Ann Dermatol.  2017 Aug;29(4):508-511. 10.5021/ad.2017.29.4.508.

Glyceraldehyde-Derived Advanced Glycation End Products Accumulate Faster Than N(ε)-(Carboxymethyl) Lysine

Affiliations
  • 1Laboratory of Dermatological Physiology, Faculty of Pharmaceutical Sciences, Josai University, Saitama, Japan. tokudome@josai.ac.jp
  • 2School of Bioscience and Biotechnology, Tokyo University of Technology, Tokyo, Japan.
  • 3Department of Advanced Medicine, Medical Research Institute, Kanazawa Medical University, Ishikawa, Japan.

Abstract

No abstract available.


MeSH Terms

Glycosylation End Products, Advanced*
Lysine*
Glycosylation End Products, Advanced
Lysine

Figure

  • Fig. 1 Glyceraldehyde-derived advanced glycation end products (Glycer-AGEs) in sections of human skin from the abdominal area of individuals 28 and 63 years of age following immunohistochemical staining with anti-Glycer-AGEs antibody. Pretreatment with a blocking peptide resulted in significant loss of signal. Lower panels are shown with nuclear counterstaining. Bar=100 µm.

  • Fig. 2 (A) Macroscopic view of hairless mouse skin glycated using glyoxal (GO) or glyceraldehyde (GA). Rate of increase in advanced glycation end product (AGE) formation indicated by fluorescence intensity (excitation: 365 nm/emission: 450 nm) and b* value. Glycation induced by 50 mM of GO: ○, or GA: ▲. (B) Macroscopic view of glycated amino acids before hydrolysis (6 h) and after hydrolysis (6, 12, 24 h). Rate of modification of Lys as determined by amino acid analysis.


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