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(Circulation. 2003;108:2041.)
© 2003 American Heart Association, Inc.

Special Review

Biomarkers of Vascular Disease Linking Inflammation to Endothelial Activation

Part II

Paul E. Szmitko, BSc; Chao-Hung Wang, MD; Richard D. Weisel, MD; Greg A. Jeffries, BSc; Todd J. Anderson, MD; Subodh Verma, MD, PhD

From the Division of Cardiology, University of Calgary, Calgary, Alberta (T.J.A.) and Division of Cardiac Surgery, University of Toronto, Toronto, Ontario (P.E.S., C.-H.W., R.D.W., G.A.J., S.V.), Canada.

Correspondence to Subodh Verma, MD, PhD, Division of Cardiac Surgery, Toronto General Hospital, 14EN-215, 200 Elizabeth St, Toronto, Ontario, Canada M5G 2C4. E-mail subodh.verma@sympatico.ca

An extract of the first 250 words of the full text is provided, because this article has no abstract.

	Introduction

 
Atherosclerosis is regarded as a dynamic and progressive disease arising from the combination of endothelial dysfunction and inflammation.^1–6 This article is the second in a 2-part series examining emerging markers of inflammation and endothelial cell activation. The first article⁷ provided a brief overview of the link between inflammation, endothelial dysfunction, and atherosclerosis and began the examination of emerging inflammatory mediators. This second article continues with an exploration of more novel markers for cardiovascular disease.

	Novel Inflammatory Mediators of Inflammation and Endothelial Cell Activation

 
Lectin-Like Oxidized Low-Density Lipoprotein (LDL) Receptor-1
The endothelial injury, activation, and dysfunction caused by oxidized LDL (oxLDL) in the pathogenesis of atherosclerosis are exerted via lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1) activation.^8,9 LOX-1, initially identified as the major receptor for oxLDL in endothelial cells, can also be expressed in macrophages and smooth muscle cells (SMCs).^10–12 It is a type II membrane protein with a C-type lectin–like extracellular domain that can be cleaved, to release the soluble form of LOX-1, by an unknown protease.⁸ In addition to being the main receptor for oxLDL, LOX-1 has the ability to bind damaged or apoptotic cells, activated platelets, advanced glycation end products, and pathogenic organisms.^13–15 Once bound, these ligands can be endocytosed or phagocytosed into the cell. Under physiological conditions, LOX-1 may play a role in host defense or serve to scavenge cellular debris.⁸ However, in pathological states, LOX-1 may be involved in binding proatherogenic materials, such as oxLDL, that activate the endothelium. With its ability to bind products that induce inflammation and endothelial activation, it is not surprising that elevated LOX-1 expression is observed in . . . [Full Text of this Article]

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