| pubmed-article:7718622 | pubmed:abstractText | Short-term exposure of human serum albumin to glucose in vitro results in the formation of fructosyllysine residues. Using short-term glucose-modified albumin the interactions with human monocytes and with the human monocyte-like cells U937, MonoMac 6, HL60, and THP1 were studied. Short-term glycated albumin was specifically bound by monocytes, U937 and MonoMac 6 cells, but not by HL60 and THP1 cells. This specific binding of short-term glycated albumin was inhibited by fructosyllysine, but not by hexitollysine. Short-term glycated albumin did not compete for binding of albumin, modified by advanced glycation end products. Scatchard analysis of the binding data indicated that there are 10,000 binding sites per cell in monocytes or U937 cells and 2000 sites per cell on MonoMac 6 cells with affinity constants of 9 x 10(6) M-1. Specific binding of short-term glycated albumin to human monocytes was observed in 29% of the 101 human subjects investigated. Ligand-receptor cross-linking and ligand blotting experiments revealed two binding proteins of 100 to 110 and 190 kDa in SDS-PAGE after membrane protein solubilization of U937 and MonoMac 6 cells. The binding of short-term glycated albumin to MonoMac 6 cells induced the production of the cytokines IL-1 and TNF. | lld:pubmed |
