Recently, a new protein containing a disintegrin domain, alternagin-C (Alt-C), was purified fromBothrops alternatus venom. Unlike other disintegrins, in Alt-C an ECD amino acid motif takes the place of the RGD sequence. Most dis-integrins contain an RGD/KGD sequence and are very potent inhibitors of platelet aggregation, as well as other cell interactions with the extracellular matrix, including tumor cell metastasis and angiogenesis. The present study investi-gated the effects of Alt-C on human neutrophil chemotaxis in vitro and the activation of integrin-mediated pathways
