DETERMINATION OF ADVANCED GLYCATION END-PRODUCTS IN SERUM BY FLUORESCENCE SPECTROSCOPY AND COMPETITIVE ELISA

Citation
G. Munch et al., DETERMINATION OF ADVANCED GLYCATION END-PRODUCTS IN SERUM BY FLUORESCENCE SPECTROSCOPY AND COMPETITIVE ELISA, European journal of clinical chemistry and clinical biochemistry, 35(9), 1997, pp. 669-677
Citations number
34
Categorie Soggetti
Biology,"Medical Laboratory Technology
ISSN journal
09394974
Volume
35
Issue
9
Year of publication
1997
Pages
669 - 677
Database
ISI
SICI code
0939-4974(1997)35:9<669:DOAGEI>2.0.ZU;2-7
Abstract
Recent studies suggest that advanced glycation endproducts play an imp ortant role in cardiovascular complications of ageing, diabetes and en d-stage renal failure. Since highly elevated levels of advanced glycat ion endproducts are present in serum of patients on maintenance haemod ialysis, an accurate and rapid assay for their determination would be useful. This would be particularly valuable for monitoring the removal of advanced glycation endproducts by novel dialysis membranes, as wel l as the effect of new drugs for the inhibition of their formation. Me asurement of advanced glycation endproducts in serum was performed by two competitive ELISAs, using a monoclonal antibody directed against i midazolone, an advanced glycation endproduct formed by the reaction of arginine with 3-deoxyglucosone, and a polyclonal antibody directed ag ainst keyhole limpet haemocyanin-advanced glycation endproduct, as wel l as by quantitative fluorescence spectroscopy. Each of the assays sho wed significant differences between the controls and the maintenance h aemodialysis patients. Advanced glycation endproduct levels determined by each of the ELISAs correlated with total and protein-bound fluores cence, but not with each other, suggesting a variable distribution of advanced glycation endproducts on serum proteins among the maintenance haemodialysis patients.