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...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 2010-11, Vol.344 (1-2), p.185-193
Main Authors: Méndez, José D, Xie, Jianling, Aguilar-Hernández, Montserrat, Méndez-Valenzuela, Verna
Format: Article
Language:English
Subjects:
Advanced glycation end products
Amino acids
Atherosclerosis
Biochemistry
Biomedical and Life Sciences
Cardiology
Cardiovascular diseases
Chronic complications
Diabetes
Diabetes Complications - metabolism
diabetes mellitus
Diabetes Mellitus - metabolism
Disease susceptibility
Enzymes
Glucose - metabolism
Glycosylation
Humans
Hyperglycemia
Life Sciences
Lipids
Medical Biochemistry
Molecular biology
Nucleic acids
Oncology
Physiological aspects
proteins
Vascular diseases
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Summary: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.
ISSN:0300-8177
1573-4919
DOI:10.1007/s11010-010-0541-3