Evidence that pioglitazone, metformin and pentoxifylline are inhibitors of glycation

Enhanced formation and accumulation of advanced glycation end products (AGEs) have been proposed to play a major role in the pathogenesis of diabetic complications, and atherosclerosis, leading to the development of a range of diabetic complications including nephropathy, retinopathy and neuropathy....

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Bibliographic Details
Published in:Clinica chimica acta 2000-11, Vol.301 (1), p.65-77
Main Authors: Rahbar, Samuel, Natarajan, Rama, Yerneni, KiranKumar, Scott, Stephen, Gonzales, Noe, Nadler, Jerry L
Format: Article
Language:English
Subjects:
AGEs
Biological and medical sciences
Enzyme-Linked Immunosorbent Assay
Glycated Hemoglobin A - analysis
Glycation
Glycation End Products, Advanced - antagonists & inhibitors
Glycation inhibitors
Hormones. Endocrine system
Humans
Hypoglycemic Agents - pharmacology
Medical sciences
Metformin
Metformin - pharmacology
Pentoxifylline
Pentoxifylline - pharmacology
Pharmacology. Drug treatments
Pioglitazone
Thiazoles - pharmacology
Thiazolidinediones
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Summary:Enhanced formation and accumulation of advanced glycation end products (AGEs) have been proposed to play a major role in the pathogenesis of diabetic complications, and atherosclerosis, leading to the development of a range of diabetic complications including nephropathy, retinopathy and neuropathy. Several potential drug candidates as AGE inhibitors have been reported recently. Aminoguanidine is the first drug extensively studied. However, there are no currently available medications known to block AGE formation. We have previously reported a number of novel and structurally diverse compounds as potent inhibitors of glycation and AGE formation. We have now studied several of the existing drugs, which are in therapeutic practice for lowering blood sugar or the treatment of peripheral vascular disease in diabetic patients, for possible inhibitory effects on glycation. We show that that three compounds; pioglitazone, metformin and pentoxifylline are also inhibitors of glycation.
ISSN:0009-8981
1873-3492
DOI:10.1016/S0009-8981(00)00327-2