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- Title
The serum concentration of the advanced glycation end-product N<sup><em>ε</em></sup>-(carboxymethyl)lysine is increased in uremia.
- Authors
Degenhardt, Thorsten P.; Grass, Linda; Reddy, Sharanya; Thorpe, Suzanne R.; Diamandis, Eleftherios P.; Baynes, John W.
- Abstract
Advanced glycation end products (AGEs) such as pentosidine and N4 -(carboxymethyl)lysine (CML) have been traditionally quantified by HPLC or gas chromatography mass spectrometry (GC/MS). Enzyme-inked immunosorbent assays (ELISA) have been introduced as a convenient alternative to simplify the detection and measurement of AGEs in proteins and tissues, but sonic of these studies are limited by the lack of information on the structure of the epitopes recognized by antibodies to AGE-proteins. In this work we demonstrate that an antibody used in a previous study, reporting increased levels of AGEs in patients with diabetes or on continuous ambulator peritoneal dialysis (CAPD) and hemodialysis (HD) recognizes CML as its major epitope. We also show that there is a significant correlation between the concentration of AGEs in serum measured by ELISA and a GC/MS assay for CML in serum proteins. Both analyses, yielded comparable resubs. with patients on CAPD and HD having about threefold higher AGES or CML-concentrations in their serum. Our' data suggest that ELISA assays for `CML should be useful for the clinical measurement of AGEs in serum proteins.
- Subjects
CARBOHYDRATE intolerance; HEMODIALYSIS; IMMUNOGLOBULINS; THERAPEUTICS; AMINO acids; PEOPLE with diabetes
- Publication
Kidney International, 1997, Vol 52, Issue 4, p1064
- ISSN
0085-2538
- Publication type
Article
- DOI
10.1038/ki.1997.429