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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2002;22:1365.)
© 2002 American Heart Association, Inc.

Editorials

Lysyl Oxidase

New Looks on LOX

Ruud A. Bank; Victor W.M. van Hinsbergh

From the TNO Prevention and Health (R.A.B, V.W.M.v.H.) Gaubius Laboratory, Leiden, and Department of Physiology (V.W.M.v.H.), Institute for Cardiovascular Research, VU University Medical Center, Amsterdam, The Netherlands.

Correspondence to V.W.M. van Hinsbergh, PhD, Gaubius Laboratory TNO-PG, Zernikedreef 9, 2301 CE Leiden. E-mail vwm.vanhinsbergh@pg.tno.nl

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

The extracellular matrix proteins collagen and elastin determine, to a large extent, the biomechanical properties of the vessel wall. Both molecules are secreted as monomers, but are posttranslationally modified in the extracellular space in order to generate stable polymers. A critical feature of collagen and elastin fibers is the degree of cross-linking. The first step in cross-linking is the oxidative deamination of the -amino group of certain peptidyl (hydroxy)lysyl residues, resulting in the aldehyde (hydroxy)allysine. In collagen, (hydroxy)allysine is restricted to the C- and N-telopeptide. The aldehyde reacts with a lysyl (Lys) or hydroxylysyl (Hyl) residue in the triple helix, resulting in a variety of cross-links.¹ In elastin, the oxidative deamination of Lys (Hyl is absent in elastin) is less restrictive, resulting in modification of most of the Lys residues. Well known elastin cross-links are lysinonorleucine and the pyridiniums desmosine and isodesmosine.¹ The cross-links in collagen are responsible for the stiffness of collagen fibers,² whereas the cross-links in elastin are important for the rubber-like properties of elastin fibers.³

See page 1409

The enzyme responsible for the oxidative deamination of the -amino groups is lysyl oxidase (LOX), a copper-dependent amine oxidase.⁴ Reduced activity levels of this enzyme result in decreased degree of cross-linking, affecting the biomechanical properties of extracellular matrices² as well as the susceptibility of collagen and elastin to degradation by proteinases.⁵

In this issue, Rodríguez et al⁶ describe the downregulation of LOX expression in porcine endothelial cells subjected to atherogenic levels of LDL. The authors hypothesize that . . . [Full Text of this Article]