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Arquivos de Medicina

versão On-line ISSN 2183-2447


CASTRO, Elisabete. The role of advanced glycosylation end products in diabetic nephropathy. Arq Med [online]. 2011, vol.25, n.1, pp.27-37. ISSN 2183-2447.

Diabetic nephropathy is the leading cause of chronic renal disease, affecting at present, about 15-25% of type 1 diabetics and 30-40% of type 2 diabetics. several decades of extensive research have clarified on the various pathogenic pathways implicated in the development of diabetic nephropathy. The advanced glycation end products (AGEs) are a heterogeneous group of proteins, lipids and nucleic acids to which glycidyl residues are covalently linked. The formation of AGEs is increased in situations of hyperglycemia and is also stimulated by oxidative stress. It appears that the activation of the renin-angiotensin system may contribute to the formation of AGEs through various mechanisms. besides being able to connect on a non-specific to basement membranes and modify their properties, the AGEs are also able to induce specific cellular responses to interact with their receptors. AGEs are involved in structural changes of progressive nephropathies inducing glomerulosclerosis, interstitial fibrosis and tubular atrophy. Thus, these effects contribute to the pathophysiology of most chronic renal disease, but more prominently for diabetic nephropathy. With this thesis we aim to provide an overview of the different pathways involved in the pathogenesis of diabetic nephropathy emphasizing the role of AGEs, with particular regard to the therapeutic perspectives that have been explored over the last decade, that focus on the formation and degradation of AGEs, as well as the interaction with their receptors. It is expected that over the next few years, some of these promising therapies are widely evaluated in clinical context, thereby helping to reduce the incidence of diabetic nephropathy and heavy medical and economic costs it entailed.

Palavras-chave : diabetic nephropathy; glycosylation end products, advanced; advanced glycosylation end-product receptor; therapeutics.

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