Abstract
The dynamic natures of matrix proteins (fibrinogen, vitronectin) were compared in hemodialysis patients with the formation of hemostatic plugs (blood line coagulation) in dialyzers during hemodialysis (plug positive group) and in patients without the formation of hemostatic plugs during hemodialysis (plug negative group). The plasma concentration of fibrinogen during hemodialysis was not altered and no significant difference between these two groups was found. Plasma vitronectin concentrations tended to increase in the plug positive group. In addition, plasma thrombin-antithrombin III complex (TAT) values were not altered during hemodialysis in either group. This implies that the formation of hemostatic plugs is due mainly to platelet adhesion to the surface and not to the activation of blood coagulation. We analyzed the adsorbance of matrix proteins (fibrinogen, vitronectin) to the dialyzer membrane during hemodialysis. Fibrinogen was not identified in eluted fractions with TBS-1M NaCl from the dialyzer.
Immunoblotting analysis showed that vitronectin multimers were identified in eluted fractions with TBS-1M NaCl under non-reducing conditions in the plug positive group. In contrast, vitronectin multimers were not identified in the plug negative group. Vitronectin multimers were not present under reducing conditions, indicating that the multimers were disulfide bonded. It has been speculated that vitronectin multimers are involved in platelet-platelet and platelet-surface (subendothelial) interactions, like vWF-multimer, in the platelet-subendothelium. These date suggest that vitronectin-multimers are intimately involved in the augmented effect on residual blood volume during hemodialysis.
