Abstract:
:Several genes related to the ubiquitin (Ub)-proteasome pathway, including those coding for proteasome subunits and conjugation enzymes, are differentially expressed during the Schistosoma mansoni life cycle. Although deubiquitinating enzymes have been reported to be negative regulators of protein ubiquitination and shown to play an important role in Ub-dependent processes, little is known about their role in S. mansoni . In this study, we analysed the Ub carboxyl-terminal hydrolase (UCHs) proteins found in the database of the parasite's genome. An in silico ana- lysis (GeneDB and MEROPS) identified three different UCH family members in the genome, Sm UCH-L3, Sm UCH-L5 and Sm BAP-1 and a phylogenetic analysis confirmed the evolutionary conservation of the proteins. We performed quantitative reverse transcription-polymerase chain reaction and observed a differential expression profile for all of the investigated transcripts between the cercariae and adult worm stages. These results were corroborated by low rates of Z-Arg-Leu-Arg-Gly-Gly-AMC hydrolysis in a crude extract obtained from cercariae in parallel with high Ub conjugate levels in the same extracts. We suggest that the accumulation of ubiquitinated proteins in the cercaria and early schistosomulum stages is related to a decrease in 26S proteasome activity. Taken together, our data suggest that UCH family members contribute to regulating the activity of the Ub-proteasome system during the life cycle of this parasite.
journal_name
Mem Inst Oswaldo Cruzjournal_title
Memorias do Instituto Oswaldo Cruzauthors
Pereira RV,Vieira HG,Oliveira VF,Gomes Mde S,Passos LK,Borges Wde C,Guerra-Sá Rdoi
10.1590/0074-0276130107subject
Has Abstractpub_date
2014-02-01 00:00:00pages
1-8issue
1eissn
0074-0276issn
1678-8060pii
S0074-02762013005030107journal_volume
109pub_type
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journal_title:Memorias do Instituto Oswaldo Cruz
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