Article ID Journal Published Year Pages File Type
2064916 Toxicon 2011 11 Pages PDF
Abstract

Platelets play a central role in hemostasis during vascular injury. Patients affected with the hemorrhagic syndrome caused by contact with Lonomia achelous caterpillars (Lac) Lepidoptera distributed in various South American countries, show digestive, pulmonary and intraperitoneal bleeding in combination with hematomas and echymosis. In the present study, we have evaluated the effects of Lonomin V (serine protease isolated from Lac hemolymph) on some functional properties of platelets, evaluating its importance in primary hemostasis. Platelet adhesion to fibrinogen was reduced by 19, 20, 36, and 37% after pre-treated with 0.2, 2, 20 and 40 nM of Lonomin V, respectively. Pre-incubation of the platelets with 408 nM of Lonomin V, for 4 min at 37 °C, resulted in complete inhibition of the collagen-induced platelet aggregation, in contrast to 56% inhibition of the ADP - induced platelet aggregation. Lonomin V also inhibited anti-αIIbβ3 integrin binding to platelets by 56, 57, 52 and 54% at concentrations of 0.2, 2, 20 and 40 nM respectively. Additionally, Lonomin V inhibited anti-P-selectin binding to platelets by 28, 37, 33 and 33% at the same concentrations. The platelets tested with Lonomin V did not modify their viability. In summary, Lonomin V inhibited platelet aggregation, probably caused by the degradation of collagen. The anti-platelet activity of Lonomin V has been shown to be unique and a potentially useful tool for investigating cell-matrix and cell–cell interactions and for the development of antithrombotic agents in terms of their anti-adhesive activities.

► We evaluated the effect of Lonomin V (serine proteinase) on platelets functions. ► Cell adhesion was reduced probably due to the degradation of some integrins and/or fibrinogen. ► Platelet aggregation was reduced probably caused by the degradation of collagen. ► Other mechanisms independent of the enzymatic activity could be affecting platelet function. ► The anti-platelet activity of Lonomin V has potential in the use of an antithrombotic agent.

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