A receptor-based bioadsorbent to target advanced glycation end products in chronic kidney disease

Artificial Organs

Volumn 38, Issue 6, 2014, Pages 474-483

  Zhang, Yangrong ^a   Lapidos, Karen A ^a   Gal Moscovici, Anca ^b,f   Sprague, Stuart M ^b,d   Ameer, Guillermo A ^a,c,e  

^a Northwestern University   (United States)

^b NORTHSHORE UNIVERSITY HEALTHSYSTEM   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

^d UNIVERSITY OF CHICAGO   (United States)

^e NORTHWESTERN UNIVERSITY   (United States)

^f HADASSAH HEBREW UNIVERSITY MEDICAL CENTER   (Israel)

Author keywords

Advanced glycation end products; End stage renal disease; Extracorporeal; Hollow fiber device; Inflammation; Receptor for advanced glycation end products

Indexed keywords

BLOOD; CELL ADHESION; ENDOTHELIAL CELLS; GLYCOSYLATION;

ADVANCED GLYCATION END PRODUCTS; BIOADSORBENT; CHRONIC KIDNEY DISEASE; END-STAGE RENAL DISEASE; EXTRACORPOREAL; FIBER DEVICES; HOLLOW FIBER; HOLLOW FIBER DEVICE; RECEPTOR FOR ADVANCED GLYCATION END PRODUCT;

PATHOLOGY;

ADSORBENT; ADVANCED GLYCATION END PRODUCT; AGAROSE; BOVINE SERUM ALBUMIN; RECEPTOR; SODIUM CHLORIDE; VASCULAR CELL ADHESION MOLECULE 1; ADVANCED GLYCATION END PRODUCTS-BOVINE SERUM ALBUMIN; ADVANCED GLYCOSYLATION END-PRODUCT RECEPTOR; BIOLOGICAL MARKER; IMMUNOGLOBULIN RECEPTOR; POLYMER; POLYSULFONE P 1700; PROTEIN BINDING; SEPHAROSE; SULFONE;

ALBUMIN BLOOD LEVEL; ARTICLE; BINDING AFFINITY; BLOOD; CHRONIC KIDNEY DISEASE; CONCENTRATION (PARAMETERS); DIABETES MELLITUS; FREEZE DRYING; GENERAL DEVICE; HOLLOW FIBER DEVICE; HUMAN; HUMAN CELL; INFLAMMATION; KIDNEY FAILURE; LABORATORY DEVICE; OSTEOCLAST; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; RECEPTOR BINDING; SERUM; STEM CELL; ADSORPTION; ANIMAL; CELL LINE; DETOXIFICATION; DEVICES; DOWN REGULATION; EQUIPMENT DESIGN; EXTRACORPOREAL CIRCULATION; FEASIBILITY STUDY; KIDNEY FAILURE, CHRONIC; METABOLISM; MOUSE; PROCEDURES; TIME; UMBILICAL VEIN ENDOTHELIAL CELL;

BOVINAE;

ADSORPTION; ANIMALS; BIOLOGICAL MARKERS; CELL LINE; DOWN-REGULATION; EQUIPMENT DESIGN; EXTRACORPOREAL CIRCULATION; FEASIBILITY STUDIES; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMAN UMBILICAL VEIN ENDOTHELIAL CELLS; HUMANS; KIDNEY FAILURE, CHRONIC; MICE; OSTEOCLASTS; POLYMERS; PROTEIN BINDING; RECEPTORS, IMMUNOLOGIC; SEPHAROSE; SERUM ALBUMIN, BOVINE; SORPTION DETOXIFICATION; SULFONES; TIME FACTORS; VASCULAR CELL ADHESION MOLECULE-1;

EID: 84901934234     PISSN: 0160564X     EISSN: 15251594     Source Type: Journal    
DOI: 10.1111/aor.12203     Document Type: Article

References (30)

1. Busch M, Franke S, Rüster C, Wolf G. Advanced glycation end-products and the kidney. Eur J Clin Invest 2010;40:742-755.
2. Kilhovd BK, Juutilainen A, Lehto S, etal. Increased serum levels of advanced glycation endproducts predict total, cardiovascular and coronary mortality in women with type 2 diabetes: a population-based 18 year follow-up study. Diabetologia 2007;50:1409-1417.
3. Nin JW, Jorsal A, Ferreira I, etal. Higher plasma levels of advanced glycation end products are associated with incident cardiovascular disease and all-cause mortality in type 1 diabetes: a 12-year follow-up study. Diabetes Care 2011;34:442-447.
4. United States Renal Data System. Annual data report: atlas of chronic kidney disease and end-stage renal disease. Bethesda, MD: National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases, 2009.
5. Meerwaldt R, Zeebregts CJ, Navis G, Hillebrands JL, Lefrandt JD, Smit AJ. Accumulation of advanced glycation end products and chronic complications in ESRD treated by dialysis. Am J Kidney Dis 2009;53:138-150.
6. Schmidt AM, Vianna M, Gerlach M, etal. Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface. J Biol Chem 1992;267:14987-14997.
7. Kislinger T, Fu C, Huber B, etal. N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J Biol Chem 1999;274:31740-31749.
8. Yan S, Ramasamy R, Schmidt A. Receptor for AGE (RAGE) and its ligands-cast into leading roles in diabetes and the inflammatory response. J Mol Med 2009;87:235-247.
9. Bierhaus A, Nawroth P. Multiple levels of regulation determine the role of the receptor for AGE (RAGE) as common soil in inflammation, immune responses and diabetes mellitus and its complications. Diabetologia 2009;52:2251-2263.
10. Engelen L, Stehouwer CD, Schalkwijk CG. Current therapeutic interventions in the glycation pathway: evidence from clinical studies. Diabetes Obes Metab 2013;15:677-689.
11. Wendt T, Harja E, Bucciarelli L, etal. RAGE modulates vascular inflammation and atherosclerosis in a murine model of type 2 diabetes. Atherosclerosis 2006;185:70-77.
12. Ekong U, Zeng S, Dun H, etal. Blockade of the receptor for advanced glycation end products attenuates acetaminophen-induced hepatotoxicity in mice. J Gastroenterol Hepatol 2006;21:682-688.
13. Mitsuhashi T, Li YM, Fishbane S, Vlassara H. Depletion of reactive advanced glycation endproducts from diabetic uremic sera using a lysozyme-linked matrix. J Clin Invest 1997;100:847-854.
14. Wilton R, Yousef MA, Saxena P, Szpunar M, Stevens FJ. Expression and purification of recombinant human receptor for advanced glycation endproducts in Escherichia coli. Protein Expr Purif 2006;47:25-35.
15. Reichelt P, Schwarz C, Donzeau M. Single step protocol to purify recombinant proteins with low endotoxin contents. Protein Expr Purif 2006;46:483-488.
16. Ameer GA, Grovender EA, Ploegh H, etal. A novel immunoadsorption device for removing [bgr]2-microglobulin from whole blood. Kidney Int 2001;59:1544-1550.
17. Daniels CM, Woolverton EM, Sprague SM, Ameer GA. Assessment of the stability of an immunoadsorbent for the extracorporeal removal of beta-2-microglobulin from blood. Blood Purif 2005;23:287-297.
18. Grovender EA, Cooney CL, Langer R. Immunoadsorption model for a novel fluidized-bed blood detoxification device. AIChE J 2002;48:2357-2365.
19. Menaa C, Reddy SV, Kurihara N, etal. Enhanced RANK ligand expression and responsivity of bone marrow cells in Paget's disease of bone. J Clin Invest 2000;105:1833-1838.
20. Takeuchi M, Yamagishi S. TAGE (toxic AGEs) hypothesis in various chronic diseases. Med Hypotheses 2004;63:449-452.
21. Miyata T, Kawai R, Taketomi S, Sprague SM. Possible involvement of advanced glycation end-products in bone resorption. Nephrol Dial Transplant 1996;11(Suppl. 5):54-57.
22. Penfold SA, Coughlan MT, Patel SK, etal. Circulating high-molecular-weight RAGE ligands activate pathways implicated in the development of diabetic nephropathy. Kidney Int 2010;78:287-295.
23. Ameer GA, Harmon W, Sasisekharan R, Langer R. Investigation of a whole blood fluidized bed Taylor-Couette flow device for enzymatic heparin neutralization. Biotechnol Bioeng 1999;62:602-608.
24. Valencia JV, Weldon SC, Quinn D, etal. Advanced glycation end product ligands for the receptor for advanced glycation end products: biochemical characterization and formation kinetics. Anal Biochem 2004;324:68-78.
25. Holmes CJ. Hemodialyzer performance: biological indices. Artif Organs 1995;19:1126-1135.
26. Fowers KD, Janatova J. Specific inhibition of C3 to facilitate general complement inhibition on endotoxin affinity sorbents for apheresis applications. Biomaterials 2001;22:1749-1761.
27. Ikeda K, Higashi T, Sano H, etal. Nε-(Carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. Biochemistry 1996;35:8075-8083.
28. Williams ME. New therapies for advanced glycation end product nephrotoxicity: current challenges. Am J Kidney Dis 2003;41:S42-47.
29. Semba RD, Fink JC, Sun K, Windham BG, Ferrucci L. Serum carboxymethyl-lysine, a dominant advanced glycation end product, is associated with chronic kidney disease: the Baltimore longitudinal study of aging. J Ren Nutr 2010;20:74-81.
30. Takeuchi M, Yamagishi S. Possible involvement of advanced glycation end-products (AGEs) in the pathogenesis of Alzheimer's disease. Curr Pharm Des 2008;14:973-978.