Abstract
Sialic acid is believed to play a critical role in the survival of blood platelets in circulation. Wheat germ agglutinin, which shows specificity for sialic acid, N-acetylglucosamine, and N- acetylgalactosamine, strongly activates platelets. The role of sialic acid in platelet activation by this lectin was studied utilizing neuraminidase-treated platelets and the succinylated lectin that has been reported not to recognize sialic acid. The succinylated lectin had a dimeric structure similar to the native lectin, but migrated more slowly in gel electrophoresis. The modified lectin bound to about 2.8 X 10(5) sites/cell, with an apparent dissociation constant of 2 microM compared to 5 X 10(5) sites/cell and a dissociation constant of 0.4 microM for the native lectin. The succinylated lectin neither aggregated nor agglutinated platelets, but agglutination of red cells in microtiter plates was normal. Aggregation of platelets by either wheat germ agglutinin or ristocetin was not affected by the succinylated lectin. Since the native wheat germ agglutinin is a strong activator of platelets and the succinylated derivative was devoid of all activity, it appears that a sialoprotein acts as the biologic receptor of wheat germ agglutinin in human platelets. This suggestion was strengthened by the observation that platelets treated with different concentrations of neuraminidase had a decreased capacity to bind this lectin. These platelets also showed reduced aggregation and serotonin secretion when activated with the native lectin. Since sialic acid has been implicated in the removal of platelets from circulation, wheat germ agglutinin may prove to be a useful tool to explore those clinical conditions in which platelet survival is shortened.
