Proteinases of XXXX : patential targets for the chemotherapy of Changas desease.

@entity1 @entity462 @entity10783 @entity1527 @entity19 @entity102 @entity1526 @entity563 @entity141 @entity1889 @entity16628
@entity1527 , the agent of the @entity1526 , @entity1526 , contains @entity462 , @entity563 , @entity1889 and metallo proteinases. Aspartic proteinases have not been found so far. The most abundant among these enzymes is cruzipain, a @entity462 proteinase expressed as a complex mixture of isoforms by the major developmental stages of the parasite, including some membrane-bound isoforms. The enzyme is an immunodominant antigen in @entity1 @entity102 and seems to be important in the host/parasite relationship. Inhibitors of cruzipain kill the parasite and cure infected @entity19 , thus making the enzyme a very promising target for the development of new drugs against @entity1526 . In addition 30 kDa cathepsin B-like enzymes have been described. @entity563 peptidases described in the parasite include oligopeptidase B, a member of the @entity10783 oligopeptidase family involved in @entity141 -signalling during @entity1 cell invasion; a @entity10783 endopeptidase (Tc80), against which inhibitors are being developed, and a @entity563 carboxypeptidase belonging to the S10 family. Metalloproteinases homologous to the gp63 of Leishmania spp. are also present. The proteasome has properties similar to those of other eukaryotes, and its inhibition by @entity16628 blocks some differentiation steps in the life cycle of the parasite.
