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Papers In Press, published online ahead of print December 1, 2002
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Department of Microbiology and Immunology, Medical University of South Carolina, Charleston, SC 29425
Corresponding Author: virellag{at}musc.edu
Advanced glycosylation end-products (AGE) accumulate in tissues with advancing age, diabetes mellitus, and end-stage renal disease. AGE-LDL and other AGE products are believed to play a significant role in the development vascular complications in diabetic patients. One of the potentially pathogenic consequences of LDL modification by AGE is its immunogenicity. The goal of this study was to isolate and characterize human AGE-LDL antibodies and to identify the modifications recognized by the isolated antibodies. The AGE-LDL preparation used for this purpose contained primarily the AGE Ne(carboxymethyl)lysine (CML, 14.6 mmol/mol lysine), and smaller amounts of the AGE Ne(carboxyethyl)lysine (CEL, 2.7 mmol/mol lysine). AGE-LDL antibodies isolated from the sera of 7 patients with type 1 diabetes contained predominantly IgG, of subclasses 1 and 3, considered pro-inflammatory because of their ability to interact with all types of human FcgR receptors and to activate the complement system. We determined average dissociation constants (Kd) for the purified antibodies. The Kd values (4.76±2.52x10-9, ranging from 7.6 x 10-10 to 8.1 x 10-9 mol/L) indicated that AGE-LDL antibodies are of higher avidity than oxLDL antibodies measured previously (Kd = 1.53±07x10-8 ml/L), but of lower avidity than rabbit polyclonal LDL antibodies (Kd=9.34x10-11). Analysis of the apolipoprotein B-rich lipoproteins isolated with polyethylene glycol-precipitated antigen-antibody complexes from the same patients showed the presence of both CML and CEL, thus confirming that these two modifications are recognized by human autoantibodies. A comparative study of the reactivity of puri-fied AGE-LDL antibodies with CML-LDL and CML-serum albumin showed no reactivity with CML-albumin, proving that one other AGE-modified major serum protein does not share epitopes with CML-LDL.
Revised on November 7, 2002
Accepted on November 19, 2002
Autoimmune response to advanced glycosylation end-products of human low density lipoprotein
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