Affiliations: [a] Student Research Committee, Urmia University of Medical Sciences, Urmia, Iran
| [b] Department of Pharmacology and Toxicology, Faculty of Pharmacy, Urmia University of Medical Sciences, Urmia, Iran
| [c] Research Center for Experimental and Applied Pharmaceutical Sciences, Urmia University of Medical Sciences, Urmia, Iran
Correspondence:
[*]
Correspondence to: Mohammad Rafi Khezri, Pharm.D student, Department of Pharmacology and Toxicology, Faculty of Pharmacy, Urmia University of Medical Sciences, Sero Road, Urmia 5715799313, Iran. Fax: +98 4432754990; E-mail: drmnkh76@gmail.com. ORCID: 0000-0002-4280-0378 and Dr. Morteza Ghasemnejad-Berenji, Assistant
Professor of Pharmacology, Department of Pharmacology and Toxicology, Faculty of Pharmacy, Urmia University of
Medical Sciences, Urmia, Iran. E-mail: ghasemnejad.m@umsu.ac.ir. ORCID: 0000-0001-5672-9202
Abstract: Alzheimer’s disease (AD) is the most common neurodegenerative disorder worldwide. Although the main cause of the onset and development of AD is not known yet, neuronal death due to pathologic changes such as amyloid-β (Aβ) deposition, tau aggregation, neuroinflammation, oxidative stress, and calcium dyshomeostasis are considered to be the main cause. At the present, there is no cure for this insidious disorder. However, accurate identification of molecular changes in AD can help provide new therapeutic goals. Caspases are a group of proteases which are known because of their role in cellular apoptosis. In addition, different caspases are involved in other cellular responses to the environment, such as induction of inflammation. Emerging evidence suggest that these proteases play a central role in AD pathophysiology due to their role in the processing of amyloid-β protein precursor, tau cleavage, and neuroinflammation. Therefore, it seems that targeting caspases may be a suitable therapeutic option to slow the progression of AD. This review focuses on the role of caspases in AD pathophysiology and introduce results from studies targeted caspases in different models of AD.
