Role of Posttranslational Modifications of Proteins in Cardiovascular Disease

Abstract

Cardiovascular disease (CVD) has become a leading cause of mortality and morbidity globally, making it an urgent concern. Although some studies have been performed on CVD, its molecular mechanism remains largely unknown for all types of CVD. However, recent in vivo and in vitro studies have successfully identified the important roles of posttranslational modifications (PTMs) in various diseases, including CVD. Protein modification, also known as PTMs, refers to the chemical modification of specific amino acid residues after protein biosynthesis, which is a key process that can influence the activity or expression level of proteins. Studies on PTMs have contributed directly to improving the therapeutic strategies for CVD. In this review, we examined recent progress on PTMs and highlighted their importance in both physiological and pathological conditions of the cardiovascular system. Overall, the findings of this review contribute to the understanding of PTMs and their potential roles in the treatment of CVD.

Virus-Associated CD8 + T-Cells Are Not Activated Through Antigen-Mediated Interaction Inside Atherosclerotic Lesions

“…51 In the atherosclerotic lesion, proteins can be posttranslationally modified via oxidation, acetylation, phosphorylation, succinylation, O-GlcNAcylation, methylation, ubiquitination, Sumoylation, glutathionylation, tyrosine nitration, and propionylation. 52 Only 2 out of 85 potential mimicry peptides presented posttranslational oxidation on methionine (Table S7), indicating that cross-reactivity of virus-associated CD8 + T-cells against posttranslationally modified mimicry peptides in the lesion is unlikely.…”

Sex-specific mechanisms of cerebral microvascular BKCadysfunction in a mouse model of Alzheimer’s disease

“…Together, this nitro-oxidative environment can result in exacerbated PTMs within the BK α subunit. PTMs are the result of binding of different moieties to proteins, such as phosphorylation, acetylation, lipidation, oxidation and nitrosylation 24,54 . PTMs play a vital role in the known heterogeneity and tissue specificity of the biophysical properties of BK Ca , as they have profound effects on gating, voltage and Ca 2+ sensitivity, and membrane availability of the channel 16 .…”

Orthogonal Translation for Site-Specific Installation of Post-translational Modifications

“…Later, lysine acetylation in histones was discovered by Vincent Allfrey in 1964 . During the past decade, PTM studies have encountered a new era with the development of advanced proteomics techniques that have identified more than 600 distinct types of PTMs in thousands of proteins covering almost all the biological processes in bacteria, archaea, and eukarya. − PTMs can change charges of protein side chains such as phosphorylation and acetylation to affect substrate binding or interactions with other biomolecules. − PTMs can also add specific tags to proteins for triggering corresponding biological processes such as ubiquitination and glycosylation. − More importantly, PTMs have been found to be closely associated with a variety of human diseases including cancers, cardiovascular diseases, diabetes, neurodegenerative diseases, and even coronavirus diseases in the recent COVID-19 pandemic . Thus, protein PTMs have been attracting attentions of scientists from different research fields for decades.…”

“…11−14 PTMs can also add specific tags to proteins for triggering corresponding biological processes such as ubiquitination and glycosylation. 15−18 More importantly, PTMs have been found to be closely associated with a variety of human diseases including cancers, 19 cardiovascular diseases, 20 diabetes, 21 neurodegenerative diseases, 22 and even coronavirus diseases in the recent COVID-19 pandemic. 23 Thus, protein PTMs have been attracting attentions of scientists from different research fields for decades.…”