The construct validity and reliability of the Turkish version of Spreitzer's psychological empowerment scale

<p>Abstract</p> <p>Background</p> <p>Today, many organizations have adopted some kind of empowerment initiative for at least part of their workforce. Over the last two decades, two complementary perspectives on empowerment at work have emerged: structural and psychological empowerment. Psychological empowerment is a motivational construct manifested in four cognitions: meaning, competence, self-determination and impact. The aim of this article is to examine the construct validity and reliability of the Turkish translation of Spreitzer's psychological empowerment scale in a culturally diverse environment.</p> <p>Methods</p> <p>The scale contains four dimensions over 12 statements. Data were gathered from 260 nurses and 161 physicians. The dimensionality of the scale was evaluated by exploratory factor analyses. To investigate the multidimensional nature of the empowerment construct and the validity of the scale, first- and second-order confirmatory factor analysis was conducted. Furthermore, Cronbach alpha coefficients were assessed to investigate reliability.</p> <p>Results</p> <p>Exploratory factor analyses revealed that four factors in both solutions. The first- and second-order factor analysis indicated an acceptable fit between the data and the theoretical model for nurses and physicians. Cronbach alpha coefficients varied between 0.81-0.94 for both groups, which may be considered satisfactory.</p> <p>Conclusions</p> <p>The analyses indicated that the psychometric properties of the Turkish version of the scale can be considered satisfactory.</p

Effects of work ability and health promoting interventions for women with musculoskeletal symptoms: A 9-month prospective study

<p>Abstract</p> <p>Background</p> <p>Women working in the public human service sector in 'overstrained' situations run the risk of musculoskeletal symptoms and long-term sick leave. In order to maintain the level of health and work ability and strengthen the potential resources for health, it is important that employees gain greater control over decisions and actions affecting their health – a process associated with the concept of self-efficacy. The aim of this study was to describe the effects of a self-efficacy intervention and an ergonomic education intervention for women with musculoskeletal symptoms, employed in the public sector.</p> <p>Methods</p> <p>The design of the study was a 9-month prospective study describing the effects of two interventions, a comprehensive self-efficacy intervention (<it>n </it>= 21) and an ergonomic education intervention (<it>n </it>= 21). Data were obtained by a self-report questionnaire on health- and work ability-related factors at baseline, and at ten weeks and nine months follow-up. Within-group differences over time were analysed.</p> <p>Results</p> <p>Over the time period studied there were small magnitudes of improvements within each group. Within the self-efficacy intervention group positive effects in perceived work ability were shown. The ergonomic education group showed increased positive beliefs about future work ability and a more frequent use of pain coping strategies.</p> <p>Conclusion</p> <p>Both interventions showed positive effects on women with musculoskeletal symptoms, but in different ways. Future research in this area should tailor interventions to participants' motivation and readiness to change.</p

The Arg233Lys AQP0 Mutation Disturbs Aquaporin0-Calmodulin Interaction Causing Polymorphic Congenital Cataract

Calmodulin (CaM) directly interacts with the aquaporin 0 (AQP0) C-terminus in a calcium dependent manner to regulate the water permeability of AQP0. We previously identified a missense mutation (p.R233K) in the putative CaM binding domain of AQP0 C-terminus in a congenital cataract family. This study was aimed at exploring the potential pathogenesis of this mutation causative of cataract and mainly identifying how it influenced the binding of AQP0 to CaM. Wild type and R233K mutant AQP0 with EGFP-tag were transfected separately into Hela cells to determine the expression and subcellular localizations. The co-immunoprecipitation (CoIP) assay was used to detect the interaction between AQP0 and CaM. AQP0 C-terminus peptides were synthesized with and without R233K, and the binding abilities of these peptides to CaM were assessed using a fluorescence binding assay. Localizations of wild type and R233K mutant AQP0 were determined from EGFP fluorescence, and the chimeric proteins were both localized abundantly in the plasma membrane. Protein expression levels of the culture cells showed no significant difference between them. The results from CoIP assay implied that R233K mutant presented more weakly in association with CaM than wild type AQP0. The AQP0 C-terminal mutant peptide was found to have 2.5-fold lower binding affinity to CaM than wild type peptide. These results suggested that R233K mutation did not affect the expression, location and trafficking of the protein but did influence the interaction between AQP0 and CaM. The binding affinity of AQP0 C-terminus to CaM was significantly reduced. Due to lack of the modulation of the Ca2+-calmodulin complex, the water permeability of AQP0 was subsequently augmented, which might lead to the development of this cataract

Absence of mutations in four genes encoding for congenital cataract and expressed in the human brain in Tunisian families with cataract and mental retardation

<p>Abstract</p> <p>Background</p> <p>To identify the genetic defect associated with autosomal recessive congenital cataract (ARCC), mental retardation (MR) and ARCC, MR and microcephaly present in most patients in four Tunisian consanguineous families.</p> <p>Methods</p> <p>We screened four genes implicated in congenital cataract by direct sequencing in two groups of patients; those affected by ARCC associated to MR and those who presented also microcephaly. Among its three genes <it>PAX6</it>, <it>PITX3 </it>and <it>HSF4 </it>are expressed in human brain and one gene <it>LIM2 </it>encodes for the protein MP20 that interact with the protein galectin-3 expressed in human brain and plays a crucial role in its development. All genes were screened by direct sequencing in two groups of patients; those affected by ARCC associated to MR and those who presented also microcephaly.</p> <p>Results</p> <p>We report no mutation in the four genes of congenital cataract and its flanking regions. Only variations that did not segregate with the studied phenotypes (ARCC associated to MR, ARCC associated with MR and microcephaly) are reported. We detected three intronic variations in <it>PAX6 </it>gene: IVS4 -274insG (intron 4), IVS12 -174G>A (intron12) in the four studied families and IVS4 -195G>A (intron 4) in two families. Two substitutions polymorphisms in <it>PITX3 </it>gene: c.439 C>T (exon 3) and c.930 C>A (exon4) in one family. One intronic variation in <it>HSF4 </it>gene: IVS7 +93C>T (intron 7) identified in one family. And three intronic substitutions in <it>LIM2 </it>gene identified in all four studied families: IVS2 -24A>G (intron 2), IVS4 +32C>T (intron 4) and c.*15A>C (3'-downstream sequence).</p> <p>Conclusion</p> <p>Although the role of the four studied genes: <it>PAX6</it>, <it>PITX3</it>, <it>HSF4 </it>and <it>LIM2 </it>in both ocular and central nervous system development, we report the absence of mutations in all studied genes in four families with phenotypes associating cataract, MR and microcephaly.</p

Universal DNA methylation age across mammalian tissues.

Aging, often considered a result of random cellular damage, can be accurately estimated using DNA methylation profiles, the foundation of pan-tissue epigenetic clocks. Here, we demonstrate the development of universal pan-mammalian clocks, using 11,754 methylation arrays from our Mammalian Methylation Consortium, which encompass 59 tissue types across 185 mammalian species. These predictive models estimate mammalian tissue age with high accuracy (r > 0.96). Age deviations correlate with human mortality risk, mouse somatotropic axis mutations and caloric restriction. We identified specific cytosines with methylation levels that change with age across numerous species. These sites, highly enriched in polycomb repressive complex 2-binding locations, are near genes implicated in mammalian development, cancer, obesity and longevity. Our findings offer new evidence suggesting that aging is evolutionarily conserved and intertwined with developmental processes across all mammals

Analysis of Familial Hemophagocytic Lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cells

Natural killer (NK) cell secretory lysosome exocytosis and cytotoxicity are impaired in familial hemophagocytic lymphohistiocytosis type 4 (FHL-4), a disorder caused by mutations in the gene encoding the SNARE protein syntaxin 11. We show that syntaxin 11 binds to SNAP23 in NK cells and that this interaction is reduced by FHL-4 truncation and frameshift mutation proteins that delete all or part of the SNARE domain of syntaxin 11. In contrast the FHL-4 mutant proteins bound to the Sec-1/Munc18-like (SM) protein Munc18-2. We demonstrate that the C-terminal cysteine rich region of syntaxin 11, which is deleted in the FHL-4 mutants, is S-acylated. This posttranslational modification is required for the membrane association of syntaxin 11 and for its polarization to the immunological synapse in NK cells conjugated to target cells. Moreover, we show that Munc18-2 is recruited by syntaxin 11 to intracellular membranes in resting NK cells and to the immunological synapse in activated NK cells. This recruitment of Munc18-2 is abolished by deletion of the C-terminal cysteine rich region of syntaxin 11. These results suggest a pivotal role for S-acylation in the function of syntaxin 11 in NK cells

Author Correction: Universal DNA methylation age across mammalian tissues

Correction to: Nature Aging, published online 10 August 2023. In the version of Supplementary Data initially published with this article, data were missing from Table S1.13 (Updated AnAge version in Class Mammalia), which now appear in an updated Supplementary Data file in the online version of the article

The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex

Major histocompatibility complex (MHC) class I complexes present peptides from both self and foreign intracellular proteins on the surface of most nucleated cells. The assembled heterotrimeric complexes consist of a polymorphic glycosylated heavy chain, non-polymorphic β2 microglobulin, and a peptide of typically nine amino acids in length. Assembly of the class I complexes occurs in the endoplasmic reticulum and is assisted by a number of chaperone molecules. A multimolecular unit termed the peptide-loading complex (PLC) is integral to this process. The PLC contains a peptide transporter (transporter associated with antigen processing), a thiooxido-reductase (ERp57), a glycoprotein chaperone (calreticulin), and tapasin, a class I-specific chaperone. We suggest that class I assembly involves a process of optimization where the peptide cargo of the complex is edited by the PLC. Furthermore, this selective peptide loading is biased toward peptides that have a longer off-rate from the assembled complex. We suggest that tapasin is the key chaperone that directs this action of the PLC with secondary contributions from calreticulin and possibly ERp57. We provide a framework model for how this may operate at the molecular level and draw parallels with the proposed mechanism of action of human leukocyte antigen-DM for MHC class II complex optimization