RESUMO
BACKGROUND: The changing demands on healthcare require continuous development and education in the nursing profession. Homogeneity in nursing qualifications reduces educational inconsistencies between and within countries. However, despite various initiatives, modifying nurse education remains challenging because different countries have their own legislations, structures, motivations, and policies. OBJECTIVES: To summarize the characteristics of nurse education programs around the globe and analyze the similarities and differences between them. DESIGN AND METHODS: A scoping review was performed to identify different characteristics of nurse education programs in Organization for Economic Co-operation and Development (OECD) countries. Records published between January 2016 and July 2021 were searched in the PubMed, Cinahl, and ERIC databases. The reference lists of all included articles were also searched manually for relevant studies. Articles were eligible if they described nurse education in one or more of the selected countries with a focus on nursing degrees (both undergraduate and postgraduate programs), nursing titles, program duration, study load hours, or practice hours. Data were independently extracted using a predefined extraction sheet. We asked the respective nursing associations for confirmation and to provide any additional information. RESULTS: After searching 9769 records, 117 were included in the synthesis. The included records described characteristics of undergraduate nursing educational programs (nâ¯=â¯50), postgraduate programs (nâ¯=â¯30), or both (nâ¯=â¯37). In total, 86 undergraduate and 82 postgraduate programs were described, with a great variety in degrees, nursing titles, study load hours, and practice hours. CONCLUSIONS: This study demonstrates that there is still considerable variation in nurse education programs between countries. These diverse educational pathways lead to different nursing titles and internationally standardized definitions of nursing roles have not been established. This makes it difficult to understand the healthcare role of nurses. Hence, efforts are needed to increase the quality and uniformity of nurse education around the world.
Assuntos
Bacharelado em Enfermagem, Estudantes de Enfermagem, Humanos, Currículo, Papel do Profissional de EnfermagemRESUMO
Na(+) and sugar transport by cotransporters (symporters) is thought to occur as a series of ordered ligand-induced conformational changes. To localize these conformational changes in a bacterial Na(+)/galactose cotransporter, we have employed a combination of cysteine-scanning and fluorescence techniques. Single or pairs of cysteine residues were introduced into the external face of a cysteine-less Vibrio parahaemolyticus sodium/glucose cotransporter for expression in Escherichia coli, and each transporter was purified using affinity chromatography. All the mutant proteins retained transport activity in bacteria and proteoliposomes. Each mutant was exposed to two different fluorescence reagents, ThioGlo3 or pyrene maleimide, that are essentially nonfluorescent until they react with a thiol. Fluorescence was recorded as a function of time and ligand concentrations. The reagents specifically labeled six of the seven cysteine mutants, but only in Cysteine 423 was the fluorescence affected by ligands. The rate of labeling of Cys423 by ThioGlo3 or pyrene maleimide was reduced by D-galactose in Na(+) buffer. Furthermore, the fluorescence of Thioglo3-labeled Cys423 was quenched by D-galactose, but only in the presence of Na(+). This quench was not accompanied by a Stokes shift and was not produced by nontransported sugars, e.g., L-glucose. Reducing the sodium concentration from 200 to 10 mM decreased the apparent affinity for d-galactose without altering the maximum quench with saturating D-galactose. Reducing the galactose concentration from 20 to 0.5 mM reduced both the apparent affinity for Na(+) and the maximum quench at saturating Na(+). These results suggest an ordered reaction scheme with Na(+) binding first. The fluorescence results with ThioGlo3-labeled Cys423 indicate that conformational changes underlying Na(+)/galactose cotransport occur at or near the extracellular domain between transmembrane helices 10 and 11.
Assuntos
Galactose/metabolismo, Proteínas de Transporte de Monossacarídeos/química, Vibrio parahaemolyticus/química, Sequência de Aminoácidos, Proteínas de Bactérias, Cisteína/genética, Transferência Ressonante de Energia de Fluorescência, Humanos, Ligantes, Lipossomos, Glicoproteínas de Membrana/química, Dados de Sequência Molecular, Proteínas de Transporte de Monossacarídeos/genética, Proteínas de Transporte de Monossacarídeos/metabolismo, Mutagênese Sítio-Dirigida, Conformação Proteica, Sódio/química, Proteínas de Transporte de Sódio-Glucose, Transportador 1 de Glucose-Sódio, Espectrometria de Fluorescência, Triptofano/química, Vibrio parahaemolyticus/genética, Vibrio parahaemolyticus/metabolismoRESUMO
The human multidrug resistance-associated protein(MRP1) is an ATP-dependent efflux pump that transports anionic conjugates, and hydrophobic compounds in a glutathione dependent manner. Similar to the other, well-characterized multidrug transporter P-gp, MRP1 comprises two nucleotide-binding domains (NBDs) in addition to transmembrane domains. However, whereas the NBDs of P-gp have been shown to be functionally equivalent, those of MRP1 differ significantly. The isolated NBDs of MRP1 have been characterized in Escherichia coli as fusions with either the glutathione-S-transferase (GST) or the maltose-binding domain (MBP). The nonfused NBD1 was obtained by cleavage of the fusion protein with thrombin. The GST-fused forms of NBD1 and NBD2 hydrolyzed ATP with an apparent K(m) of 340 microm and a V(max) of 6.0 nmol P(I) x mg-1 x min-1, and a K(m) of 910 microm ATP and a V(max) of 7.5 nmol P(I) x mg-1 x min-1, respectively. Remarkably, S-decyl-glutathione, a conjugate specifically transported by MRP1 and MRP2, was able to stimulate the ATPase activities of the isolated NBDs more than 2-fold in a concentration-dependent manner. However,the stimulation of the ATPase activity was found to coincide with the formation of micelles by S-decyl-glutathione. Equivalent stimulation of ATPase activity could be obtained by surfactants with similar critical micelle concentrations.
