GSBS Student Publications

Title

Non-enzymatic interactions of glyoxylate with lysine, arginine, and glucosamine: a study of advanced non-enzymatic glycation like compounds

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Cancer Biology

Date

9-15-2006

Document Type

Article

Medical Subject Headings

Arginine; Chromatography, High Pressure Liquid; Electrophoresis, Capillary; Fructose; Glucosamine; Glucose; Glyceraldehyde; Glycosylation End Products, Advanced; Glyoxylates; Lysine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Glyoxylate is a 2 carbon aldo acid that is formed in hepatic tissue from glycolate. Once formed, the molecule can be converted to glycine by alanine-glyoxylate aminotransferase (AGAT). In defects of AGAT, glyoxylate is transformed to oxalate, resulting in high levels of oxalate in the body. The objective of this study was 2-fold. First, it was to determine, if akin to D-glucose, D-fructose or DL-glyceraldehyde, glyoxylate was susceptible to non-enzymatic attack by amino containing molecules such as lysine, arginine or glucosamine. Second, if by virtue of its molecular structure and size, glyoxylate was as reactive a reagent in non-enzymatic reactions as DL-glyceraldehyde; i.e., a glycose that we previously demonstrated to be a more effective glycating agent than D-glucose or D-fructose. Using capillary electrophoresis (CE), high performance liquid chromatography and UV and fluorescence spectroscopy, glyoxylate was found to be a highly reactive precursor of advanced glycation like end products (AGLEs) and a more effective promoter of non-enzymatic end products than D-glucose, D-fructose or DL-glyceraldehyde.

Rights and Permissions

Citation: Bioorg Chem. 2007 Feb;35(1):11-24. Epub 2006 Sep 12. Link to article on publisher's site

Related Resources

Link to Article in PubMed

Journal Title

Bioorganic chemistry

PubMed ID

16970975