Purified platelet aggregating factor (PAF) was obtained from bovine BaSO
4-adsorbed plasma through DEAE cellulose column after bentonite adsorption and polyethylene glycol fractionation. This purified PAF was stable to heat (54°C, 150 min.), and plasmin digestion (1 cu/m
l, 120 min.), against the obserbations of Vermylen, J. et al. & Fukui, H. Using this purified PAF, PAF-induced platelet aggregation was studied on human platelets in comparison with Ristocetin-induced platelet agreegation (RIPA).
Five patients with hemophilia A showed normal platelet aggregation with both Ristocetin and PAF. Studied were PRP of three patients with von Willebrand's disease whose Ristocetin cofactor (VIII
VWF) was below 12.5% of normal. In two of them, whose AHF like antigen (VIII
AGN) level was 64%, 49% of normal, PRP showed no aggregation with Ristocetin, but normal aggregation with PAF. However, the other case with von Willebrand's disease, whose VIII
AGN level was not detected, showed hyperaggregation with PAF. It may be suggested that human VIII
AGN have some inhibitory effects on PAF-induced aggregation, through saturation of receptors on platelets.
In five cases with thrombasthenia, the intensity of platelet aggregation with both Ristocetin and PAF was reduced, and their PRP showed spontaneous disaggregation. Addition of ADP (10 μM) inhibited Ristocetin- and PAF-induced aggregation, and ATP (2.5 mM) overcomed these inhibitory effects of ADP. ATP also prevented disaggregation seen in thrombasthenic PRP as well as EDTA treated normal PRP. Although addition of ADP to formalin fixed normal platelets did not inhibit RIPA, aggregation was reduced when ADP was added before these EDTA treated platelets were fixed. ATP prevented this inhibitory effects of ADP, too. These findings support the reports of Cohen, I. et al. & Grant, R. A. et al, and might suggest that ADP and/or ATP bind to platelet membrane so that the receptors to von Willebrand factor, or PAF may become transformed.
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