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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2007;27:445.)
© 2007 American Heart Association, Inc.

Editorials

PLA₂-V

A Real Player in Atherogenesis

Katariina Öörni; Petri T. Kovanen

From the Wihuri Research Institute, Helsinki, Finland.

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

An important early step in atherosclerosis is binding of apolipoprotein B-100 (apoB-100)–containing lipoproteins (VLDL, IDL, and LDL) to the proteoglycan component of the extracellular matrix of the arterial intima.^1,2 When oxidative agents or enzymes attack the proteoglycan-bound lipoproteins, they become oxidatively modified, and when various intimal proteases or lipases hydrolyze them, they become nonoxidatively modified. Whereas oxidation of proteoglycan-bound apoB-100–containing particles triggers their release and subsequent uptake by macrophages, the nonoxidative modifications do the opposite: they enhance the strength of particle binding to proteoglycans.³ In addition, such nonoxidatively modified apoB-100–containing lipoprotein particles tend to aggregate and fuse, which allows progressive extracellular accumulation of lipoprotein lipids, a key phenomenon in atherogenesis. The nonoxidative modifications can also lead to intracellular lipid accumulation and so induce foam cell formation, a hallmark of early atherogenesis.⁴ Thus, local modification of apoB-100–containing lipoproteins leads to both extra- and intracellular accumulation of lipids in the arterial intima.

See page 600

In general, the nonoxidative modifications are caused by enzymes that are hydrolytic in nature, either proteolytic or lipolytic. Indeed, the arterial intima contains many different types of hydrolytic enzymes capable of lipoprotein modification. Unfortunately, however, it is currently not known which hydrolytic enzymes of the human arterial intima are actually responsible for turning the intimal lipoproteins into atherogenic particles. Among the lipolytic enzymes potentially involved in such atherogenic conversion of lipoproteins are several members of the secretory phospholipase A₂ (sPLA₂) family. The hydrolytic action of these enzymes on phosphatidylcholine, the major glycerophospholipid in lipoprotein particles, leads . . . [Full Text of this Article]

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Arterioscler Thromb Vasc Biol 2007 27: 600-606. [Abstract] [Full Text] [PDF]

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