Summary
Anticoagulated whole blood from patients and control subjects was circulated through
an annular perfusion chamber in which the fibrillar collagen of α chymotrypsin-digested
subendothelium and intact subendothelium were exposed. The blood flow conditions corresponded
to those in arteries (830 sec–1 wall shear rate). Platelet surface interaction was measured mor-phometrically.
Decreased adhesion to fibrillar collagen associated with normal spreading and normal
adhesion-induced formation of platelet thrombi was found with blood of patients with
von Willebrand’s disease and the Bernard Soulier Syndrome, indicating a defect in the initial attachment reaction of platelets with collagen.
Platelets of patients with thrombasthenia did normally adhere to the collagen fibrils and also lost their subcellular organelles
during this reaction, but they totally failed to adhere to each other. In storage pool disease platelet thrombus formation was consistently inhibited whereas adhesion and spreading
was inhibited in some patients and normal in others. In contrast adhesion was always
normal after ingestion of aspirin which consistently caused a marked inhibition of platelet thrombi. These findings
correspond – in essence – to those previously described on intact subendothelium.
However, the observed defects are more pronounced on the fibrillar collagen than on
intact subendothelium.
