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Proteasome activation plays role in 18α-glycyrrhetinic acid protectiveeffect in 5XFAD animal model of Alzheimer’s disease

Mladenović, Aleksandra; Jović, Milena; Lončarević-Vasiljković, Nataša; Athanasopoulou, Sofia; Gonos, Efstathios S; Kanazir, Selma

(Belgrade: Serbian Neuroscience Society, 2017)

TY  - CONF
AU  - Mladenović, Aleksandra
AU  - Jović, Milena
AU  - Lončarević-Vasiljković, Nataša
AU  - Athanasopoulou, Sofia
AU  - Gonos, Efstathios S
AU  - Kanazir, Selma
PY  - 2017
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/5809
AB  - Introduction. Aging represents the most important risk factor for Alzheimer’s
disease (AD), the most common neurodegenerative disorders worldwide. One of 
the hallmarks of AD is the accumulation of plaques composed of aggregated 
amyloid-β peptides (Aβ) which are formed by sequential proteolytic processing 
of the amyloid-precursor protein (APP).It is well known that different factors 
can influence amyloidogenic pathway and/or clearance of already formed Aβ. 
Growing evidence suggest that ubiquitin proteasomal system represents an 
important factor in AD development and a potential target for the management 
of disease. Recently it has been shown that several natural compounds, 
including 18α-glycyrrhetinic acid (18α-GA) protects from protein aggregation related pathology in AD model system. Methods. In order to investigate the 
protective effect of 18α-GA, we used 5xFAD transgenic mouse AD model, 
characterized by early amyloid deposition and intra-neuronal Aβ42 aggregation. 
Both female and male mice were exposed to 18α-GA treatment for one month, 
started at 2-months of age. This is considered as an early phase of AD pathology, 
known to be suitable for therapeutics application. In the cortex and 
hippocampus CT-L, T-L, and PGPH proteasome activities were assayed by 
hydrolysis of Suc-LLVY-AMC, Boc-LRR-AMC, and Z-LLE-AMC fluorogenic 
peptides. The number and size of amyloid plaques were determined in these 
structures. Results. This study revealed that 18α-GA treatment influence 
neuritic dystrophy, increase proteasome activity, decrease Aβ content and 
number of amyloid plaques in 5xFAD mice. Conclusion. These preliminary 
intriguing data open up new directions using natural compounds for the most 
efficient treatment of neurodegenerative disorders.
PB  - Belgrade: Serbian Neuroscience Society
C3  - Book of Abstract: 7th Congress of Serbian Neuroscience Society with international participation; 2017 Oct 25-27; Belgrade, Serbia
T1  - Proteasome activation plays role in 18α-glycyrrhetinic acid protectiveeffect in 5XFAD animal model of Alzheimer’s disease
SP  - 109
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_5809
ER  - 
@conference{
author = "Mladenović, Aleksandra and Jović, Milena and Lončarević-Vasiljković, Nataša and Athanasopoulou, Sofia and Gonos, Efstathios S and Kanazir, Selma",
year = "2017",
abstract = "Introduction. Aging represents the most important risk factor for Alzheimer’s
disease (AD), the most common neurodegenerative disorders worldwide. One of 
the hallmarks of AD is the accumulation of plaques composed of aggregated 
amyloid-β peptides (Aβ) which are formed by sequential proteolytic processing 
of the amyloid-precursor protein (APP).It is well known that different factors 
can influence amyloidogenic pathway and/or clearance of already formed Aβ. 
Growing evidence suggest that ubiquitin proteasomal system represents an 
important factor in AD development and a potential target for the management 
of disease. Recently it has been shown that several natural compounds, 
including 18α-glycyrrhetinic acid (18α-GA) protects from protein aggregation related pathology in AD model system. Methods. In order to investigate the 
protective effect of 18α-GA, we used 5xFAD transgenic mouse AD model, 
characterized by early amyloid deposition and intra-neuronal Aβ42 aggregation. 
Both female and male mice were exposed to 18α-GA treatment for one month, 
started at 2-months of age. This is considered as an early phase of AD pathology, 
known to be suitable for therapeutics application. In the cortex and 
hippocampus CT-L, T-L, and PGPH proteasome activities were assayed by 
hydrolysis of Suc-LLVY-AMC, Boc-LRR-AMC, and Z-LLE-AMC fluorogenic 
peptides. The number and size of amyloid plaques were determined in these 
structures. Results. This study revealed that 18α-GA treatment influence 
neuritic dystrophy, increase proteasome activity, decrease Aβ content and 
number of amyloid plaques in 5xFAD mice. Conclusion. These preliminary 
intriguing data open up new directions using natural compounds for the most 
efficient treatment of neurodegenerative disorders.",
publisher = "Belgrade: Serbian Neuroscience Society",
journal = "Book of Abstract: 7th Congress of Serbian Neuroscience Society with international participation; 2017 Oct 25-27; Belgrade, Serbia",
title = "Proteasome activation plays role in 18α-glycyrrhetinic acid protectiveeffect in 5XFAD animal model of Alzheimer’s disease",
pages = "109",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_5809"
}
Mladenović, A., Jović, M., Lončarević-Vasiljković, N., Athanasopoulou, S., Gonos, E. S.,& Kanazir, S.. (2017). Proteasome activation plays role in 18α-glycyrrhetinic acid protectiveeffect in 5XFAD animal model of Alzheimer’s disease. in Book of Abstract: 7th Congress of Serbian Neuroscience Society with international participation; 2017 Oct 25-27; Belgrade, Serbia
Belgrade: Serbian Neuroscience Society., 109.
https://hdl.handle.net/21.15107/rcub_ibiss_5809
Mladenović A, Jović M, Lončarević-Vasiljković N, Athanasopoulou S, Gonos ES, Kanazir S. Proteasome activation plays role in 18α-glycyrrhetinic acid protectiveeffect in 5XFAD animal model of Alzheimer’s disease. in Book of Abstract: 7th Congress of Serbian Neuroscience Society with international participation; 2017 Oct 25-27; Belgrade, Serbia. 2017;:109.
https://hdl.handle.net/21.15107/rcub_ibiss_5809 .
Mladenović, Aleksandra, Jović, Milena, Lončarević-Vasiljković, Nataša, Athanasopoulou, Sofia, Gonos, Efstathios S, Kanazir, Selma, "Proteasome activation plays role in 18α-glycyrrhetinic acid protectiveeffect in 5XFAD animal model of Alzheimer’s disease" in Book of Abstract: 7th Congress of Serbian Neuroscience Society with international participation; 2017 Oct 25-27; Belgrade, Serbia (2017):109,
https://hdl.handle.net/21.15107/rcub_ibiss_5809 .