Abstract:
:Proteasomes are multi-subunit proteases involved in several mechanisms and thought to contribute to the regulation of cellular homeostasis. Here, we report for the first time biochemical evidence for the existence of a ubiquitin-proteasome proteolytic pathway in this parasite. Proteasomes from both cercariae and adult worms exhibited a high preference for hydrolysis of the substrate Suc-LLVY-AMC, although in the cercariae extract the rate of hydrolysis was 50% lower when compared to adult worms extracts. The same difference in proteasome activities was observed when endogenous proteins were broken down in the presence of ATP and ubiquitin. Additionally, accumulation of high molecular weight conjugates was observed when cercariae were pre-incubated with proteasome inhibitors. Finally, we present evidence that during experimental schistosomiasis, proteasome inhibitors were able to reduce the number of lung stage schistosomula, reduce the worm burden and consequently decrease the egg output in infected mice.
journal_name
Exp Parasitoljournal_title
Experimental parasitologyauthors
Guerra-Sá R,Castro-Borges W,Evangelista EA,Kettelhut IC,Rodrigues Vdoi
10.1016/j.exppara.2005.01.002keywords:
subject
Has Abstractpub_date
2005-04-01 00:00:00pages
228-36issue
4eissn
0014-4894issn
1090-2449pii
S0014-4894(05)00009-3journal_volume
109pub_type
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