Abstract:
:Investigation of protease activities during the transformation of Trypanosoma cruzi epimastigotes into metacyclic trypomastigoes (metacyclo-genesis) revealed three major components with apparent molecular weights of 65, 52, and 40 kDa. The 65-kDa protease is a metacyclic trypomastigote stage-specific protease with an isoelectric point of 5.2 whose activity is inhibited by 1,10-phenanthroline, suggesting that it might be a metalloprotease. The 52-kDa component is also a metalloprotease which is constitutively expressed in epimastigotes and metacyclic trypomastigoes. On the other hand, the 40-kDa component is apparently made up of several isoforms of a cysteine protease which is expressed in much higher levels in epimastigotes than in metacyclic trypomastigote forms. The fact that the 65- and 40-kDa proteases are developmentally regulated suggests that proteases might be important for T. cruzi differentiation. Accordingly, T. cruzi metacyclogenesis is blocked by metallo- and cysteine-protease inhibitors.
journal_name
Exp Parasitoljournal_title
Experimental parasitologyauthors
Bonaldo MC,d'Escoffier LN,Salles JM,Goldenberg Sdoi
10.1016/0014-4894(91)90006-isubject
Has Abstractpub_date
1991-07-01 00:00:00pages
44-51issue
1eissn
0014-4894issn
1090-2449pii
0014-4894(91)90006-Ijournal_volume
73pub_type
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