Monoamine oxidases in age-associated diseases: New perspectives for old enzymes.
Age-associated chronic diseases
Autophagy
Mitochondria
Monoamine oxidases
ROS
Senescence
Journal
Ageing research reviews
ISSN: 1872-9649
Titre abrégé: Ageing Res Rev
Pays: England
ID NLM: 101128963
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
04
09
2020
revised:
04
12
2020
accepted:
05
01
2021
pubmed:
13
1
2021
medline:
27
3
2021
entrez:
12
1
2021
Statut:
ppublish
Résumé
Population aging is one of the most significant social changes of the twenty-first century. This increase in longevity is associated with a higher prevalence of chronic diseases, further rising healthcare costs. At the molecular level, cellular senescence has been identified as a major process in age-associated diseases, as accumulation of senescent cells with aging leads to progressive organ dysfunction. Of particular importance, mitochondrial oxidative stress and consequent organelle alterations have been pointed out as key players in the aging process, by both inducing and maintaining cellular senescence. Monoamine oxidases (MAOs), a class of enzymes that catalyze the degradation of catecholamines and biogenic amines, have been increasingly recognized as major producers of mitochondrial ROS. Although well-known in the brain, evidence showing that MAOs are also expressed in a variety of peripheral organs stimulated a growing interest in the extra-cerebral roles of these enzymes. Besides, the fact that MAO-A and/or MAO-B are frequently upregulated in aged or dysfunctional organs has uncovered new perspectives on their roles in pathological aging. In this review, we will give an overview of the major results on the regulation and function of MAOs in aging and age-related diseases, paying a special attention to the mechanisms linked to the increased degradation of MAO substrates or related to MAO-dependent ROS formation.
Identifiants
pubmed: 33434685
pii: S1568-1637(21)00003-9
doi: 10.1016/j.arr.2021.101256
pii:
doi:
Substances chimiques
Monoamine Oxidase
EC 1.4.3.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
101256Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.