Heterogeneous production of metallo-type peptidases in parasites belonging to the family Trypanosomatidae

dc.creatorSantos, André Luis Souza dos
dc.creatorSoares, Rosangela Maria de Araújo
dc.creatorAlviano, Celuta Sales
dc.creatorKneipp, Lucimar Ferreira
dc.date2019-03-14T13:16:57Z
dc.date2019-03-14T13:16:57Z
dc.date2008
dc.date.accessioned2023-09-26T22:20:14Z
dc.date.available2023-09-26T22:20:14Z
dc.identifierSANTOS, André Luis Souza dos; et al. Heterogeneous production of metallo-type peptidases in parasites belonging to the family Trypanosomatidae. European Journal of Protistology, v.44, p.103-113, 2008.
dc.identifier0932-4739
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/32077
dc.identifier10.1016/j.ejop.2007.08.006
dc.identifier1618-0429
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8878021
dc.descriptionProteolytic enzymes play a central role in the physiology of all living organisms, participating in several metabolic pathways and in different phases of parasite–host interactions. We have identified cell-associated peptidase activities in 33 distinct flagellates, including representatives of almost all known trypanosomatid genera parasitizing insects (Herpetomonas, Crithidia, Leishmania, Trypanosoma, Leptomonas, Phytomonas, Blastocrithidia and Endotrypanum) as well as the biflagellate kinetoplastid Bodo, by using SDS–PAGE containing gelatin as co-polymerized substrate and proteolytic inhibitors. Under the alkaline pH (9.0) conditions employed, all the flagellates presented at least one peptidase, with the exception of Crithidia acanthocephali and Phytomonas serpens, which did not display any detectable proteolytic enzyme activity. All the proteolytic activities were completely inhibited by 1,10-phenanthroline, a zincchelating agent, putatively identifying these activities as metallo-type peptidases. EDTA and EGTA, two other metallopeptidase inhibitors, E-64 (a cysteine peptidase inhibitor), pepstatin A (an aspartyl peptidase inhibitor) and PMSF (a serine peptidase inhibitor) did not interfere with the metallopeptidase activities detected in the studied trypanosomatids. Conversely, Bodo-derived peptidases were resistant to 1,10-phenanthroline and only partially inhibited by EDTA, showing a distinct inhibition profile. Together, our data demonstrated great heterogeneity of expression of metallopeptidases in a wide range of parasites belonging to the family Trypanosomatidae.
dc.description2022-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectTrypanosomatina
dc.subjectMetaloproteases
dc.subjectEnzimas proteolíticas celulares
dc.subjectCellular proteolytic enzymes
dc.subjectMetallopeptidases
dc.subjectTrypanosomatidae
dc.subjectMetaloproteases
dc.subjectTrypanosomatina
dc.titleHeterogeneous production of metallo-type peptidases in parasites belonging to the family Trypanosomatidae
dc.typeArticle


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