Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators
Biocell
;
30(3): 479-490, dec. 2006. ilus, tab
Article
in English
| LILACS
| ID: lil-491547
ABSTRACT
Trypanosoma cruzi, the parasite causing Chagas disease, contains a number of proteolytic enzymes. The recent completion of the genome sequence of the T. cruzi CL Brener clone suggests the presence of 70 cysteine peptidases, 40 serine peptidases (none of them from the chymotrypsin family), about 250 metallopeptidases (most leishmanolysin homologues), 25 threonine peptidases, and only two aspartyl peptidases, none of them from the pepsin family. The cysteine peptidases belong to 7 families of Clan CA, 3 families of Clan CD, and one each of Clans CE and CF In Clan CA, the C1 family is represented by cruzipains 1 and 2, biochemically well characterized, as well as cathepsin B and two other cathepsins. There are a number of homologues to calpains (family C2), probably non-functional, lacking the Ca-binding domain. Family C54 includes the Atg4 proteinases (autophagins), which seem to be involved in the autophagic process. Clan CD includes family C14, the metacaspases. We have expressed the metacaspases TcMCA3 and TcMCA5, and obtained indirect evidence of their participation in programmed cell death induced by fresh human serum in the parasite. More experiments are required to better define their role in apoptosis.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Trypanosoma cruzi
/
Cysteine Endopeptidases
/
Amino Acid Sequence
Limits:
Animals
/
Humans
Language:
English
Journal:
Biocell
Journal subject:
Clulas
Year:
2006
Type:
Article
Affiliation country:
Slovenia
Institution/Affiliation country:
Jozef Stefan Institute/SI
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