Hemoglobin-AGE: A Circulating Marker of Advanced Glycosylation

Advanced glycosylation end products (AGEs) form spontaneously from glucose-derived Amadori products and accumulate on long-lived tissue proteins. AGEs have been implicated in the pathogenesis of several of the complications of aging and diabetes, including atherosclerosis and renal disease. With the...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1992-10, Vol.258 (5082), p.651-653
Hauptverfasser: Makita, Zenji, Vlassara, Helen, Rayfield, Elliot, Cartwright, Kenneth, Friedman, Eli, Rodby, Roger, Cerami, Anthony, Bucala, Richard
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Sprache:eng
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Zusammenfassung:Advanced glycosylation end products (AGEs) form spontaneously from glucose-derived Amadori products and accumulate on long-lived tissue proteins. AGEs have been implicated in the pathogenesis of several of the complications of aging and diabetes, including atherosclerosis and renal disease. With the use of recently developed AGE-specific antibodies, an AGE-modified form of human hemoglobin has been identified. Termed hemoglobin-AGE (Hb-AGE), this modified species accounts for 0.42 percent of circulating hemoglobin in normal individuals but increases to 0.75 percent in patients with diabetes-induced hyperglycemia. In a group of diabetic patients treated with the advanced glycosylation inhibitor aminoguanidine, Hb-AGE levels decreased significantly over a 1-month period. Hemoglobin-AGE measurements may provide an index of long-term tissue modification by AGEs and prove useful in assessing the contribution of advanced glycosylation to a variety of diabetic and age-related complications.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1411574