Albumin competitively inhibits glycation of less abundant proteins

Protein Pept Lett. 2008;15(7):663-7. doi: 10.2174/092986608785133690.

Abstract

Glycation, a non-enzymatic reaction between glucose and protein is the primary cause of diabetic complications. Albumin, the most abundant plasma protein undergoes glycation both in vivo and in vitro. The influence of albumin on glycation of less abundant proteins has not been addressed. For the first time, we show that albumin competitively inhibits the glycation of less abundant proteins. This study suggests that at least in the initial stages of diabetes, albumin may protect other proteins from glycation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoproteins / chemistry
  • Apoproteins / metabolism
  • Binding, Competitive
  • Carbonic Anhydrases / metabolism
  • Diabetes Complications / metabolism
  • Glycation End Products, Advanced / chemistry
  • Glycation End Products, Advanced / metabolism
  • Glycosylation
  • Humans
  • In Vitro Techniques
  • Insulin / chemistry
  • Insulin / metabolism
  • Kinetics
  • Myoglobin / chemistry
  • Myoglobin / metabolism
  • Papain / metabolism
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Serum Albumin / chemistry*
  • Serum Albumin / metabolism*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Apoproteins
  • Glycation End Products, Advanced
  • Insulin
  • Myoglobin
  • Proteins
  • Serum Albumin
  • apomyoglobin
  • Papain
  • Carbonic Anhydrases