Universidad Peruana Cayetano Heredia

Comparative zymographic analysis of metallopeptidase of Leishmania (Viannia) peruviana and Leishmania (Viannia) braziliensis isolates from Peru

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dc.contributor.author Reyes-Uribe, P.
dc.contributor.author Pereira-dos-Santos, T.
dc.contributor.author De Jesus, J.B.
dc.contributor.author Mesquita-Rodrigues, C.
dc.contributor.author Arévalo Zelada, Jorge Luis
dc.contributor.author Cupolillo, E.
dc.contributor.author Cuervo, P.
dc.date.accessioned 2022-01-18T19:26:48Z
dc.date.available 2022-01-18T19:26:48Z
dc.date.issued 2012
dc.identifier.uri https://hdl.handle.net/20.500.12866/10884
dc.description.abstract American tegumentary leishmaniasis (ATL) in Peru is mainly associated with Leishmania (Viannia) peruviana and L. (V.) braziliensis. These parasites are genetically related, and their characterization as distinct species is controversial. Despite their genetic similarity, each species is associated with different clinical manifestations of ATL; L. (V.) peruviana causes only cutaneous leishmaniasis, whereas L. (V.) braziliensis can cause both cutaneous and mucocutaneous leishmaniasis. Because the primary cutaneous lesions caused by infection with these species are indistinguishable, it is necessary to develop a suitable method to differentiate them in order to prevent possible metastasis to oropharyngeal mucosa. In the present study, we investigated the proteolytic profile of L. (V.) peruviana and L. (V.) braziliensis isolates from Peru by zymographic analysis in SDS-PAGE copolymerized with gelatin. Enzymes were characterized according to their pH range of activity and sensitivity to distinct peptidase inhibitors. We observed that L. (V.) peruviana isolates displayed three proteolytic bands with molecular masses ranging from 55 to 80. kDa, whereas L. (V.) braziliensis isolates showed six proteolytic activities between 55 and 130. kDa. Using specific inhibitors, we determined that these proteolytic activities are due to metallopeptidases and present optimal activity between the pH range 5.5 and 10.0. Our results suggest that the expression of metallopeptidases in L. (V.) peruviana and L. (V.) braziliensis isolates from Peru is species-specific. en_US
dc.language.iso eng
dc.publisher Elsevier
dc.relation.ispartofseries Parasitology International
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject Humans en_US
dc.subject Peru|Polymerase Chain Reaction en_US
dc.subject Zymography en_US
dc.subject Ph en_US
dc.subject Leishmaniasis Cutaneous en_US
dc.subject Restriction Fragment Length Polymorphism en_US
dc.subject Leishmania en_US
dc.subject Enzyme Activity en_US
dc.subject Leishmania Peruviana en_US
dc.subject Species Specificity en_US
dc.subject Hydrogen-Ion Concentration en_US
dc.subject Protein Degradation en_US
dc.subject Molecular Weight en_US
dc.subject Polyacrylamide Gel Electrophoresis en_US
dc.subject Leishmania (Viannia) Braziliensis en_US
dc.subject Gene Expression Regulation Enzymologic en_US
dc.subject Leishmania (Viannia) Peruviana en_US
dc.subject Metallopeptidases en_US
dc.subject Peptidases en_US
dc.title Comparative zymographic analysis of metallopeptidase of Leishmania (Viannia) peruviana and Leishmania (Viannia) braziliensis isolates from Peru en_US
dc.type info:eu-repo/semantics/article
dc.identifier.doi https://doi.org/10.1016/j.parint.2012.03.007
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#3.03.07
dc.relation.issn 1873-0329


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