Research Paper Volume 12, Issue 19 pp 19012—19021
Apremilast ameliorates ox-LDL-induced endothelial dysfunction mediated by KLF6
- 1 Department of Cardiology, The Second Medical Center, National Clinical Research Center for Geriatric Diseases, Chinese PLA General Hospital, Beijing 100853, China
- 2 Department of Nephrology, The Second Medical Center, National Clinical Research Center for Geriatric Diseases, Chinese PLA General Hospital, Beijing 100853, China
- 3 Department of Endocrinology, The Seventh Medical Center, Chinese PLA General Hospital, Beijing 100700, China
- 4 Department of Cardiology, The First Medical Center, Chinese PLA General Hospital, Beijing 100853, China
- 5 Department of General Practice, The First Medical Center, Chinese PLA General Hospital, Beijing 100853, China
Received: May 7, 2020 Accepted: June 22, 2020 Published: October 14, 2020
https://doi.org/10.18632/aging.103665How to Cite
Copyright: © 2020 Wang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Apremilast is a phosphodiesterase 4 (PDE4) inhibitor used in the treatment of psoriasis and several other inflammatory diseases. Interest has been expressed in seeking out therapies that address both psoriasis and atherosclerosis. In the present study, we explored the effects of apremilast in human aortic endothelial cells (HAECs) exposed to oxidized low-density lipoprotein (ox-LDL) to simulate the atherosclerotic microenvironment in vitro. Our findings indicate that apremilast may reduce the expression of lectin-like oxidized-low-density-lipoprotein receptor-1 (LOX-1), the main ox-LDL scavenging receptor. Apremilast also inhibited the expression of tumor necrosis factor-α (TNF-α), interleukin-6 (IL-6), and interleukin-8 (IL-8), which are deeply involved in the chronic inflammatory response associated with atherosclerosis. Interestingly, we found that apremilast inhibited the attachment of U937 monocytes to HAECs by reducing the expression of the chemokine monocyte chemotactic protein 1 (MCP-1) and the cellular adhesion molecule vascular cell adhesion molecule-1 (VCAM-1). This effect was found to be mediated through the rescue of Krüppel like factor 6 (KLF6) expression, which was reduced in response to ox-LDL via increased phosphorylation of c-Jun N-terminal kinase (JNK). These findings suggest a potential role for apremilast in the treatment of atherosclerosis.