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Research Article Open access CC BY 4.0

The Essentials of Biochemistry of the Proteins as Related to Alzheimer’s Disease: A Review

A. S. V. Prasad

International Journal of Biochemistry Research & Review · pp. 34–49 · Published 22 Feb 2020

10.9734/ijbcrr/2020/v29i130163

Abstract

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.

Amyloid Precursor Protein (APP) amyloid beta amyloid plaques tau protein amyloid cascade theory amyloidogenic pathway non-amyloidogenic pathway secretases.

References (28)

  1. 1 Neuropathological stageing of Alzheimer-related changes [DOI]
  2. 2 Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo [DOI]
  3. 3 A protein factor essential for microtubule assembly. [DOI]
  4. 4 Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease [DOI]
  5. 5 Amyloid beta: structure, biology and structure-based therapeutic development [DOI]
  6. 6 The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease [DOI]
  7. 7 Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease [DOI]
  8. 8 Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau. [DOI]
  9. 9 Autophagy Induction and Autophagosome Clearance in Neurons: Relationship to Autophagic Pathology in Alzheimer's Disease [DOI]
  10. 10 The MAP1 family of microtubule-associated proteins. [DOI]
  11. 11 Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. [DOI]
  12. 12 Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques [DOI]
  13. 13 Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory [DOI]
  14. 14 Synapse Formation and Function Is Modulated by the Amyloid Precursor Protein [DOI]
  15. 15 The antimicrobial protection hypothesis of Alzheimer's disease [DOI]
  16. 16 Nuclear Tau, a Key Player in Neuronal DNA Protection [DOI]
  17. 17 Apolipoprotein E element 4 association with dementia in a population-based study [DOI]
  18. 18 Amyloid Peptide Channels [DOI]
  19. 19 The physiology of the β‐amyloid precursor protein intracellular domain AICD [DOI]
  20. 20 Non-Fibrillar Oligomeric Amyloid-β within Synapses [DOI]
  21. 21 Insulin-degrading Enzyme Rapidly Removes the β-Amyloid Precursor Protein Intracellular Domain (AICD) [DOI]
  22. 22 Phosphorylation of Tau Is Regulated by PKN [DOI]
  23. 23 Trafficking of Alzheimer's Disease–Related Membrane Proteins and Its Participation in Disease Pathogenesis [DOI]
  24. 24 The role of annealing and fragmentation in human tau aggregation dynamics [DOI]
  25. 25 Amino acid and hormonal control of macromolecular turnover in perfused rat liver. Evidence for selective autophagy. [DOI]
  26. 26 The Amyloidogenic Pathway of Amyloid Precursor Protein (APP) Is Independent of Its Cleavage by Caspases [DOI]
  27. 27 Microtubule Defects and Neurodegeneration [DOI]
  28. 28 Mode of action of yeast killer toxins: channel formation in lipid bilayer membranes [DOI]

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