4-Hydroxynonenal (HNE) modified proteins in metabolic diseases

被引：181

作者：

Castro, Jose Pedro ^{[1
,2
,5
,6
]}

Jung, Tobias ^{[1
,3
]}

Grune, Tilman ^{[1
,2
,3
,4
]}

Siems, Werner ^{[7
,8
]}

机构：

[1] German Inst Human Nutr, Dept Mol Toxicol, Potsdam, Germany

[2] German Ctr Diabet Res DZD, D-85764 Munich, Germany

[3] German Ctr Cardiovasc Res DZHK, D-10117 Berlin, Germany

[4] NutriAct Competence Cluster Nutr Sci Berlin Potsd, Nuthetal, Germany

[5] Univ Porto, Fac Med, Dept Biomed, P-4200319 Oporto, Portugal

[6] Inst Innovat & Hlth Res I3S, Aging & Stress Grp, P-4200135 Oporto, Portugal

[7] Inst Physiotherapy & Gerontol Kortexmed, D-38667 Bad Harzburg, Germany

[8] Univ Salzburg, Inst Biol, Dept Cellular Physiol, A-5020 Salzburg, Austria

来源：

FREE RADICAL BIOLOGY AND MEDICINE | 2017年 / 111卷

关键词：

4-hydroxynonenal; HNE-modified Proteins; Proteasome; Proteolysis; HNE metabolism; LIPID-PEROXIDATION; OXIDATIVE STRESS; OXYGEN RADICALS; 20S PROTEASOME; CROSS-LINKING; CELL-DEATH; CARBONYLATION; IDENTIFICATION; DEGRADATION; LIPOFUSCIN;

D O I：

10.1016/j.freeradbiomed.2016.10.497

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

4-Hydroxynonenal (HNE) is one of the quantitatively most important products of lipid peroxidation. Due to its high toxicity it is quickly metabolized, however, a small share of HNE avoids enzymatic detoxification and reacts with biomolecules including proteins. The formation of HNE-protein-adducts is one of the accompanying processes in oxidative stress or redox disbalance. The modification of proteins might occur at several amino acids side chains, leading to a variety of products and having effects on the protein function and fate. This review summarizes current knowledge on the formation of HNE-modified proteins, their fate in mammalian cells and their potential role as a damaging agents during oxidative stress. Furthermore, the potential of HNE-modified proteins as biomarkers for several diseases are highlighted.

引用

页码：309 / 315

页数：7

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