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Glycoprotein 2 is a cell membrane protein of Trypanosoma cruzi that is cleaved into fragments by calpain. This study aimed to assess the susceptibility of glycoprotein 2 to calpain. Expression of the glycoprotein 2 was analyzed by western blot in extracts of epimastigotes incubated with the calpain inhibitor calpastatin. A time course of calpastatin treatment, combined or not with the proteasome inhibitor epoxomicin, was performed. G2 expression was evaluated by immunofluorescence using different glycoprotein 2-specific antibodies. The intracellular level of calpastatin was assessed by western blot, and the level of calpain activity was assessed by the release of KERNA from endogenous substrates. Glycoprotein 2 expression was reduced in extracts of epimastigotes incubated with calpastatin for a period of time up to 24 h. Incubation of epimastigotes for 6 h with calpastatin in the presence of epoxomicin, had no effect on G2 expression. Calpastatin treatment for 6 h in the absence of epoxomicin reduced G2 expression to 70 %. However, the proteasome inhibitor had no effect on G2 expression of epimastigotes incubated for 6 h with