Scavenger receptors are associated with cellular interactions of S100A12 in vitro and in vivo |
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| Authors: | Susan Hoppmann Joerg Steinbach Jens Pietzsch |
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| Institution: | 1. 4th Department of Internal Medicine, University of Athens, Medical School, Greece;2. Department of Surgery, AHEPA Hospital, University of Thessaloniki Medical School, Thessaloniki, Greece;3. Laboratory of Molecular Pharmacology, School of Pharmacy, University of Patras, Greece;4. Department of Experimental Physiology, University of Athens, Medical School, Greece;1. Department of Traditional Chinese Medicine, Children''s Hospital of Fudan University, Shanghai 201102, China;2. Department of Nephrology, Children''s Hospital of Fudan University, Shanghai 201102, China;3. Pediatric Institute, Children''s Hospital of Fudan University, Shanghai 201102, China;4. Department of Pathology, Shanghai medical college of Fudan University, Shanghai 200032, China;1. EndoCeutics Inc, Quebec, QC, Canada;2. Oncology, Molecular Endocrinology, and Human Genomics Research Center, Laval University, Quebec, QC, Canada;1. Laboratory of Nutritional Physiology, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka, Shizuoka, Japan;2. Laboratory of Nutritional Physiology, School of Food and Nutritional Sciences, University of Shizuoka, Shizuoka, Japan;3. Laboratory of Food and Nutritional Sciences, Department of Local Produce and Food Sciences, Faculty of Life and Environmental Sciences, University of Yamanashi, Yamanashi, Japan;1. Nursing Research Center, Kerman University of Medical Sciences, Kerman, Iran;2. Department of Community Health Nursing, School of Nursing and Midwifery, Kerman University of Medical Sciences, Kerman, Iran;3. Department of Medical Surgical Nursing, School of Nursing and Midwifery, Kerman University of Medical Sciences, Kerman, Iran;4. Immunology of Infectious Diseases Research Center, Rafsanjan University of Medical Sciences, Rafsanjan, Iran;1. Neuroscience Graduate Program, Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157-1040, USA;2. Department of Physiology & Pharmacology, Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157-1040, USA;3. Department of Pathology (Comparative Medicine), Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157-1040, USA |
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| Abstract: | Increased plasma levels of S100 proteins and interaction of S100 proteins with receptor for advanced glycation end products (RAGE) have been associated with a number of disease states, including chronic inflammatory processes and atherosclerosis. However, data concerning the role of circulating S100 proteins in these pathologies in vivo are scarce and, furthermore, it is currently not known whether RAGE is the sole receptor for extracellular S100 proteins in vivo. We report a novel methodology using recombinant human S100 proteins radiolabelled with fluorine-18, particularly, 18F-S100A12, in receptor binding studies and cellular association studies in vitro, and in dynamic small animal positron emission tomography (PET) studies in rats in vivo. Association to both human aortic endothelial cells and macrophages revealed specific binding of 18F-S100A12 to RAGE, but, furthermore, provides evidence for interaction of 18F-S100A12 to various scavenger receptors (SR). PET data showed temporary association of 18F-S100A12 with tissues overexpressing RAGE (e.g., lung), and, moreover, accumulation of 18F-S100A12 in tissues enriched in cells overexpressing SR (e.g., liver and spleen). Blockade of overall SR interaction by maleylated BSA (malBSA) clearly shows diminished in vivo association of 18F-S100A12 to these tissues as well as a significant increment of the mean plasma residence time of 18F-S100A12 (4.8 ± 0.4 h vs. 2.3 ± 0.3 h). The present approach first demonstrates that besides RAGE also scavenger receptors contribute to distribution, tissue association and elimination of circulating proinflammatory S100A12. |
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