An Intervention to Enhance Recognition of Nursing Assistant Roles and Enhance Information-Sharing.

This column describes a quasi-experimental trial that examined the effects of an intervention in which both nurses and nursing assistants shared their perceptions of the nursing assistant role on the frequency of information-sharing behaviors. In the intervention group, the frequency of nurses' linguistic responses in the intervention group increased in the nursing assistants' evaluations. The frequency of nursing assistants' linguistic response and feedback in the intervention group increased in self-evaluation and nurses' evaluation, respectively.

Experiences and attitude of task shifting and task sharing of physicians, nurses, and nursing assistants in hospitals: a qualitative systematic review protocol.

OBJECTIVE: The objective of this review is to explore the experiences and attitudes of physicians, nurses, and nursing assistants regarding task-shifting and task-sharing in hospitals. INTRODUCTION: Despite multiple health care professionals performing overlapping tasks, the need for effective task-shifting and task-sharing remains a concern. Understanding task-shifting and task-sharing experiences, as well as the attitudes of health care providers in hospitals, is essential for providing safe and patient-appropriate care with limited human resources. INCLUSION CRITERIA: Qualitative studies that examine the experiences and attitudes of physicians, nurses, and nursing assistants in hospitals regarding task-shifting and task-sharing will be included. The review will include physicians, advanced practice nurses who are nurse practitioners or clinical nurse specialists, registered nurses, and nursing assistants. Midwives, pharmacists, occupational therapists, physical therapists, and students will be excluded. METHODS: PubMed, MEDLINE, CINAHL, PsycINFO, Cochrane Database, and Web of Science will be searched as part of a 3-step search strategy. We will search for unpublished research and gray literature using Google Scholar and ProQuest Dissertations and Theses. Inclusion criteria will be studies published in English or Japanese from the time each database was established to the present. The methodological quality of all studies will be evaluated by screening against the inclusion criteria and by at least 2 critical evaluations using the standardized JBI checklist. Synthesized results will be pooled by meta-aggregation and published as a ConQual Summary of Findings. REVIEW REGISTRATION: PROSPERO CRD42023409612.

Relationship between Unit-Level Nurses' Expectations from Nursing Assistant Roles and Individual Nursing Assistants' Information-Sharing Behaviors: A Multilevel Mediation Analysis.

PURPOSE: This study aimed to investigate the relationship between the expectations of unit-level nurses from nursing assistants (NAs), frequency of individual NAs' information-sharing behaviors with nurses, and the effect of NAs' self-perceived roles on this relationship. NAs provide patient care along with nurses, and their information-sharing behaviors with nurses may be influenced by the expectations of the nurses. METHODS: Nurses and NAs from 104 integrated community care (sub- and postacute) units were included in this Japanese cross-sectional study conducted from July to September 2018. Nurses' expectations from NAs and the NAs' self-perceived roles and information-sharing frequency were measured. Multilevel mediation analysis was performed for NAs' information-sharing behaviors, such as expressing, asking, providing linguistic responses, and providing feedback. RESULTS: Unit-level nurses' expectations from NAs were associated with the frequency of NAs' asking and responding behaviors with nurses (p < .05), mediated by the NAs' self-perceived roles. The frequency of NAs' expressing behaviors and feedback were also associated with their self-perceived roles (p < .001). CONCLUSIONS: High expectations of unit-level nurses from NAs led to better perception by NAs of their roles and led to better information-sharing behaviors. Educating nurses on NAs' roles may improve information-sharing between nurses and NAs that leads to safe and appropriate care to patients.

Nursing assistants' desired roles, perceptions of nurses' expectations and effect on team participation: A cross-sectional study.

AIMS: To examine the gap between nursing assistants' desired roles and their perceptions of nurses' expectations, and the relationship between these perceptions and nursing assistants' nursing team participation. BACKGROUND: Nursing assistants' role perceptions may be related to their participation in nursing teams. METHODS: We performed a secondary analysis of questionnaire data from 1,316 nursing assistants in Japan. RESULTS: Participants rated their desired roles higher than their perceptions of nurses' expectations of them. Where perceptions of nurses' expectations were higher, higher desired role scores were associated with greater nursing team participation. Where perceptions of nurses' expectations were lower, the desired role score was not associated with team participation. CONCLUSIONS: Nursing assistants perceive their roles as higher and inclusive of more duties than what nurses have expected of them. When perceptions of nurse expectations were high, they performed at a higher level. When perceptions of nurse expectations were low, they performed at a lower level, despite their desire to do more. IMPLICATIONS FOR NURSING MANAGEMENT: It may be useful for nurses and nursing assistants to jointly reflect on and promote awareness of nursing assistants' functional roles in the ward. This would promote nursing assistant team participation and optimize their scope of practice.

Irradiation effect of a submillimeter wave from 420†GHz gyrotron on amyloid peptides in vitro.

On using the far-infrared radiation system, whether the irradiation effect is thermal or non-thermal is controversial. We irradiated amyloid peptides that are causal factors for amyloidosis by using a submillimeter wave from 420 GHz gyrotron. Fluorescence reagent assay, optical and electron microscopies, and synchrotron-radiation infrared microscopy showed that the irradiation increased the fibrous conformation of peptides at room temperature for 30 min. The temperature increase on the sample was only below 5 K, and a simple heating up to 318 K hardly induced the fibril formation. Therefore, the amyloid aggregation was driven by the far-infrared radiation with little thermal effect.

Relationship between nurses' perceptions of nursing assistant roles and information-sharing behaviors: A cross-sectional study.

Information-sharing between nurses and nursing assistants is necessary for appropriate inpatient care. Nurses who perceive nursing assistant roles highly may display positive behaviors related to information-sharing with nursing assistants. This study aims to examine the relationship between nurses' perceptions of nursing assistant roles and the frequency of their sharing information with nursing assistants. Using a self-administered, cross-sectional survey questionnaire, data from 2,642 nurses in 182 hospitals were collected. Nurses' perceptions of nursing assistant roles were measured with a scale containing four factors: (i) improving patients' abilities through daily care; (ii) caring for various patients using broad perspectives; (iii) facilitating co-ordination and co-operation among team members; and (iv) increasing the amount of information on patients among team members. Information-sharing behaviors included "expressing," "asking," "linguistic response," and "feedback." Multiple regression analyses for each nurse's information-sharing behaviors were conducted. Nurses' perceptions of nursing assistant roles were positively correlated with the frequency of sharing information with nursing assistants. The degree of the correlations differed, depending on the type of information-sharing behavior. Therefore, improving nurses' understanding of nursing assistant roles might increase their information-sharing behaviors.

Structural stability of amyloid fibrils depends on the existence of the peripheral sequence near the core cross-ß region.

Amyloid fibrils are fibrous protein assemblies with distinctive cross-ß structures. For amyloidosis, there are disease-associated mutations outside of the cross-ß structures. Thus, it is necessary to elucidate the role of peripheral sequences outside the cross-ß structure. Amyloid fibrils are generally 10nm in width; however, the amyloid fibrils of truncated barnase M1 peptides missing the C-terminal sequence outside the cross-ß structure are 20 nm in width. In this study, we performed comparative analysis of the structural stability of amyloids formed by the respective peptides. We found that the C-terminal amino acids dramatically affect the conformational instability in the presence of a denaturing reagent.

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.

The mammalian endoplasmic reticulum (ER) contains a diverse oxidative protein folding network in which ERp46, a member of the protein disulfide isomerase (PDI) family, serves as an efficient disulfide bond introducer together with Peroxiredoxin-4 (Prx4). We revealed a radically different molecular architecture of ERp46, in which the N-terminal two thioredoxin (Trx) domains with positively charged patches near their peptide-binding site and the C-terminal Trx are linked by unusually long loops and arranged extendedly, forming an opened V-shape. Whereas PDI catalyzes native disulfide bond formation by the cooperative action of two mutually facing redox-active sites on folding intermediates bound to the central cleft, ERp46 Trx domains are separated, act independently, and engage in rapid but promiscuous disulfide bond formation during early oxidative protein folding. Thus, multiple PDI family members likely contribute to different stages of oxidative folding and work cooperatively to ensure the efficient production of multi-disulfide proteins in the ER.

Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding.

The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1α and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding. Here, we clarified the Prx4 preferential recognition of two PDI family proteins, P5 and ERp46, and the mode of interaction between Prx4 and P5 thioredoxin domain. Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides. Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding. Thus, the mammalian ER seems to contain highly systematized oxidative networks for the efficient production of large quantities of secretory proteins.

Stem-forming regions that are essential for the amyloidogenesis of prion proteins.

Prion diseases represent fatal neurodegenerative disorders caused by the aggregation of prion proteins. With regard to the formation of the amyloidogenic cross-ß-structure, the initial mechanism in the conversion to a ß-structure is critically important. To explore the core regions forming a stem of the amyloid, we designed and prepared a series of peptides comprised of two native sequences linked by a turn-inducing dipeptide moiety and examined their ability to produce amyloids. A sequence alignment of the peptides bearing the ability to form amyloid structures revealed that paired strands consisting of VNITI (residues 180-184) and VTTTT (residues 189-193) are the core regions responsible for initiating the formation of cross-ß-structures and for further ordered aggregation. In addition, most of the causative mutations responsible for inherited prion diseases were found to be located in these stem-forming regions on helix H2 and their counterpart on helix H3. Moreover, the volume effect of the nonstem domain, which contains ~200 residues, was deduced to be a determinant of the nature of the association such as oligomerization, because the stem-forming domain is only a small part of a prion protein. Taken together, we conclude that the mechanism underlying the initial stage of amyloidogenesis is the exposure of a newly formed intramolecular ß-sheet to a solvent through the partial transition of a native structure from an α-helix to a ß-structure. Our results also demonstrate that prion diseases caused by major prion proteins except the prions of some fungi such as yeast are inherent only in mammals, as evidenced by a comparison of the corresponding sequences to the stem-forming regions among different animals.

Acceleration of disulfide-coupled protein folding using glutathione derivatives.

Protein folding occurs simultaneously with disulfide bond formation. In general, the in vitro folding of proteins containing disulfide bond(s) is carried out in the presence of redox reagents, such as glutathione, to permit native disulfide pairing to occur. It is well known that the formation of a disulfide bond and the correct tertiary structure of a target protein are strongly affected by the redox reagent used. However, little is known concerning the role of each amino acid residue of the redox reagent, such as glutathione. Therefore, we prepared glutathione derivatives - glutamyl-cysteinyl-arginine (ECR) and arginyl-cysteinyl-glycine (RCG) - and examined their ability to facilitate protein folding using lysozyme and prouroguanylin as model proteins. When the reduced and oxidized forms of RCG were used, folding recovery was greater than that for a typical glutathione redox system. This was particularly true when high protein concentrations were employed, whereas folding recovery using ECR was similar to that of the glutathione redox system. Kinetic analyses of the oxidative folding of prouroguanylin revealed that the folding velocity (K(RCG) = 3.69 × 10(-3) s(-1)) using reduced RCG/oxidized RCG was approximately threefold higher than that using reduced glutathione/oxidized glutathione. In addition, folding experiments using only the oxidized form of RCG or glutathione indicated that prouroguanylin was converted to the native conformation more efficiently in the case of RCG, compared with glutathione. The findings indicate that a positively charged redox molecule is preferred to accelerate disulfide-exchange reactions and that the RCG system is effective in mediating the formation of native disulfide bonds in proteins.

Fiber formation of a synthetic spider peptide derived from Nephila clavata.

Dragline silk is a high-performance biopolymer with exceptional mechanical properties. Artificial spider dragline silk is currently prepared by a recombinant technique or chemical synthesis. However, the recombinant process is costly and large-sized synthetic peptides are needed for fiber formation. In addition, the silk fibers that are produced are much weaker than a fiber derived from a native spider. In this study, a small peptide was chemically synthesized and examined for its ability to participate in fiber formation. A short synthetic peptide derived from Nephila clavata was prepared by a solid-phase peptide method, based on a prediction using the hydrophobic parameter of each individual amino acid residue. After purification of the spider peptide, fiber formation was examined under several conditions. Fiber formation proceeded in the acidic pH range, and larger fibers were produced when organic solvents such as trifluoroethanol and acetonitrile were used at an acidic pH. Circular dichroism measurements of the spider peptide indicate that the peptide has a beta-sheet structure and that the formation of a beta-sheet structure is required for the spider peptide to undergo fiber formation.

Recognition of the N-terminal histone H2A and H3 peptides by peptidylarginine deiminase IV.

Peptidylarginine deiminase IV (PAD4) catalyzes the conversion of an Arg residue to a citrulline residue in various proteins. In particular, citrullination of histone subunits, such as H2A and H3, by PAD4 is thought to be related to rheumatoid arthritis. However, the details of the citrullination mechanism of histone H2A and H3 are not yet well known. Moreover, the effects of N-terminal acetylation on histone subunits with respect to PAD4 recognition have not yet been studied. To further study the mechanism of PAD4 recognition of histone H2A and H3 subunits, a series of the N-terminal peptides was chemically synthesized and the citrullination sites were identified using MALDI-TOF/MS. N-terminal acetylation of histone H2A was not significant with respect to PAD4 recognition in vitro, but the acetylation of H3 peptide had a significant effect on PAD4 recognition in vitro, resulting in predominant citrullination at the Arg2 residue.

Interaction-based evaluation of the propensity for amyloid formation with cross-beta structure.

In order to reveal the requirements for amino acid sequences prone to form amyloid fibrils, a novel prediction method based on the original structural model of amyloids was developed. As a working hypothesis, two fundamental conditions were introduced into the design of the present system for the evaluation of the propensity for amyloidogenicity. The first of these two conditions was to ensure that the hydrophobic and hydrogen-bonding interactions between residues on neighboring antiparallel beta-strands were formed along a fibril axis. The other condition was that the hydrophobic interacting residues appeared on both faces of the protofibril, which gave line-matching interactions. Most peptides with sequences exhibiting high scores, as evaluated by this method, were found to easily form amyloids with the aid of a turn-inducing structure designed as a connection of two beta-strands. On the other hand, peptides with low-scoring native sequences and those modified by an internal residue-residue exchange (the latter yielding a null score) did not lead to amyloid formation. These data demonstrated the validity of this method for the prediction of amyloid structures. Moreover, the present study provided support for the proposed model of the essential structure associated with the above working hypothesis. The predicted high-scoring regions were in good agreement with the putative amyloid core regions reported thus far.

Peripheral region for core cross-beta plays important role in amyloidogenicity.

The role of the peripheral sequence neighboring the core cross-beta region was investigated using a peptide library constructed with all possible combinations of Lys, Glu, Ser, and Leu at three residue positions (X1-X3) forming the N-terminal region linked to the amyloid core sequence of the barnase-derived segment (A4-K22). By means of CD spectra and thioflavin T binding assay for 64 peptides, not only the composition but also the sequence in the peripheral region were found to be responsible for amyloid formation. The preferences of amino acid residues in the peripheral region of the amyloid-forming peptides were in the order of Leu approximately SerGlu>>Lys. A balance of positive and negative charges was found to be essential for amyloid formation, suggesting that the electrostatic interaction at the surface of the amyloid fibrils is relevant to their stability. On the basis of the maximum fluorescence wavelength of fibril-bound thioflavin T, the highly amyloidogenic peptides were classified into two classes, which exhibited the sequence preferences of (Leu, Ser/Glu, and Leu) and (Glu, Leu, and Ser) for the peripheral sequence (X1, X2, and X3). The former class can be rationally assigned to the structural model with deep grooves along the fibril axis. Thus, the peripheral sequence regulates the manner of molecular packing in the fibrils as well as the amyloidogenicity. In addition, the chains of the peripheral sequence are most likely to form thioflavin T binding sites.

Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains.

Various mutants of the protein fragment, barnase module-1 (1-24) were investigated in order to reveal the structural principle of amyloid-like fibrils. By means of circular dichroism spectroscopy, X-ray diffraction, electron microscopy, and thioflavin T binding assay, we found that the molecules containing two beta-strands and an intervening turn structure are assembled to form a cross-beta structure. Stabilization by both the hydrophobic interactions and hydrogen bonding between the respective paired side-chains on the coupled beta-strands was essential for fibril formation. These two types of interaction can also arrange the corresponding residues in lines on both sheet surfaces of protofilaments with a cross-beta structure. This leads to the most probable fibril structure constructed with the line-matching interactions between protofilaments. Consideration of the geometrical symmetry resulted in our finding that a limited number of essential models for molecular packing in fibril structure are stable, which would rationally explain the occurrence of two or three morphologies from an identical molecular species. The ribbon-like fibrils exhibited striped texture along the axis, which was assigned to a stacked two-sheet repeat as a structural unit. The comprehensively proposed structural model, that is, the sheet-sheet interaction between left-handed cross-beta structures, results in a slightly right-handed twist of beta-sheet stacking, which reasonably elucidates the intrinsic sizes of the fibril width and its helical period along the fibril axis, as the bias in the orientation of the hydrogen-bonded beta-strand pair at the lateral edge is larger than that at the central protofilament.