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THE DIVERSE CALPAIN FAMILY IN TRYPANOSOMATIDAE: FUNCTIONAL PROTEINS DEVOID OF PROTEOLYTIC ACTIVITY?
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Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Estudos Integrados em Protozoologia. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Laboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Laboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes. Rio de Janeiro, RJ, Brasil / Universidade Federal do Rio de Janeiro. Instituto de Química. Programa de Pós-Graduação em Bioquímica. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Estudos Integrados em Protozoologia. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Laboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes. Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro. Instituto de Microbiologia Paulo de Góes. Laboratório de Estudos Avançados de Microrganismos Emergentes e Resistentes. Rio de Janeiro, RJ, Brasil / Universidade Federal do Rio de Janeiro. Instituto de Química. Programa de Pós-Graduação em Bioquímica. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Estudos Integrados em Protozoologia. Rio de Janeiro, RJ, Brasil.
Abstract
Calpains 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?
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