Closing the digital divide: Developing a platform to conduct training, outreach, and education for employment skills.

El Paso, Texas, like many communities along the United States/Mexico border, suffers from a lack of access to many social determinants of health, especially in low-income neighborhoods. These long-standing problems have only been exacerbated by the COVID-19 pandemic. The Texas Tech University Health Sciences Center El Paso Health Education and Awareness Team (EP-HEAT) is an organization that was established with a focus on disseminating health information to the community. EP-HEAT received funding from Microsoft Corporation to facilitate technology education workshops for underserved populations. These workshops were held in English and Spanish and attempted to improve social determinants of health in the community which can be negatively exacerbated by a lack of digital inclusion. Community members who attended workshops completed a LinkedIn Learning Path, or both were offered an anonymous post-course survey with a mixed method questionnaire on how their knowledge of basic technology or job skills was improved by engaging with the provided workshops and learning paths. Overall, 80% of community members who participated in the workshops reported learning a new skill, and 91% of participants who started a LinkedIn Learning Path were able to finish. The workshops were well received by the community and highlighted the potential for these programs to enhance digital skills and upward workforce mobility.

Efficacy of Video-Based Forearm Anatomy Model Instruction for a Virtual Education Environment.

INTRODUCTION: As virtual education becomes more widespread, particularly considering the recent COVID-19 pandemic, studies that assess the impact of online teaching strategies are vital. Current anatomy curriculum at Paul L. Foster School of Medicine consists of self-taught PowerPoint material, clinical vignette-centered team-based learning (dry lab), and prosection-based instruction (wet lab). This study examined the impact of video-based muscle model (VBMM) instruction using a student-designed forearm muscle model on anatomy quiz scores and student perceptions of its effectiveness with regards to learning outcomes. METHODS: Students divided into Group 1 (54 students) and Group 2 (53 students) were assessed prior to and following a 3.5-minute video on anterior forearm compartment musculature using the muscle model. Group 1 began by completing a pretest, then received VBMM instruction, and then completed a posttest prior to participating in the standard dry lab and 1 hour wet lab. Group 2 completed the wet lab, then received the pretest, VBMM instruction, and posttest prior to participating in the dry lab. Both groups took an identical five-question quiz covering locations and functions of various anterior forearm muscles each time. RESULTS: Mean scores were higher than no formal intervention with exposure to VBMM instruction alone (0.73 points, P = .01), wet lab alone (0.88 points, P = .002), and wet lab plus VBMM instruction (1.35 points, P= <.001). No significant difference in scores was found between instruction with VBMM versus wet lab alone (P = 1.00), or between either instruction method alone compared to a combination of the two methods (P = .34, .09). Student survey opinions on the VBMM instruction method were positive. CONCLUSION: VBMM instruction is comparable to prosection-based lab with regards to score outcomes and was well received by students as both an independent learning tool and as a supplement to cadaveric lab. When compared to either instruction method alone, the supplementation of VBMM with cadaveric prosection instruction was best. VBMM instruction may be valuable for institutions without access to cadaveric specimens, or those looking to supplement their current anatomy curriculum.

Histological investigation of human glaucomatous eyes: Extracellular fibrotic changes and galectin 3 expression in the trabecular meshwork and optic nerve head.

Glaucoma is a leading cause of irreversible vision loss and is associated with fibrotic changes in two ocular tissues-the optic nerve head (ONH) and trabecular meshwork (TM). We investigated the differences in extracellular matrix components (ECM) including collagen, elastin, transforming growth factor beta-2, type-II receptor (TGFßRII) and Galectin3 (Gal3) in the glaucomatous human eyes to quantify fibrotic changes in ONH and TM. Glaucomatous and control human donor eyes were prepared for chemical and immunological staining to quantify ECM protein expression in the TM and ONH. Chemical staining included: Trichrome (collagen), Vernhoeff-Van Giesen (elastin) and Sirius Red (collagen). Immunohistochemistry was used to determine levels of Gal3 and TGFß2RII. Quantitative analyses were performed using Image J software. Student's t-test was used to compare groups and Pearson's test was used to determine correlations P-values of 0.05 (or less) were considered statistically significant. Deposition of ECM proteins was elevated in glaucomatous tissues. There was increased collagen (P = 0.0469), Gal3 (P < 0.0001) and TGFß2RII (P = 0.0005) in the TM of glaucomatous eyes. Likewise, collagen (P = 0.0517) and Galectin3 (P = 0.041) were increased in the ONH glaucomatous eyes. There was a correlation of TGFßRII with Gal3 in the TM (P < 0.0001) and optic nerve (P = 0.0003). The TM and ONH of glaucomatous eyes showed increased expression of ECM proteins supporting a fibrotic pathology. Galectin3 and TGFß-2R II showed a positive correlation in TM and optic nerve supporting co-localization and suggesting their potential role in the glaucoma fibrotic process. Clin. Anat. 31:1031-1049, 2018. © 2018 The Authors. Clinical Anatomy published by Wiley Periodicals, Inc. on behalf of American Association of Clinical Anatomists.

Cellular fibronectin expression in human trabecular meshwork and induction by transforming growth factor-ß2.

PURPOSE: Levels of TGF-ß2 are higher in POAG aqueous humor, causing deposition of extracellular matrix (ECM) proteins, including fibronectin (FN), in the glaucomatous human trabecular meshwork (HTM) that may be responsible for elevated IOP. The purpose of this study was to identify the expression of cellular FN (cFN) isoforms (EDA and EDB) in HTM cells and tissues, and to determine whether TGF-ß2 can induce cFN expression and fibril formation in cultured HTM cells. METHODS: Expression of cFN mRNA isoforms and induction by recombinant TGF-ß2 (5 ng/mL) were determined by quantitative RT-PCR. The TGF-ß2 induction of EDA isoform protein expression and FN fibril formation were analyzed using Western immunoblots and immunocytochemistry (ICC), respectively. Immunohistochemistry (IHC) analysis was used to examine total FN and EDA isoform expression in normal (NTM) and glaucomatous (GTM) trabecular meshwork (TM) tissues. RESULTS: Both cFN mRNA isoforms were expressed in cultured HTM cells and were induced by TGF-ß2 after 2, 4, and 7 days (P < 0.05). Similarly, EDA isoform protein and fibril formation were increased after 4 and 7 days of TGF-ß2 treatment. Finally, GTM tissues had significantly greater EDA isoform protein levels (1.7-fold, P < 0.05) compared to NTM tissues. CONCLUSIONS: This study demonstrated that cFN isoforms are expressed and induced in HTM cells by TGF-ß2. Also, increased EDA isoform protein levels were seen in GTM tissues. Our findings suggest that induction of cFN isoform expression in the TM ECM may be a novel pathologic mechanism involved in the TM changes associated with glaucoma.

Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger.

Sodium/calcium (Na(+)/Ca(2+)) exchangers (NCX) are membrane transporters that play an essential role in maintaining the homeostasis of cytosolic Ca(2+) for cell signaling. We demonstrated the Na(+)/Ca(2+)-exchange function of an NCX from Methanococcus jannaschii (NCX_Mj) and report its 1.9 angstrom crystal structure in an outward-facing conformation. Containing 10 transmembrane helices, the two halves of NCX_Mj share a similar structure with opposite orientation. Four ion-binding sites cluster at the center of the protein: one specific for Ca(2+) and three that likely bind Na(+). Two passageways allow for Na(+) and Ca(2+) access to the central ion-binding sites from the extracellular side. Based on the symmetry of NCX_Mj and its ability to catalyze bidirectional ion-exchange reactions, we propose a structure model for the inward-facing NCX_Mj.