Sharing Stories Of Development: How School Leaders Perceive Developing A Trauma-Informed School

ABSTRACT This narrative inquiry explored how educational leaders perceive the development of a trauma-informed school. A trauma-informed school acknowledges the impact of trauma and responds by integrating effective practices, programs, and procedures to build resilience. The problem addressed by this study is, with rising numbers of adverse childhood experiences (ACEs), school staff lack targeted skills to help students mitigate trauma. Further, this qualitative study fills the gap in literature by providing the lived experiences of educational leaders in developing trauma-informed schools. Through narrative research, semistructured interviews which lasted up to 60 minutes were individually conducted with five educational leaders who worked in trauma-informed schools in Maine. Data analysis included restorying the interview transcripts and data coding. Each narrative was sent to participants for member checking to ensure accuracy. Restoried narratives were examined in depth and revealed the following themes: Connections, Readiness for Change, and Availability of Time. Key findings showed connections are the foundation of a trauma-informed school to foster belonging. Readiness for change among staff is necessary for professional development to be meaningful, and time is essential to engage in the work. Success is measured by whole-child well-being over test scores. Implications suggest a collaborative, whole-school approach may promote a student’s daily resilience

Alien Registration- Cyr, Andrew L. (Pittston, Kennebec County)

https://digitalmaine.com/alien_docs/16638/thumbnail.jp

Stereociliary Myosin-1c Receptors Are Sensitive to Calcium Chelation and Absent from Cadherin 23 Mutant Mice

The identities of some of the constituents of the hair-cell transduction apparatus have been elucidated only recently. The molecular motor myosin-1c (Myo1c) functions in adaptation of the hair-cell response to sustained mechanical stimuli and is therefore an integral part of the transduction complex. Recent data indicate that Myo1c interacts in vitro with two other molecules proposed to be important for transduction: cadherin 23 (Cdh23), a candidate for the stereociliary tip link, and phosphatidylinositol 4,5-bisphosphate (PIP2), which is abundant in the membranes of hair-cell stereocilia. It is not known, however, whether these interactions occur in hair cells. Using an in situ binding assay on saccular hair cells, we demonstrated previously that Myo1c interacts with molecules at stereociliary tips, the site of transduction, through sequences contained within its calmodulin (CaM)-binding neck domain, which can bind up to four CaM molecules. In the current study, we identify the second CaM-binding IQ domain as a region of Myo1c that mediates CaM-sensitive binding to stereociliary tips and to PIP2 immobilized on a solid support. Binding of Myo1c to stereociliary tips of cochlear and vestibular hair cells is disrupted by treatments that break tip links. In addition, Myo1c does not bind to stereocilia from mice whose hair cells lack Cdh23 protein despite the presence of PIP2 in the stereociliary membranes. Collectively, our data suggest that Myo1c and Cdh23 interact at the tips of hair-cell stereocilia and that this interaction is modulated by CaM

Does level of training Influence the ability to detect hepatosplenomegaly in children with leukemia?

Background: Children with leukemia often have hepatosplenomegaly present. This can be diagnosed with physical examination and confirmed with ultrasound. We sought to determine if level of training influenced the ability to detect hepatosplenomegaly. Methods: All children diagnosed with leukemia during the past 5 years were reviewed. The training level of the examiner, the documentation of hepatosplenomegaly, and the ultrasound findings were collected and analyzed. Results: There were 245 examinations of the spleen and 254 of the liver. Splenomegaly was correctly diagnosed by medical students 54% of the time, by residents 81%, and by staff 79% of the time. First year residents diagnosed it correctly 68% of the time, R2s 64%, R3s 76% and R4s 86% of the time. Hepatomegaly was correctly diagnosed by medical students 44% of the time, by residents 73% and by staff 68% of the time. First year residents diagnosed it correctly 77% of the time, R2s 54%, R3s 81% and R4s 75% of the time. Conclusions: Pediatric residents had the best ability to detect hepatosplenomegaly, and were better than staff and medical students, although this was not statistically significant

Calmodulin binding to recombinant myosin-1c and myosin-1c IQ peptides

BACKGROUND: Bullfrog myosin-1c contains three previously recognized calmodulin-binding IQ domains (IQ1, IQ2, and IQ3) in its neck region; we identified a fourth IQ domain (IQ4), located immediately adjacent to IQ3. How calmodulin binds to these IQ domains is the subject of this report. RESULTS: In the presence of EGTA, calmodulin bound to synthetic peptides corresponding to IQ1, IQ2, and IQ3 with K(d )values of 2–4 μM at normal ionic strength; the interaction with an IQ4 peptide was much weaker. Ca(2+ )substantially weakened the calmodulin-peptide affinity for all of the IQ peptides except IQ3. To reveal how calmodulin bound to the linearly arranged IQ domains of the myosin-1c neck, we used hydrodynamic measurements to determine the stoichiometry of complexes of calmodulin and myosin-1c. Purified myosin-1c and T701-Myo1c (a myosin-1c fragment with all four IQ domains and the C-terminal tail) each bound 2–3 calmodulin molecules. At a physiologically relevant temperature (25°C) and under low-Ca(2+ )conditions, T701-Myo1c bound two calmodulins in the absence and three calmodulins in the presence of 5 μM free calmodulin. Ca(2+ )dissociated nearly all calmodulins from T701-Myo1c at 25°C; one calmodulin was retained if 5 μM free calmodulin was present. CONCLUSIONS: We inferred from these data that at 25°C and normal cellular concentrations of calmodulin, calmodulin is bound to IQ1, IQ2, and IQ3 of myosin-1c when Ca(2+ )is low. The calmodulin bound to one of these IQ domains, probably IQ2, is only weakly associated. Upon Ca(2+ )elevation, all calmodulin except that bound to IQ3 should dissociate

Hubble distancing: Focusing on distance measurements in cosmology

The Hubble-Lemaitre tension is currently one of the most important questions in cosmology. Most of the focus so far has been on reconciling the Hubble constant value inferred from detailed cosmic microwave background measurement with that from the local distance ladder. This emphasis on one number -- namely $H_0$ -- misses the fact that the tension fundamentally arises from disagreements of distance measurements. To be successful, a proposed cosmological model must accurately fit these distances rather than simply infer a given value of $H_0$. Using the newly developed likelihood package `distanceladder', which integrates the local distance ladder into MontePython, we show that focusing on $H_0$ at the expense of distances can lead to the spurious detection of new physics in models which change late-time cosmology. As such, we encourage the observational cosmology community to make their actual distance measurements broadly available to model builders instead of simply quoting their derived Hubble constant values.Comment: 21 pages, 8 figure

The role of the UPS in cystic fibrosis

CF is an inherited autosomal recessive disease whose lethality arises from malfunction of CFTR, a single chloride (Cl-) ion channel protein. CF patients harbor mutations in the CFTR gene that lead to misfolding of the resulting CFTR protein, rendering it inactive and mislocalized. Hundreds of CF-related mutations have been identified, many of which abrogate CFTR folding in the endoplasmic reticulum (ER). More than 70% of patients harbor the ΔF508 CFTR mutation that causes misfolding of the CFTR proteins. Consequently, mutant CFTR is unable to reach the apical plasma membrane of epithelial cells that line the lungs and gut, and is instead targeted for degradation by the UPS. Proteins located in both the cytoplasm and ER membrane are believed to identify misfolded CFTR for UPS-mediated degradation. The aberrantly folded CFTR protein then undergoes polyubiquitylation, carried out by an E1-E2-E3 ubiquitin ligase system, leading to degradation by the 26S proteasome. This ubiquitin-dependent loss of misfolded CFTR protein can be inhibited by the application of ‘corrector’ drugs that aid CFTR folding, shielding it from the UPS machinery. Corrector molecules elevate cellular CFTR protein levels by protecting the protein from degradation and aiding folding, promoting its maturation and localization to the apical plasma membrane. Combinatory application of corrector drugs with activator molecules that enhance CFTR Cl- ion channel activity offers significant potential for treatment of CF patients