Author | Santos, André Luis Souza dos | |
Author | Soares, Rosangela Maria de Araújo | |
Author | Alviano, Celuta Sales | |
Author | Kneipp, Lucimar Ferreira | |
Access date | 2019-03-14T13:16:57Z | |
Available date | 2019-03-14T13:16:57Z | |
Document date | 2008 | |
Citation | SANTOS, 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. | pt_BR |
ISSN | 0932-4739 | pt_BR |
URI | https://www.arca.fiocruz.br/handle/icict/32077 | |
Language | eng | pt_BR |
Publisher | Elsevier | pt_BR |
Rights | restricted access | pt_BR |
Subject in Portuguese | Trypanosomatina | pt_BR |
Subject in Portuguese | Metaloproteases | pt_BR |
Subject in Portuguese | Enzimas proteolíticas celulares | pt_BR |
Title | Heterogeneous production of metallo-type peptidases in parasites belonging to the family Trypanosomatidae | pt_BR |
Type | Article | pt_BR |
DOI | 10.1016/j.ejop.2007.08.006 | |
Abstract | Proteolytic 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. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Departamento de Microbiologia Geral. Rio de Janeiro, RJ, Brasil. | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Departamento de Micologia. Rio de Janeiro, RJ. Brasil. | pt_BR |
Subject | Cellular proteolytic enzymes | pt_BR |
Subject | Metallopeptidases | pt_BR |
Subject | Trypanosomatidae | pt_BR |
DeCS | Metaloproteases | pt_BR |
DeCS | Trypanosomatina | pt_BR |
e-ISSN | 1618-0429 | |
Embargo date | 2022-01-01 | |