Consulta: subjectFacets:"Peroxiredoxin"
Registros recuperados: 4
Data/hora: 10/06/2024 06:35:14

Multiple genes contribute to anhydrobiosis (tolerance to extreme desiccation) in the nematode Panagrolaimus superbus
Provedor de dados: Genetics and Molecular Biology
Autores: Evangelista,Cláudia Carolina Silva; Guidelli,Giovanna Vieira; Borges,Gustavo; Araujo,Thais Fenz; Souza,Tiago Alves Jorge de; Neves,Ubiraci Pereira da Costa; Tunnacliffe,Alan; Pereira,Tiago Campos.
Abstract The molecular basis of anhydrobiosis, the state of suspended animation entered by some species during extreme desiccation, is still poorly understood despite a number of transcriptome and proteome studies. We therefore conducted functional screening by RNA interference (RNAi) for genes involved in anhydrobiosis in the holo-anhydrobiotic nematode Panagrolaimus superbus. A new method of survival analysis, based on staining, and proof-of-principle RNAi experiments confirmed a role for genes involved in oxidative stress tolerance, while a novel medium-scale RNAi workflow identified a further 40 anhydrobiosis-associated genes, including several involved in proteostasis, DNA repair and signal transduction pathways. This suggests that multiple genes...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Peroxiredoxin; Kinase; RNAi; Proteostasis.
Ano: 2017
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572017000500790

Identification and functional analysis of a novel mitochondria-localized 2-Cys peroxiredoxin, BbTPx-2, from Babesia bovis
Provedor de dados: Obihiro University of Agriculture and Veterinary Medicine Academic Repository (OAK)
Autores: Masatani, Tatsunori; Asada, Masahito; Hakimi, Hassan; Hayashi, Kei; Yamagishi, Junya; Kawazu, Shin-ichiro; Xuan, Xuenan.
Cysteine-based peroxidases, known as peroxiredoxins (Prx) or thioredoxin peroxidases (TPx), are important antioxidant enzymes that prevent oxidative damage caused by reactive oxygen species (ROS). In this study, we identified a novel mitochondrial 2-Cys Prx, BbTPx-2, from a bovine Babesia parasite, B. bovis. BbTPx-2 complementary DNA (cDNA) encodes a polypeptide of 254 amino acid residues. This protein has a mitochondrial targeting peptide at the N-terminus and two conserved cysteine residues of the typical 2-Cys Prx. By using a thiol mixed-function oxidation assay, the antioxidant activity of recombinant BbTPx-2 was revealed, and its antioxidant activity was comparable to that of a cytosolic 2-Cys Prx from B. bovis, BbTPx-1. Notably, we confirmed that...
Palavras-chave: Antioxidant activity; Babasia bovis; Mitochondria; Peroxiredoxin.
Ano: 2016
URL: http://ir.obihiro.ac.jp/dspace/handle/10322/4487

Development of Monoclonal Antibodies That Target 1-Cys Peroxiredoxin and Differentiate Plasmodium falciparum from P. vivax and P. knowlesi
Provedor de dados: Obihiro University of Agriculture and Veterinary Medicine Academic Repository (OAK)
Autores: Hakimi, Hassan; Nguyen, Thu-Thuy; Suganuma, Keisuke; Masuda-Suganuma, Hirono; Ma. M. Angeles, Jose; Inoue, Noboru; Kawazu, Shin-ichiro; 井上, 昇; 河津, 信一郎.
Prompt and accurate diagnosis of malarial patients is a crucial factor in controlling the morbidity and mortality of the disease. Effective treatment decisions require a correct diagnosis among mixed-species malarial patients. Differential diagnosis is particularly important in cases of Plasmodium vivax, a species that shares endemicity with P. falciparum in most endemic areas. Moreover, it is difficult to identify P. knowlesi on the basis of morphology alone, and rapid diagnostic tests are still not available for this malaria species. Therefore, the development of diagnostic tests applicable to the field is urgently needed. 1-Cys peroxiredoxin (1-Cys-Prx) in P. falciparum is abundantly expressed in the mature asexual stages, making it a promising...
Palavras-chave: Malaria diagnosis; Monoclonal antibody; Peroxiredoxin; Plasmodium knowlesi; P. vivax.
Ano: 2013
URL: http://ir.obihiro.ac.jp/dspace/handle/10322/3859

Cloning and Characterization of a 2-Cys Peroxiredoxin from Babesia gibsoni
Provedor de dados: Obihiro University of Agriculture and Veterinary Medicine Academic Repository (OAK)
Autores: MASATANI, Tatsunori; ASADA, Masahito; ICHIKAWA-SEKI, Madoka; USUI, Miho; TERKAWI, Mohamad A.; HAYASHI, Kei; KAWAZU, Shin-ichiro; XUAN, Xuenan; 河津, 信一郎; 玄, 学南.
Peroxiredoxins (Prxs) are a family of antioxidant enzymes. Here, we cloned a 2-Cys Prx, BgTPx-1, from the canine Babesia parasite B. gibsoni. Sequence identity between BgTPx-1 and 2-Cys Prx of B. bovis was 81% at the amino acid level. Enzyme activity assay by using recombinant BgTPx-1 (rBgTPx-1) indicated that BgTPx-1 has antioxidant activity. Antiserum from a mouse immunized with rBgTPx-1 reacted with parasite lysates and detect a protein with a monomeric size of 22 kDa and also a 44 kDa protein, which might be an inefficiently reduced dimer. BgTPx-1 was expressed in the cytoplasm of B. gibsoni merozoites. These results suggest that the BgTPx-1 may play a role to control redox balance in the cytoplasm of B. gibsoni.
Palavras-chave: Antioxidant activity; Babesia gibsoni; Canine; Peroxiredoxin.
Ano: 2014
URL: http://ir.obihiro.ac.jp/dspace/handle/10322/3925