Abstract
Concanavalin A interacts specifically with the oligosaccharides from protein-C and modifies its anticoagulant activity. The lectin activates the protein-C activity in a dose dependent manner as demonstrated by in vitro and in vivo assays. Concanavalin A at low concentration (0.1 to 2 μg/mL) induces an increase on the catalytic activity of protein-C; at higher concentrations (5 to 20 μg/mL), the catalytic activity returns to the baseline. The effect of Concanavalin A was prevented by incubating the protein-C with α-methyl-mannoside or by treating the purified protein-C with α-mannosidase; furthermore, cleavage of mannosidic residues diminishes its catalytic activity. Our results indicate that the oligomannosidic portion of protein-C participates in the regulation of the catalytic activity of this protein.
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