Abstract
The glycation of plasma fibrinogen (Fbg) in diabetic patients, an alteration in clotting and fibrinolytic activities of glycated Fbg and the effect of various drugs on glycation of Fbg were investigated. The amount of furosine, which was a specific product by hydrolysis of glycated lysine residue of Fbg were determined using HPLC in 92 diabetic patients and 90 age-matched normal subjects as a control. Also the cloting and fibrinolytic activity of the glycated Fbg separated by aminophenyl boronate chromatography and inhibitory effects of acetyl salicylic acid (ASA), ascrobic asid (ACA) and pyridoxal phosphate (PP) on the production of furosine by hydrolysis of Fbg or lysine were examined.
The amount of furosine in hydrolysate of plasma Fbg was significantly higher in diabetic patients than normal subjects (p<0.001).
There was no difference in the release of fibrinopeptide-A from glycated and non-glycated Fbgs by after an addition of thrombin.
The polymerization and cross linking of fibrin monomer, were however, accelerated in the glycated Fbg and the fibrinolysis by plasmin was delayed in fibrin formed from the glycated Fbg. The production of furosine by a hydrolysis of Fbg or lysine after an incubation with glucose was suppressed by an addition of ASA and ACA.
