Advanced glycation end products and diabetic complications

• Published in: The Korean journal of physiology & pharmacology Vol. 18; no. 1; pp. 1 - 14
• Main Authors: Singh, Varun Parkash, Bali, Anjana, Singh, Nirmal, Jaggi, Amteshwar Singh
• Format: Journal Article
• Language: English
• Published: Korea (South) The Korean Physiological Society and The Korean Society of Pharmacology 01.02.2014; 대한약리학회
• Subjects: Review; 약리학; Oxidative stress; Diabetic complications; Advanced glycation end-products; Plasma proteins; Inflammation
• ISSN: 1226-4512; 2093-3827
• DOI: 10.4196/kjpp.2014.18.1.1

During long standing hyperglycaemic state in diabetes mellitus, glucose forms covalent adducts with the plasma proteins through a non-enzymatic process known as glycation. Protein glycation and formation of advanced glycation end products (AGEs) play an important role in the pathogenesis of diabetic complications like retinopathy, nephropathy, neuropathy, cardiomyopathy along with some other diseases such as rheumatoid arthritis, osteoporosis and aging. Glycation of proteins interferes with their normal functions by disrupting molecular conformation, altering enzymatic activity, and interfering with receptor functioning. AGEs form intra- and extracellular cross linking not only with proteins, but with some other endogenous key molecules including lipids and nucleic acids to contribute in the development of diabetic complications. Recent studies suggest that AGEs interact with plasma membrane localized receptors for AGEs (RAGE) to alter intracellular signaling, gene expression, release of pro-inflammatory molecules and free radicals. The present review discusses the glycation of plasma proteins such as albumin, fibrinogen, globulins and collagen to form different types of AGEs. Furthermore, the role of AGEs in the pathogenesis of diabetic complications including retinopathy, cataract, neuropathy, nephropathy and cardiomyopathy is also discussed.