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Amino Acids

, Volume 48, Issue 7, pp 1631–1639 | Cite as

The glycation of fibronectin by glycolaldehyde and methylglyoxal as a model for aging in Bruch’s membrane

  • Mai T. Thao
  • Elizabeth R. GaillardEmail author
Original Article

Abstract

The purpose of the study is to identify the sites of modification when fibronectin reacts with glycolaldehyde or methylglyoxal as a model system for aging of Bruch’s membrane. A synthetic peptide consisting of the α5β1 integrin binding region of fibronectin was incubated with glycolaldehyde for 12 h or with methylglyoxal for 1 h at 37 °C. After tryptic digestion, the samples were analyzed with liquid chromatography–mass spectrometry (LC/MS). Tandem MS was used to determine the sites of modification. The adducts, aldoamine and N ε-carboxymethyl-lysine, attached preferably at lysine residues when the fibronectin peptide reacted with glycolaldehyde. When the fibronectin peptide reacted with methylglyoxal, modifications occurred at lysine and arginine residues. At lysine residues, N ε-carboxyethyl-lysine adducts were present. At arginine residues, hydroimidazolone and tetrapyrimidine adducts were present. Several advanced glycation endproducts were generated when fibronectin was glycated via glycolaldehyde and methylglyoxal. These results can help explain the structural changes Bruch’s membrane undergoes during aging.

Keywords

Bruch’s membrane Fibronectin Retinal pigment epithelium Glycation Aging 

Notes

Compliance with ethical standards

Conflict of interests

The authors do not have competing interests and/or commercial relationships.

The work reported here does not invovle human participants or animal subjects.

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Copyright information

© Springer-Verlag Wien 2016

Authors and Affiliations

  1. 1.Department of Chemistry and BiochemistryNorthern Illinois UniversityDeKalbUSA
  2. 2.Department of Biological SciencesNorthern Illinois UniversityDeKalbUSA

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