Macrophage recognition of LDL modified by levuglandin E2, an oxidation product of arachidonic acid |
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| Institution: | 1. Department of Cell Biology, Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA;2. Department of Chemistry, Case Western Reserve University, Cleveland, OH 44106, USA;1. Department of Anatomy & Cell Biology, Schulich Medicine and Dentistry, Medical Sciences Building Room 443, Western University, London, Ontario N6A 5C1, Canada;2. Matthew Mailing Centre for Translational Transplant Studies, 339 Windermere Rd., London Health Sciences Centre, London, Ontario N6A 5A5, Canada;3. Department of Biology, 1151 Richmond St., Western University, London, Ontario N6A 5B7, Canada;4. London Regional Cancer Program, 790 Commissioners Rd. E, London Health Sciences Centre, London, Ontario N6A 5A5, Canada;5. Department of Surgery, Schulich Medicine and Dentistry, 268 Grosvenor St., St Joseph''s Hospital, London, Ontario N6A 4V2, Canada;6. Translational Prostate Cancer Research Laboratory, F3-124, 268 Grosvenor St., St Joseph''s Hospital, London, Ontario N6A 4V2, Canada;7. Department of Chemistry & Biochemistry, 1253 University of Oregon, University of Oregon, Eugene, OR 97403, USA;8. Department of Microbiology and Immunology, Schulich Medicine and Dentistry, Dental Sciences Building Room 3014, Western University, London, Ontario N6A 5C1, Canada;9. Schulich School of Medicine and Dentistry, Clinical Skills Building, Western University, London, Ontario N6A 5C1, Canada;10. Department of Oncology, Schulich Medicine and Dentistry, 790 Commissioners Rd. E Room A4901, London Regional Cancer Program, London, Ontario N6A 4L6, Canada;11. Multiorgan Transplant Program, 339 Windermere Rd., London Health Sciences Centre, London, Ontario N6A 5A5, Canada;1. Kolling Institute of Medical Research, Royal North Shore Hospital, and The University of Sydney, Sydney, Australia;2. Department of Cardiology, Royal North Shore Hospital, Sydney, Australia;3. Division of Perinatal Research, Royal North Shore Hospital, Sydney, Australia;1. Department of Anesthesiology, Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27159-1009, USA;2. Department of Cardiology, Jinan Central Hospital, Affiliated with Shandong University, 105 Jiefang Road, Jinan, 250013, China;3. Hypertension and Vascular Disease Center, Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA;4. Office of Women in Medicine and Science, Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA;1. Department of Microbiology and Immunology, Western University, London, Ontario, Canada;2. Department of Surgery, Western University, London, Ontario, Canada;3. Department of Pathology, Western University, London, Ontario, Canada;4. Schulich School of Medicine and Dentistry, Western University, London, Ontario, Canada;5. Multi-Organ Transplant Program, London Health Sciences Center, London, Ontario, Canada;6. Matthew Mailing Center for Translational Transplant Studies, London Health Sciences Center, London, Ontario, Canada;7. University of Exeter Medical School, University of Exeter, Exeter, Devon, United Kingdom;1. Histology, Embryology and Cell Biology Laboratory, Medicine School, University of Tunis El Manar, Jabbari Jebel Lakhdar Street 15, 1007 Tunis, Tunisia;2. Experimental Medicine Unit, Medicine School, University of Tunis El Manar, Jabbari Jebel Lakhdar Street 15, 1007 Tunis, Tunisia;3. Laboratory of Organic Synthesis and Heterocyclic Chemistry Department, School of Sciences of Tunis, University of Tunis El Manar, 2092 Tunis, Tunisia;4. Central Preparation Unit of Cytotoxic, Salah Azaiz Institute, Bab Saâdoun Square, 1006 Tunis, Tunisia |
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| Abstract: | Levuglandin (LG) E2, a secoprostanoic acid levulinaldehyde derivative, is a product of free radical oxidation that forms covalent adducts with lysyl residues on proteins. Treatment of LDL with LGE2 leads to uptake and degradation by mouse peritoneal macrophages. Oxidized LDL, but not acetyl LDL efficiently competed for binding and uptake of LGE2-modified 125I-LDL. This result suggests that LGE2-modified LDL was recognized by a class of scavenger receptor that demonstrated ligand specificity for oxidized LDL but not for acetyl LDL. |
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