Lipid glycation and protein glycation in diabetes and atherosclerosis

Teruo Miyazawa, Kiyotaka Nakagawa, Satoko Shimasaki, Ryoji Nagai

Research output: Contribution to journalReview articlepeer-review

80 Citations (Scopus)


Recent instrumental analyses using a hybrid quadrupole/linear ion trap spectrometer in LC-MS/MS have demonstrated that the Maillard reaction progresses not only on proteins but also on amino residues of membrane lipids such as phosphatidylethanolamine (PE), thus forming Amadori- PE (deoxy-D-fructosyl PE) as the principal products. The plasma Amadori-PE level is 0.08 mol% of the total PE in healthy subjects and 0.15-0.29 mol% in diabetic patients. Pyridoxal 5'-phosphate and pyridoxal are the most effective lipid glycation inhibitors, and the PE-pyridoxal 50-phosphate adduct is detectable in human red blood cells. These findings are beneficial for developing a potential clinical marker for glycemic control as well as potential compounds to prevent the pathogenesis of diabetic complications and atherosclerosis. Glucose and other aldehydes, such as glyoxal, methylglyoxal, and glycolaldehyde, react with the amino residues of proteins to form Amadori products and Heynes rearrangement products. Because several advanced glycation end-product (AGE) inhibitors such as pyridoxamine and benfotiamine inhibit the development of retinopathy and neuropathy in streptozotocin (STZ)-induced diabetic rats, AGEs may play a role in the development of diabetic complications. In the present review, we describe the recent progress and future applications of the Maillard reaction research regarding lipid and protein modifications in diabetes and atherosclerosis.

Original languageEnglish
Pages (from-to)1163-1170
Number of pages8
JournalAmino Acids
Issue number4
Publication statusPublished - 2012 Apr


  • AGE
  • Aldehydes
  • Atherosclerosis
  • Diabetes
  • Lipid glycation
  • Protein glycation

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry


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