dc.creatorEnnes-Vidal, Vitor
dc.creatorBranquinha, Marta Helena
dc.creatorSantos, André Luis Souza dos
dc.creatord`Avila-Levy, Claudia Masini
dc.date2021-09-06T21:32:39Z
dc.date2021-09-06T21:32:39Z
dc.date2021
dc.date.accessioned2023-09-26T21:15:46Z
dc.date.available2023-09-26T21:15:46Z
dc.identifierENNES-VIDAL, Vitor et al. Review The Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?. Cells, v. 10, n. 299, 11 p, Feb. 2021.
dc.identifier2073-4409
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/49014
dc.identifier10.3390/cells10020299
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8871698
dc.descriptionCalpains are calcium-dependent cysteine peptidases that were originally described in mammals and, thereafter, their homologues were identified in almost all known living organisms. The deregulated activity of these peptidases is associated with several pathologies and, consequently, huge efforts have been made to identify selective inhibitors. Trypanosomatids, responsible for life-threatening human diseases, possess a large and diverse family of calpain sequences in their genomes. Considering that the current therapy to treat trypanosomatid diseases is limited to a handful of drugs that suffer from unacceptable toxicity, tough administration routes, like parenteral, and increasing treatment failures, a repurposed approach with calpain inhibitors could be a shortcut to successful chemotherapy. However, there is a general lack of knowledge about calpain functions in these parasites and, currently, the proteolytic activity of these proteins is still an open question. Here, we highlight the current research and perspectives on trypanosomatid calpains, overview calpain description in these organisms, and explore the potential of targeting the calpain system as a thera peutic strategy. This review gathers the current knowledge about this fascinating family of peptidases as well as insights into the puzzle: are we unable to measure calpain activity in trypanosomatids, or are the functions of these proteins devoid of proteolytic activity in these parasites?
dc.formatapplication/pdf
dc.languageeng
dc.publisherMDPI
dc.rightsopen access
dc.subjectTrypanosoma
dc.subjectLeishmania
dc.subjectQuimioterapia
dc.subjectCisteína peptidase
dc.subjectCysteine peptidase
dc.subjectTrypanosoma
dc.subjectLeishmania
dc.subjectChemotherapy
dc.titleThe Diverse Calpain Family in Trypanosomatidae: Functional Proteins Devoid of Proteolytic Activity?
dc.typeArticle


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