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Targeting Mitochondrial Dynamics as a Restorative Approach in the Treatment of Alzheimer’s Disease

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Deciphering Drug Targets for Alzheimer’s Disease

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Abstract

The progressive damage and deprivation of neuronal cholinergic neurons lead to critical loss of learning and memory-based brain function, characterized as Alzheimer’s disease (AD). This disorder is associated with two main hall marker proteins in neurofibrillary tangles, i.e. amyloid-beta (Aβ) plaques and hyperphosphorylated tau along with α-synuclein, but none of them explains the complete aetiology of AD. Various attempts have been made to relate the complex interlinkage of tau and Aβ proteins with many other proteins to understand the pathophysiology of AD. Mitochondrial dynamics—a fusion and fission balance—has been linked to AD as its imbalance leads to elevated fragmentation of mitochondria and irregular mitochondrial distribution resulting in neuronal apoptosis and decline of cognitive function leading to AD. Aβ plaque formation in neuronal mitochondria imbalances the mitochondrial dynamic process by increasing the fission and reducing the fusion phenomenon. In this chapter, we tried to explore the role of different proteins such as Drp1, Fis1, Mff, MiD49, MiD51, and endophilin-B1 (mitochondrial fission proteins) and Mfn1/2, Opa1, Oma1, HDAC6, AIM2, and cAMP/PKA (mitochondrial fusion proteins) in the progression of AD, which would be targeted as potential targets for the treatment of AD in future.

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Abbreviations

AD:

Alzheimer’s disease

AIM2:

Absent in melanoma 2

APP:

Amyloid precursor protein

Aẞ:

Amyloid-beta

Ca2+:

Calcium

CL:

Cardiolipin

Drp1:

Dynamin-related protein 1

ER:

Endoplasmic reticulum

ETC:

Electron transport chain

Fis1:

Mitochondrial fission protein 1

HDAC6:

Histone deacetylase 6

IMM:

Inner mitochondrial membrane

l-OPA1:

Long-type optic atrophy protein 1

MAPT:

Microtubule-associated protein tau

Mff:

Mitochondrial fission factor

Mfn1/2:

Mitofusins 1 and 2

MiD49 and MiD51:

Mitochondrial dynamics proteins of 49 and 51 kDa

Oma1:

Overlapping with the M-AAA protease homolog

OMM:

Outer mitochondrial membrane

Opa1:

Optic atrophy protein 1

PS1:

Presenilin 1

PS2:

Presenilin 2

s-OPA1:

Short-type optic atrophy protein 1

SPs:

Senile plaques

YME1L:

Yeast mitochondrial AAA metalloprotease like 1 ATPase

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Authors and Affiliations

  1. Department of Pharmacology and Toxicology, National Institute of Pharmaceutical Education and Research (NIPER), Hajipur, Export Promotions Industrial Park (EPIP), Industrial Area, Hajipur, Bihar, India

    Ruchi Pandey, Priya Bisht, Anita Kumari, Adarsh Ray, V. Ravichandiran & Nitesh Kumar

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  1. Ruchi Pandey
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  2. Priya Bisht
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  3. Anita Kumari
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  4. Adarsh Ray
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  5. V. Ravichandiran
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  6. Nitesh Kumar
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Editor information

Editors and Affiliations

  1. Department of Entomology and Nematology, UC Davis Comprehensive Cancer Center, University of California, Davis, CA, USA

    Dileep Kumar

  2. Department of Pharmaceutical Chemistry, KIET School of Pharmacy, KIET Group of Institutions, Delhi-NCR, Ghaziabad, Uttar Pradesh, India

    Vaishali M. Patil

  3. Department of Radiological Sciences, Section of Medical Physics, University of Oklahoma, Norman, OK, USA

    Dee Wu

  4. Nuffield Department of Women’s & Reproductive Health, University of Oxford, Oxford, UK

    Nanasaheb Thorat

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Pandey, R., Bisht, P., Kumari, A., Ray, A., Ravichandiran, V., Kumar, N. (2023). Targeting Mitochondrial Dynamics as a Restorative Approach in the Treatment of Alzheimer’s Disease. In: Kumar, D., Patil, V.M., Wu, D., Thorat, N. (eds) Deciphering Drug Targets for Alzheimer’s Disease. Springer, Singapore. https://doi.org/10.1007/978-981-99-2657-2_9

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