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Amadori-glycated human serum albumin is a chemically modified form of the most abundant plasma protein, resulting from the non-enzymatic attachment of glucose to albumin's lysine and arginine residues. This modification produces a stable ketoamine intermediate known as an Amadori product, which serves as a key clinical biomarker for intermediate-term glycemic control in diabetic patients (Roohk & Zaidi, 2008). Unlike hemoglobin A1c, glycated albumin reflects glucose fluctuations over a shorter period of approximately two to three weeks and is not affected by red blood cell lifespan. Beyond its diagnostic utility, Amadori-glycated albumin plays a pathogenic role by promoting oxidative stress and inflammation through its interaction with the Receptor for Advanced Glycation End-products (RAGE) (Cohen, 2003). It also serves as a precursor to irreversible advanced glycation end-products (AGEs), which are central to the progression of diabetic complications such as nephropathy, retinopathy, and cardiovascular disease (Anguizola et al., 2013). Pharmacological interventions aim to inhibit the formation of these Amadori products or block their conversion into toxic AGEs to mitigate tissue damage.
Inhibition of the conversion of Amadori products to advanced glycation end-products (AGEs); scavenging of reactive carbonyl species; reduction of oxidative stress; blocking of RAGE activation.
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