Abstract
RECENT work1,2 has demonstrated that bovine factor VIII, not bovine fibrinogen, aggregates human platelets. This aggregation can occur in two waves, the first being independent of release of platelet adenosine-5′-diphosphate. Bovine factor VIII is rich in carbohydrate: it contains 11% hexoses (mannose and galactose, in a ratio of 1 to 3), 2% sialic acid and 7% hexosamine3. Carbohydrate side chains would play a critical role in collagen–platelet adhesion and subsequent aggregation; a substrate-enzyme complex4 would be formed between side chains of collagen containing galactose5 but not terminated by sialic acid and sialyl transferase located on the platelet membrane6. Oxidation of the galactosyl residues in collagen abolishes platelet aggregation5. We wondered whether a similar mechanism would initiate platelet aggregation by bovine factor VIII.
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