Horm Metab Res 1993; 25(5): 250-252
DOI: 10.1055/s-2007-1002089
Originals Basic

© Georg Thieme Verlag, Stuttgart · New York

In-Vitro Carboxymethylation of Low Density Lipoprotein Alters its Metabolism Via the High-Affinity Receptor

K. E. Gempel, K. D. Gerbitz, B. Olgemöller, E. D. Schleicher
  • Institute für klinische Chemie und Diabetesforschung, Städt. Krankenhaus Schwabing, München, Germany
Further Information

Publication History

1992

1992

Publication Date:
14 March 2008 (online)

Summary

Carboxymethylation of lysine residues has been shown to result from oxidation of glycated proteins in vivo and in vitro leading to an augmentation of proteins' net negative charge. The metabolism of carboxymethylated low density lipoprotein (LDL) was studied in cultured human fibroblasts and mouse peritoneal macrophages. In vitro Carboxymethylation was achieved by incubation of LDL with glyoxylic acid in the presence of Na(CN)BH3. Carboxymethylation inhibited metabolism of LDL via the high affinity receptor in fibroblasts as did methylation. The uptake of LDL into mouse peritoneal macrophages via the scavenger receptor, which was stimulated by acetylation, was not affected.