BINDING-SITES FOR SHORT-TERM GLYCATED ALBUMIN ON PERITONEAL-CELLS OF THE RAT

The interaction of in vitro short-term glycated rat serum albumin with rat peritoneal cells (40% macrophages) was investigated. Using I-125-labeled albumins the following results were obtained. Glycated albumins showed a binding reaction at 4-degrees-C, which appeared to reach equilibrium within 2 h. The concentration-dependent binding of glycated albumin showed saturation. Binding data evaluated for glycated albumin using the Sips equation are: average association constant K(o) = 3.15 . 10(7) M-1 with a heterogeneity index of a = 0.8 and 1.12 . 10(4) binding sites per cell. Such binding sites were identified in 40% of the peritoneal cell preparations studied. Native albumins, maleylated albumin, chondroitinsulfates, polylysine, lysine, fructose, glucose and hexitol-lysine could not compete with radio-labeled glycated rat albumin for its binding site on peritoneal cells. Effective competitors were glycated human serum albumin, glycated polylysine and fructose-lysine. Although the contamination with minute amounts of advanced glycosylation end products (AGE) could not be excluded, short-term glycated albumin was found to be bound to membranes of peritoneal phagocytotic cells by fructose-lysine specific proteins, whose approximately defined molecular masses of 290 kDa are distinct from hitherto described binding proteins for AGE- and aldehyde-modified proteins or for the scavenger receptors.