The Cysteine Protease Inhibitors EhICP1 and EhICP2 Perform Different Tasks in the Regulation of Endogenous Protease Activity in Trophozoites of Entamoeba histolytica

DC FieldValueLanguage
dc.contributor.authorSaric, Mirela
dc.contributor.authorIrmer, Henriette
dc.contributor.authorEckert, Daniela
dc.contributor.authorBaer, Ann-Katrein
dc.contributor.authorBruchhaus, Iris
dc.contributor.authorScholze, Henning
dc.date.accessioned2021-12-23T16:06:58Z-
dc.date.available2021-12-23T16:06:58Z-
dc.date.issued2012
dc.identifier.issn14344610
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/7641-
dc.description.abstractTrophozoites of E. histolytica are equipped with two chagasin-like cysteine protease inhibitors, EhICP1 and EhICP2, also known as amoebiasin 1 and 2. Expression studies using E. invadens as model organism showed that corresponding mRNAs were detectable in both life stages of the parasite, cyst and trophozoite state. Unlike EhICP1 known to act in the cytosol, EhICP2 co-localized with cysteine protease EhCP-A1 in lysosome-like vesicles, as demonstrated by immunofluorescence microscopy. Silencing or overexpressing of the two inhibitors did not show any effect on morphology and viability of the trophozoites. Overexpression of the EhICPs, however, although dramatically dampening the proteolytic activity of cell extracts from the corresponding cell lines, did not influence expression rate or localization of the major amoebic cysteine proteases as well as phagocytosis and digestion of erythrocytes. Activity gels of cell extracts from strains overexpressing ehicp1 showed a drastically reduced activity of EhCP-A1 suggesting a high affinity of EhICP1 towards this protease. From these data, we propose that EhCP-A1 accidentally released into the cytosol is the main target of EhICP1, whereas EhICP2, beside its role in house-keeping processes, may control the proteolytic processing of other hydrolases or fulfils other tasks different from protease inhibition. (C) 2011 Elsevier GmbH. All rights reserved.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [BR1744/11-1]; This work includes parts of the doctoral thesis of M. S., who was a recipient of a grant from the research-training group 612 of the Deutsche Forschungsgemeinschaft. The contribution of I.B. was supported by the Deutsche Forschungsgemeinschaft (project BR1744/11-1).
dc.language.isoen
dc.publisherELSEVIER GMBH
dc.relation.ispartofPROTIST
dc.subjectAmoebiasin
dc.subjectBINDING
dc.subjectCHAGASIN
dc.subjectcysteine protease inhibitor
dc.subjectEntamoeba histolytica
dc.subjectEntamoeba invadens
dc.subjectGENE-EXPRESSION
dc.subjectINVADENS
dc.subjectMicrobiology
dc.subjectPEPTIDASE INHIBITOR
dc.subjectPROTEINASE
dc.subjectPROTOZOAN
dc.subjectSECRETION
dc.subjectSEQUENCE
dc.subjectTRYPANOSOMA-CRUZI
dc.titleThe Cysteine Protease Inhibitors EhICP1 and EhICP2 Perform Different Tasks in the Regulation of Endogenous Protease Activity in Trophozoites of Entamoeba histolytica
dc.typejournal article
dc.identifier.doi10.1016/j.protis.2011.01.003
dc.identifier.isiISI:000298138600010
dc.description.volume163
dc.description.issue1
dc.description.startpage116
dc.description.endpage128
dc.contributor.orcid0000-0001-8780-8552
dc.contributor.orcid0000-0002-8763-502X
dc.publisher.placeHACKERBRUCKE 6, 80335 MUNICH, GERMANY
dcterms.isPartOf.abbreviationProtist
Show simple item record

Page view(s)

1
Last Week
0
Last month
0
checked on Apr 16, 2024

Google ScholarTM

Check

Altmetric