosphorylation is held responsible for the tau protein tangles. The over activity of the tau kinases or the failure of inhibition by the tau phosphatases is implicated, in tau tangle deposits. These biochemical aspects of AD assumed importance in connection with the interventional therapeutic strategies that are developed in the years bygone, as well as those still are in the developing stage. In keeping with this fact, it is attempted to review the essentials of the biochemical aspects of the involved proteins, as related to AD, in this article.