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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2001;21:467.)
© 2001 American Heart Association, Inc.

Editorial

Is Paraoxonase-3 Another HDL-Associated Protein Protective Against Atherosclerosis?

Bert N. La Du

From the Department of Pharmacology, University of Michigan Medical School, Ann Arbor.

Correspondence to Bert N. La Du, MD, PhD, Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109-0632.

Key Words: paraoxonase • high density lipoproteins • atherosclerosis

The article by Reddy et al¹ in the present issue of Arteriosclerosis, Thrombosis, and Vascular Biology is the first report of expression of human paraoxonase-3 (PON3) and its ability to prevent the formation of mildly oxidized LDL and also to inactivate preformed mildly oxidized LDL.

Investigations on mammalian serum paraoxonase (PON), now called PON1, started nearly 50 years ago by Aldridge^{2 3} with the study of its hydrolytic activity with paraoxon and other organophosphates. More recently, 5 years ago, it was established that PON1 is a member multigene family in mammals.⁴ There are 3 PON genes closely aligned on human chromosome 7 and mouse chromosome 6.

Research efforts on possible physiological functions of the PON family of enzymes have probably been hindered to some degree by their inappropriate designation as PONs (PON1, PON2, and PON3) and by the fact that most of our present knowledge of this homologous group of proteins has been limited to PON1, which does involve PON and arylesterase activities (reviewed by Durrington et al⁵ in the present issue of Arteriosclerosis, Thrombosis, and Vascular Biology). However, other members of the PON family (PON2 and PON3) from human and rabbit sources have recently been examined in our laboratory (Draganov et al;⁶ D.I. Draganov, personal communication), and these all completely lack PON activity and have very little, if any, arylesterase activity. Thus, PON activity of PON1 appears now to be a distinctive marker of its more recent evolutionary origin than the other PONs, but this eliminates PON activity as . . . [Full Text of this Article]

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