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1.
São Paulo med. j ; 142(3): e2023121, 2024. tab, graf
Article in English | LILACS-Express | LILACS | ID: biblio-1530517

ABSTRACT

ABSTRACT BACKGROUND: The High Activity Arthroplasty Score (HAAS) is a self-administered questionnaire, developed in British English, that reliably and validly measures the levels of sports activities in patients following hip and knee arthroplasty surgery. OBJECTIVE: To cross-culturally adapt the HAAS to Brazilian Portuguese language. DESIGN AND SETTING: A cross-sectional study was conducted at a public university hospital in Brazil. METHODS: The Brazilian version of the HAAS was created through a six-step process: translation, synthesis, committee review, pretesting, back-translation, and submission to developers. The translation step was conducted by two independent bilingual translators, both native speakers of Brazilian Portuguese. The back-translation was performed by an independent translator, a native speaker of British English. To ensure the questionnaire's comprehensibility, 46 volunteers (51% men; average age 34-63) participated in the pre-testing step. RESULTS: The cross-cultural adaptation process necessitated modifications to certain terms and expressions to achieve cultural equivalence with the original HAAS. CONCLUSION: The HAAS has been translated from English into Brazilian Portuguese and culturally adapted for Brazil. The validation process for HAAS-Brazil is currently underway.

2.
Sao Paulo Med J ; 142(3): e2023121, 2023.
Article in English | MEDLINE | ID: mdl-38088686

ABSTRACT

BACKGROUND: The High Activity Arthroplasty Score (HAAS) is a self-administered questionnaire, developed in British English, that reliably and validly measures the levels of sports activities in patients following hip and knee arthroplasty surgery. OBJECTIVE: To cross-culturally adapt the HAAS to Brazilian Portuguese language. DESIGN AND SETTING: A cross-sectional study was conducted at a public university hospital in Brazil. METHODS: The Brazilian version of the HAAS was created through a six-step process: translation, synthesis, committee review, pretesting, back-translation, and submission to developers. The translation step was conducted by two independent bilingual translators, both native speakers of Brazilian Portuguese. The back-translation was performed by an independent translator, a native speaker of British English. To ensure the questionnaire's comprehensibility, 46 volunteers (51% men; average age 34-63) participated in the pre-testing step. RESULTS: The cross-cultural adaptation process necessitated modifications to certain terms and expressions to achieve cultural equivalence with the original HAAS. CONCLUSION: The HAAS has been translated from English into Brazilian Portuguese and culturally adapted for Brazil. The validation process for HAAS-Brazil is currently underway.


Subject(s)
Arthroplasty, Replacement, Knee , Cross-Cultural Comparison , Male , Humans , Adult , Middle Aged , Female , Brazil , Cross-Sectional Studies , Surveys and Questionnaires , Translations , Reproducibility of Results
3.
Biochim Biophys Acta Gen Subj ; 1861(1 Pt A): 3429-3443, 2017 Jan.
Article in English | MEDLINE | ID: mdl-27614033

ABSTRACT

BACKGROUND: Plant defensins were discovered at beginning of the 90s'; however, their precise mechanism of action is still unknown. Herein, we studied ApDef1-Saccharomyces cerevisiae interaction. METHODS: ApDef1-S. cerevisiae interaction was studied by determining the MIC, viability and death kinetic assays. Viability assay was repeated with hydroxyurea synchronized-yeast and pretreated with CCCP. Plasma membrane permeabilization, ROS induction, chromatin condensation, and caspase activation analyses were assessed through Sytox green, DAB, DAPI and FITC-VAD-FMK, respectively. Viability assay was done in presence of ascorbic acid and Z-VAD-FMK. Ultrastructural analysis was done by electron microscopy. RESULTS: ApDef1 caused S. cerevisiae cell death and MIC was 7.8µM. Whole cell population died after 18h of ApDef1 interaction. After 3h, 98.76% of synchronized cell population died. Pretreatment with CCCP protected yeast from ApDef1 induced death. ApDef1-S. cerevisiae interaction resulted in membrane permeabilization, H2O2 increased production, chromatin condensation and caspase activation. Ascorbic acid prevented yeast cell death and membrane permeabilization. Z-VAD-FMK prevented yeast cell death. CONCLUSIONS: ApDef1-S. cerevisiae interaction caused cell death through cell cycle dependentprocess which requires preserved membrane potential. After interaction, yeast went through uncontrolled ROS production and accumulation, which led to plasma membrane permeabilization, chromatin condensation and, ultimately, cell death by activation of caspase-dependent apoptosis via. GENERAL SIGNIFICANCE: We show novel requirements for the interaction between plant defensin and fungi cells, i.e. cell cycle phase and membrane potential, and we indicate that membrane permeabilization is probably caused by ROS and therefore, it would be an indirect event of the ApDef1-S. cerevisiae interaction.


Subject(s)
Caspases/metabolism , Cell Cycle/drug effects , Defensins/pharmacology , Microbial Viability/drug effects , Oxidative Stress/drug effects , Plant Proteins/pharmacology , Saccharomyces cerevisiae/cytology , Antifungal Agents/pharmacology , Cell Membrane Permeability/drug effects , Hydrogen Peroxide/metabolism , Kinetics , Membrane Potentials/drug effects , Models, Biological , Saccharomyces cerevisiae/drug effects , Saccharomyces cerevisiae/metabolism , Saccharomyces cerevisiae/ultrastructure
4.
J Plant Physiol ; 183: 144-53, 2015 Jul 01.
Article in English | MEDLINE | ID: mdl-26140981

ABSTRACT

Jacalin-related lectins (JRLs) encompass cytosolic, nuclear and vacuolar members displaying the jacalin domain in one or more copies or in combination with unrelated domains. Helianthus annuus jacalin (Helja) is a mannose-specific JRL previously identified in the apoplast of Helianthus annuus seedlings, and this protein has been proposed to follow unconventional secretion. Here, we describe the full-length Helja cDNA sequence, which presents a unique jacalin domain (merolectin) and the absence of a signal peptide, confirming that the protein cannot follow the classical ER-dependent secretory pathway. Helja mRNA is present in seeds, cotyledons, roots and hypocotyls, but no transcripts were detected in the leaves. Searches for sequence similarity showed that Helja is barely similar to other JRLs present in H. annuus databases and less than 45% identical to other monocot or dicot JRLs. Strikingly, most of the merolectins recovered through data mining using Helja as a query were predicted as apoplastic, although most of these proteins lack the signal peptide required for classical secretion. Thus, Helja is the first bait identified to recover putative unconventionally secreted lectins. Because the recovered JRLs are widely distributed among the plant kingdom, an as yet unknown role for jacalin lectins in the apoplast is emerging.


Subject(s)
Helianthus/genetics , Plant Proteins/genetics , Amino Acid Sequence , Base Sequence , Helianthus/metabolism , Molecular Sequence Data , Open Reading Frames , Phylogeny , Plant Lectins/chemistry , Plant Proteins/metabolism
5.
Protein Pept Lett ; 19(5): 520-9, 2012 May.
Article in English | MEDLINE | ID: mdl-22486647

ABSTRACT

In this study, the antifungal activity of peptides extracted from Adenanthera pavonina seeds was assessed. Peptides were extracted and fractionated by DEAE-Sepharose chromatography. The non-retained D1 fraction efficiently inhibited the growth of the pathogenic fungi. This fraction was later further fractionated by reversed-phase chromatography, resulting in 23 sub-fractions. All separation processes were monitored by tricine-SDS-PAGE. Fractions H11 and H22 strongly inhibited the growth of Saccharomyces cerevisiae and Candida albicans. Fraction H11 caused 100% death in S. cerevisiae in an antimicrobial assay. The complete amino acid sequence of the peptide in fraction P2 was determined, revealing homology to plant defensins, which was named ApDef1. Peptides from fraction H22 were also sequenced.


Subject(s)
Antifungal Agents/pharmacology , Antimicrobial Cationic Peptides/pharmacology , Fabaceae/chemistry , Fungi/drug effects , Plant Extracts/pharmacology , Seeds/chemistry , Amino Acid Sequence , Antifungal Agents/chemistry , Antimicrobial Cationic Peptides/chemistry , Chromatography, Liquid , Microbial Sensitivity Tests , Microbial Viability/drug effects , Molecular Sequence Data , Plant Extracts/chemistry , Sequence Alignment
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