Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent
Laboratory studyOther animals
- Design
- Laboratory study
- Subjects
- not applicable (cell-free glycation assays)
- Dose used in the study
- not stated in abstract
- Duration
- not stated in abstract
- What was measured
- Non-enzymatic glycation of carnosine by glucose, galactose, deoxyribose and dihydroxyacetone; glycation of an acetyl-Lys-His-amide peptide; glycation and cross-linking of alpha-crystallin, superoxide dismutase and catalase by several sugars; mutagenicity of glycated carnosine.
What the authors reported
The authors report that carnosine was readily glycated when incubated with glucose, galactose, deoxyribose and dihydroxyacetone. Carnosine inhibited glycation of an acetyl-Lys-His-amide peptide by dihydroxyacetone, and protected alpha-crystallin, superoxide dismutase and catalase from glycation and cross-linking caused by ribose, deoxyribose, dihydroxyacetone, dihydroxyacetone phosphate and fructose. Glycated carnosine was non-mutagenic, unlike some other glycated amino acids.
Limits of this study
Cell-free biochemical experiments; the authors discuss possible biological and therapeutic significance but did not test it. The journal is FEBS Letters, not Biochemical and Biophysical Research Communications as sometimes cited. Full text not read.
Source
PubMed 7664889 · doi:10.1016/0014-5793(95)00849-5
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.