Methylglyoxal-modified arginine residues — a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells
- 1 March 1997
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1356 (1) , 84-94
- https://doi.org/10.1016/s0167-4889(96)00154-1
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albuminsProtein Journal, 1995
- Advanced glycation end products contribute to amyloidosis in Alzheimer disease.Proceedings of the National Academy of Sciences, 1994
- beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis.Journal of Clinical Investigation, 1993
- Angiogenic Effects of Advanced Glycation End Products of the Maillard Reaction on Cultured Human Umbilical Cord Vein Endothelial CellsBiochemical and Biophysical Research Communications, 1993
- Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus.Journal of Clinical Investigation, 1993
- Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: a model for diabetic and aging complications.Proceedings of the National Academy of Sciences, 1992
- Receptor-specific induction of insulin-like growth factor I in human monocytes by advanced glycosylation end product-modified proteins.Journal of Clinical Investigation, 1992
- Role of Glycation in Modification of Lens Crystallins in Diabetic and Nondiabetic Senile CataractsDiabetes, 1991
- Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging.Proceedings of the National Academy of Sciences, 1990
- High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules.Proceedings of the National Academy of Sciences, 1985