期刊
JOURNAL OF THE AMERICAN SOCIETY OF HYPERTENSION
卷 3, 期 6, 页码 374-387出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jash.2009.09.004
关键词
O-Linked beta-N-acetylglucosaminylation (O-GlcNAc); vascular (dys)function; protein kinases
资金
- National Institutes of Health
- Cardiovascular Discovery Institute
- EUA
- CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior), Brazil
O-Linked attachment of beta-N-acetyl-glucosamine (O-GlcNAc) on serine and threonine residues of nuclear and cytoplasmic proteins is a highly dynamic posttranslational modification that plays a key role in signal transduction pathways. Preliminary data show that O-GlcNAcylation may represent a key regulatory mechanism in the vasculature, modulating contractile and relaxant responses. Proteins with an important role in vascular function, such as endothelial nitric oxide synthase, sarcoplasmic reticulum Ca2+-ATPase, protein kinase C, mitogen-activated protein kinases, and proteins involved in cytoskeleton regulation and microtubule assembly are targets for O-GlcNAcylation, indicating that this posttranslational modification may play an important role in vascular reactivity. Here, we will focus on a few specific pathways that contribute to vascular function and cardiovascular disease associated vascular dysfunction, and the implications of their modification by O-GlcNAc. New chemical tools have been developed to detect and study O-GlcNAcylation, including inhibitors of O-GlcNAc enzymes, chemoenzymatic tagging methods, and quantitative proteomics strategies; these will also be briefly addressed. An exciting challenge in the future will be to better understand the cellular dynamics of this posttranslational modification, as well as the signaling pathways and mechanisms by which O-GlcNAc is regulated on specific proteins in the vasculature in health and disease. J Am Soc Hypertens 2009;3(6):374-387. (C) 2009 American Society of Hypertension. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据