Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease

doi:10.2174/1568026616666160216155927

NWIPB OpenIR

	Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease
	Blindauer, Claudia A.1; Khazaipoul, Siavash 2; Yu, Ruitao 2,3; Stewart, Alan J.2
	2016
发表期刊	CURRENT TOPICS IN MEDICINAL CHEMISTRY
卷号	16 期号:27 页码:3021-3032
文章类型	Review
摘要	Human serum albumin (HSA) is the major protein in blood plasma and is responsible for circulatory transport of a range of small molecules including fatty acids, metal ions and drugs. We previously identified the major plasma Zn2+ transport site on HSA and revealed that fatty-acid binding (at a distinct site called the FA2 site) and Zn2+ binding are interdependent via an allosteric mechanism. Since binding affinities of long-chain fatty acids exceed those of plasma Zn2+, this means that under certain circumstances the binding of fatty acid molecules to HSA is likely to diminish HSA Zn2+-binding, and hence affects the control of circulatory and cellular Zn2+ dynamics. This relationship between circulatory fatty acid and Zn2+ dynamics is likely to have important physiological and pathological implications, especially since it has been recognised that Zn2+ acts as a signalling agent in many cell types. Fatty acid levels in the blood are dynamic, but most importantly, chronic elevation of plasma fatty acid levels is associated with some metabolic disorders and disease states-including myocardial infarction and other cardiovascular diseases. In this article, we briefly review the metal-binding properties of albumin and highlight the importance of their interplay with fatty acid binding. We also consider the impact of this dynamic link upon levels and speciation of plasma Zn2+, its effect upon cellular Zn2+ homeostasis and its relevance to cardiovascular and circulatory processes in health and disease.
关键词	Allostery Circulation Fatty Acid Protein-lipid Interactions Protein-metal Interactions Serum Albumin
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
DOI	10.2174/1568026616666160216155927
关键词[WOS]	ISCHEMIA-MODIFIED ALBUMIN ; HISTIDINE-RICH GLYCOPROTEIN ; ACUTE MYOCARDIAL-INFARCTION ; ACUTE CORONARY SYNDROME ; PROTEIN-KINASE-C ; FACTOR NF-KAPPA ; ZINC-DEFICIENCY ; COBALT BINDING ; ENDOTHELIAL-CELLS ; CRYSTAL-STRUCTURE
收录类别	SCI
语种	英语
项目资助者	Biotechnology and Biological Sciences Research Council(BB/J006467/1) ; Chinese Academy of Sciences
WOS研究方向	Pharmacology & Pharmacy
WOS类目	Chemistry, Medicinal
WOS记录号	WOS:000385563100002
引用统计	被引频次：24[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://210.75.249.4/handle/363003/6417
专题	中国科学院西北高原生物研究所
作者单位	1.Univ Warwick, Dept Chem, Gibbet Hill Rd, Coventry CV4 7AL, W Midlands, England 2.Univ St Andrews, Sch Med, St Andrews KY16 9TF, Fife, Scotland 3.Chinese Acad Sci, Northwest Inst Plateau Biol, Xining 810008, Peoples R China
推荐引用方式 GB/T 7714	Blindauer, Claudia A.,Khazaipoul, Siavash,Yu, Ruitao,et al. Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease[J]. CURRENT TOPICS IN MEDICINAL CHEMISTRY,2016,16(27):3021-3032.
APA	Blindauer, Claudia A.,Khazaipoul, Siavash,Yu, Ruitao,&Stewart, Alan J..(2016).Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease.CURRENT TOPICS IN MEDICINAL CHEMISTRY,16(27),3021-3032.
MLA	Blindauer, Claudia A.,et al."Fatty Acid-Mediated Inhibition of Metal Binding to the Multi-Metal Site on Serum Albumin: Implications for Cardiovascular Disease".CURRENT TOPICS IN MEDICINAL CHEMISTRY 16.27(2016):3021-3032.