Rapid clearance of serum amyloid a from high-density lipoproteins |
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| Affiliation: | 1. Brown University Program-in-Medicine, Department of Medicine, The Miriam Hospital, 164 Summit Avenue, Providence, RI, 02906 U.S.A.;2. Harvard Medical School, The New England Regional Primate Research Center, Southborough, MA 01772 U.S.A.;1. Jiangsu Collaborative Innovation Center for Biological Functional Materials, College of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210023, China;2. Jiangsu Key Laboratory of Biofunctional Materials, Jiangsu Engineering Research Center for Biomedical Function Materials, Nanjing 210023, China;3. Nanjing Zhou Ninglin Advanced Materials Technology Company Limited, Nanjing 211505, China;1. Thrombosis and Hemostasis Program, Versiti Blood Research Institute, Milwaukee, WI, USA;2. Department of Physiology, Medical College of Wisconsin, Milwaukee, WI, USA;3. Department of Pediatrics, Medical College of Wisconsin, Milwaukee, WI, USA;4. Division of Pediatric Cardiology, The Herma Heart Institute, Children’s Wisconsin, Milwaukee, WI, USA;5. Department of Cell Biology, Neurobiology, and Anatomy, Medical College of Wisconsin, Milwaukee, WI, USA;1. Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong 2522, Australia;2. School of Biological Sciences, University of Wollongong, Wollongong 2522, Australia;2. Veterinary Laboratory, Guangzhou Zoo, Guangzhou 510642, PR China;3. College of Animal Science, South China Agricultural University, Guangzhou 510642, PR China |
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| Abstract: | The serum amyloid A proteins (SAA) occur in plasma in six polymorphic forms that are associated with the high-density lipoproteins (HDL). We studied two of the SAA proteins, SAA1 and SAA4, which have the same amino- and carboxy-terminal residues but different solution properties and electrophoretic mobilities, to determine whether they are interconverted in plasma in vivo. They were radioiodinated in vitro, incorporated into HDL, and administered to cynomolgus monkeys. Both remained associated with HDL for at least 6 h, had similar plasma die-away curves, and retained their characteristic electrophoretic mobilities, suggesting they are not related as precursor and product. The plasma clearance of the most prevalent SAA species, SAA4, was also simultaneously compared with the human A-I and C-III-2 apolipoproteins. Human apolipoprotein A-I decayed from plasma at a rate comparable to that of monkey HDL proteins. Apolipoprotein C-III-2 was cleared more rapidly and SAA4 at an even greater rate. These findings suggest that SAA are either dissociated from HDL before clearance from plasma or that SAA are contained in an HDL subspecies with metabolic fate different from that of most HDL particles. |
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