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A Novel Cell-Free, Non-Fluorescent Method to Measure LOX-1-Binding Activity Corresponding to The Functional Activity of HDL
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- Kakino Akemi
- Department of Molecular Pathophysiology, School of Medicine, Shinshu University Institute for Biomedical Sciences, Shinshu University Research Center for Next Generation Medicine, Shinshu University
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- Usami Yoko
- Department of Laboratory Medicine, Shinshu University Hospital
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- Horiuchi Sayaka
- Department of Molecular Pathophysiology, School of Medicine, Shinshu University
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- Fujita Yoshiko
- Department of Molecular Pathophysiology, School of Medicine, Shinshu University Research Center for Next Generation Medicine, Shinshu University
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- Kotani Kazuhiko
- Division of Community and Family Medicine, Jichi Medical University
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- Chen Chu-Huang
- Lipid Science and Aging Research Center, Kaohsiung Medical University Vascular and Medicinal Research, Texas Heart Institute Centers for Lipid Biosciences, Kaohsiung Medical University Hospital Graduate Institute of Medicine, College of Medicine, Kaohsiung Medical University
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- Okamura Tomonori
- Department of Preventive Medicine and Public Health, Keio University School of Medicine
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- Sawamura Tatsuya
- Department of Molecular Pathophysiology, School of Medicine, Shinshu University Institute for Biomedical Sciences, Shinshu University Research Center for Next Generation Medicine, Shinshu University Graduate Institute of Medicine, College of Medicine, Kaohsiung Medical University
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Description
<p>Aims: A functional abnormality in high-density lipoprotein (HDL) particles rather than a quantitative abnormality in HDL cholesterol levels has been suggested to promote atherosclerosis. The modification of HDL may underlie functional changes to HDL such as gaining the ability to bind and activate the lectin-like oxidized low-density lipoprotein (LDL) receptor-1 (LOX-1). We aimed to develop a novel method for measuring modified HDL on the basis of its binding to LOX-1.</p><p>Methods: We designed a LOX-1 binding–based enzyme-linked immunosorbent assay (ELISA) with recombinant LOX-1 and anti-apoAI antibody. A lipid-free standard was devised by making a chimeric fusion protein containing anti-LOX-1 antibody and human apoAI fragment. We used this system to detect modified HDL, designated as LOX-1 ligand containing apoAI (LAA).</p><p>Results: With our ELISA system, we detected HDL modified by copper oxidation, hypochlorous acid, 4-hydroxynonenal, and potassium cyanate, but not native HDL. Upon oxidation, HDL showed increased LOX-1 binding activity and decreased cholesterol efflux and paraoxonase-1 activities. In the ELISA, the chimeric fusion protein standard showed minimal variation in reference binding curves in contrast to copper-oxidized HDL preparations, suggesting better quality control of the chimeric fusion protein as the standard for measuring modified HDL activity. LAA was detectable in the plasma of healthy individuals and of mice fed a high-fat diet.</p><p>Conclusion: We have developed a novel ELISA by using recombinant LOX-1 and anti-apoAI antibody to measure the activity of modified HDL in plasma.</p>
Journal
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- Journal of Atherosclerosis and Thrombosis
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Journal of Atherosclerosis and Thrombosis 26 (11), 947-958, 2019-11-01
Japan Atherosclerosis Society
