Rutin derivatives as potent AGE inhibitors and its relevance in diabetes complications

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AudienciaPúblico en generales_ES
CoberturaMéxicoes_ES
Fecha de ingreso2026-09-15T00:31:52Z
Fecha de publicación2007-01-01
ResumenGlycation is a reversible, non‐enzymatic reaction between reducing sugars and amino groups of proteins that undergo rearrangements to stable ketoamines, which lead to the formation of advanced glycation end products (AGEs) such as fluorescent and non‐fluorescent ( N ε ‐ carboxymethyllysine, CML) protein adducts and protein crosslinks. Protein glycation, induced by hyperglycemia, has been implicated in the appearance of diabetic complications that involved kidney, eye and neuronal tissue damage. When aminoguanidine, a proven AGEs inhibitor, was tested as an anti‐diabetic drug in human clinical trials presented important side effects and this suggested a need for new and improved AGEs inhibitors. Histone H1 and ADP‐ribose were used as a model for protein glycation since it allow us to distinguish true AGE inhibitors from general antioxidants. Rutin derivatives were tested as AGEs inhibitors since rutin, a common dietary flavonoid that is consumed in fruits, vegetables and plant derived beverages, is not absorbed intact due to gut microflora degradation. Our data showed that 3,4‐dihydroxyphenylacetic acid and homovanillic acid were as powerful inhibitors of fluorescence, crosslinks and the formation of CML protein adducts as aminoguanidine. These results suggest effective natural product AGE inhibitors that might potentially be recommended as dietary supplements in diabetes complication prevention.es_ES
Doihttps://doi.org/10.1096/fasebj.21.5.a633-aes_ES
URIhttps://riuat.uat.edu.mx/handle/123456789/3608
Idiomaenes_ES
EditorialWileyes_ES
RelaciónThe FASEB Journales_ES
URL relacionadohttps://doi.org/10.1096/fasebj.21.5.a633-aes_ES
DerechosAcceso restringido / Suscripción (Metadatos de producción científica)es_ES
Licenciahttp://purl.org/coar/access_right/c_16eces_ES
FuenteThe FASEB Journal
TítuloRutin derivatives as potent AGE inhibitors and its relevance in diabetes complicationses_ES
TipoArtículoes_ES
ArbitradoHa sido Arbitradoes_ES
AutorLaurean, Daniel Cervantes
AutorPashikanti, Srinath
AutorLaurean, Daniel Cervanteses_ES
AutorPashikanti, Srinathes_ES
InstituciónUniversidad Autónoma de Tamaulipas
InstituciónUniversidad Autónoma de Tamaulipases_ES
Número5es_ES
URL relacionadahttps://doi.org/10.1096/fasebj.21.5.a633-a
Tipo de artículoIndexado
Tipo de artículoIndexadoes_ES
Volumen21es_ES

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