Molecular susceptibility to glycation and its implication in diabetes mellitus and related diseases

José D. Méndez, Jianling Xie, Montserrat Aguilar-Hernández, Verna Méndez-Valenzuela

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28 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)185-193
Number of pages9
JournalMolecular and Cellular Biochemistry
Issue number1-2
Publication statusPublished or Issued - Nov 2010
Externally publishedYes


  • Advanced glycation end products
  • Chronic complications
  • Diabetes mellitus
  • Hyperglycemia
  • Lipids
  • Nucleic acids
  • Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

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