Acetylation Modification During Autophagy and Vascular Aging.

Jiaxing Sun,Mingxian Chen,Xuping Li,Hui Yang,Zhaowei Zhu,Liang Tang,Shenghua Zhou,Yichao Xiao,Shi Tai

doi:10.3389/fphys.2021.598267

Abstract

Vascular aging plays a pivotal role in the morbidity and mortality of elderly people. Decrease in autophagy leads to acceleration of vascular aging, while increase in autophagy leads to deceleration of vascular aging. And emerging evidence indicates that acetylation plays an important role in autophagy regulation; therefore, recent research has focused on an in-depth analysis of the mechanisms underlying this regulation. In this review, current knowledge on the role of acetylation of autophagy-related proteins and the mechanisms by which acetylation including non-autophagy-related acetylation and autophagy related acetylation regulate vascular aging have been discussed. We conclude that the occurrence of acetylation modification during autophagy is a fundamental mechanism underlying autophagy regulation and provides promising targets to retard vascular aging.

Highlights

Aging is a process of functional decline of life and is associated with an increase in age-related diseases (Lopez-Otin et al, 2013)
Autophagy is a classical pathway involved in many physiological processes, including the elimination of cellular organelles, stimulation of different stress factors, and remodeling of tissues during development
Acetylation acts as a novel regulator of autophagy and participates in the whole process of autophagy

Summary

INTRODUCTION

Aging is a process of functional decline of life and is associated with an increase in age-related diseases (Lopez-Otin et al, 2013). SIRT1 increases FOXO1 deacetylation, thereby increasing the expression of Rab, which is a small GTP-binding protein that mediates autophagosome–lysosome fusion in the later stages (Hariharan et al, 2010) This is the mechanism by which resveratrol reverses myocardial oxidative stress injury in diabetic mice (Wang et al, 2014), and by which curcumin protects HUVEC survival from oxidative stress damage (Han J. et al, 2012). ATG, autophagy-related protein; BECN1, beclin; EP300, E1A binding protein p300; FIP200, FAK family kinase-interacting protein of 200 kDa; GSK3β, glycogen synthase kinase-3β; HDAC, histone deacetylase; KAT, lysine acetyltransferase; LC3, microtubule-associated protein light chain 3; PIK3C3, phosphoinositide-3-kinase class 3; RB1CC1, RB1-inducible coiled-coil protein 1; TIP60, Tat-interactive protein 60 kDa; ULK1, unc-51-like kinase 1; VPS, vacuolar protein sorting.

O2 TMAO SIRT1 inhibition

CONCLUSION AND FUTURE PERSPECTIVES