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Research Article Free access | 10.1172/JCI119634

Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL.

K Ishikawa, M Navab, N Leitinger, A M Fogelman, and A J Lusis

Department of Medicine, Division of Cardiology, UCLA School of Medicine, Los Angeles, California 90095-1679, USA.

Find articles by Ishikawa, K. in: JCI | PubMed | Google Scholar

Department of Medicine, Division of Cardiology, UCLA School of Medicine, Los Angeles, California 90095-1679, USA.

Find articles by Navab, M. in: JCI | PubMed | Google Scholar

Department of Medicine, Division of Cardiology, UCLA School of Medicine, Los Angeles, California 90095-1679, USA.

Find articles by Leitinger, N. in: JCI | PubMed | Google Scholar

Department of Medicine, Division of Cardiology, UCLA School of Medicine, Los Angeles, California 90095-1679, USA.

Find articles by Fogelman, A. in: JCI | PubMed | Google Scholar

Department of Medicine, Division of Cardiology, UCLA School of Medicine, Los Angeles, California 90095-1679, USA.

Find articles by Lusis, A. in: JCI | PubMed | Google Scholar

Published September 1, 1997 - More info

Published in Volume 100, Issue 5 on September 1, 1997
J Clin Invest. 1997;100(5):1209–1216. https://doi.org/10.1172/JCI119634.
© 1997 The American Society for Clinical Investigation
Published September 1, 1997 - Version history
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Abstract

Heme catabolic processes produce the antioxidants biliverdin and bilirubin, as well as the potent prooxidant free iron. Since these products have opposing effects on oxidative stress, it is not clear whether heme catabolism promotes or inhibits inflammatory processes, including atherosclerotic lesion formation. Heme oxygenase (HO) catalyzes the rate-limiting step of heme catabolism. We used cocultures of human aortic endothelial cells and smooth muscle cells to examine the possible role of HO in early atherosclerosis. Heme oxygenase-1 (HO-1), the inducible isoform of HO, was highly induced by mildly oxidized LDL, and augmented induction was observed with hemin pretreatment. This augmented HO-1 induction resulted in the reduction of monocyte chemotaxis in response to LDL oxidation. Conversely, inhibition of HO by a specific inhibitor, Sn-protoporphyrin IX, enhanced chemotaxis. Furthermore, pretreatment with biliverdin or bilirubin, the products of HO, reduced chemotaxis. Oxidized phospholipids in the mildly oxidized LDL appear to be responsible for HO-1 induction, since oxidized but not native arachidonic acid-containing phospholipids also induced HO-1. These results suggest that HO-1 induced by mildly oxidized LDL may protect against the induction of inflammatory responses in artery wall cells through the production of the antioxidants biliverdin and bilirubin.

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