Molecular susceptibility to glycation and its implication in diabetes mellitus and related diseases.
The modification of free amino groups on proteins, lipids, and nucleic acids by non-enzymatic glycosylation produce a variety of complex structures named advanced glycation end products (AGEs). Glycation of these molecules participate in the development of diabetic complications and related diseases. Diabetes mellitus is characterized by short-term metabolic changes in lipid and protein metabolism, and long-term irreversible changes in vascular and connective tissue. AGEs are directly implicated in the development of chronic complications in diabetes such as nephropathy, rethinopathy, neuropathy, and other related diseases such as atherosclerosis, heart disease, stroke, and peripheral vascular disease. In this review, we aim to explain how glycation occurs in different molecules and what the pathological consequence of AGE formation in diabetes mellitus and other diseases are.
Méndez
José D
JD
Medical Research Unit in Metabolic Diseases, National Medical Center, Mexican Institute of Social Security, Mexico, DF, Mexico. mendezf@servidor.unam.mx
Xie
Jianling
J
Aguilar-Hernández
Montserrat
M
Méndez-Valenzuela
Verna
V
D048909:Diabetes Complications / Q000378:metabolism; D003920:Diabetes Mellitus / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D006801:Humans
D005947:Glucose