Assessing a pharmacist provided mental health screening service in a rural community to address anxiety and depression.

BACKGROUND: The current state of the mental health crisis has been a topic of discussion around the nation, with those in rural communities being at a particularly higher risk. Community pharmacists are uniquely positioned to screen patients for mental health disorders as well as provide education and patient monitoring following medication changes by prescribers. OBJECTIVE: The objective of this study is to assess mental health screening outcomes provided by rural community pharmacists. METHODS: This retrospective evaluation of a pilot project describes a behavioral health service. Eligible patients were 18 years of age or older, taking one or more mental health medications and covered by the specific Medicaid health plan. Participating pharmacies were those that had a significant patient population participating with that plan, as well as credentialed and trained pharmacists. Pharmacists performed telehealth visits with eligible patients where they confirmed their mental health diagnosis and medications. Based on patient confirmed diagnosis a GAD-7 or PHQ-9 test was administered. The pharmacists then made recommendations to the patients or their prescribers and created a plan with the patient for implementation based on their score. Follow-up calls were conducted to re-administer the appropriate test to identify changes in mental health scores. RESULTS: There were 61 patients who participated in the services across four pharmacies. Mean GAD-7 scores were 8.1 at initial appointment and 6.4 at follow-up (N=24). Mean PHQ-9 scores were 11.2 initially and 10 at follow up (N=37). CONCLUSION: This implementation project supports the creation of additional mental health services in the community pharmacy setting to reinforce and encourage follow up provider visits in areas where there are mental health provider shortages and may possibly improve patient outcomes.

Better together: utilizing an interprofessional course and escape room to educate healthcare students about opioid use disorder.

BACKGROUND: The aim of the present study was to determine the impact of an innovative interprofessional educational activity on healthcare professional students' learning. The educational activity targeted student knowledge of opioid use disorder (OUD) and perceptions of working with an interprofessional team while caring for patients with OUD. METHODS: Students from nursing, pharmacy, physician assistant, dentistry, social work, and medicine programs were recruited to participate in the interprofessional educational activity. The educational experience included seven asynchronous modules and a virtual synchronous escape room. Prior to the educational programming, participants completed a pre-survey that assessed their knowledge and attitudes towards working on an interprofessional team and perceptions of patients with OUD. The asynchronous modules were required in order to participate in the escape room and each module contained its own pre/post quiz to assess student knowledge. RESULTS: A total of 402 students participated in the course. Prior to participating in the course, students disagreed that they had extensive educational experience with SUD (2.45 ± 0.79). The students displayed significant improvement in the knowledge based areas after completing the seven asynchronous modules. The largest significant area of knowledge-based improvement was seen in treatment of OUD where on the pre-quiz 65.54 ± 20.21% were answered correctly compared to 95.97 ± 9.61% on the post-quiz. Participation in the escape room significantly changed the students' perceptions of working in interprofessional teams while managing patients with OUD. Of the eleven perception variables assessed, seven showed a significant increase in the post-survey. Following the escape room, participants also strongly agreed that they now would refer patients to colleagues in other disciplines. CONCLUSIONS: An interprofessional educational experience including both an asynchronous course and virtual synchronous escape room can increase participant knowledge around OUD and may improve student perceptions of working with an interprofessional team and caring for patients with OUD.

Characterization of Schizosaccharomyces pombe malate permease by expression in Saccharomyces cerevisiae.

In Saccharomyces cerevisiae, L-malic acid transport is not carrier mediated and is limited to slow, simple diffusion of the undissociated acid. Expression in S. cerevisiae of the MAE1 gene, encoding Schizosaccharomyces pombe malate permease, markedly increased L-malic acid uptake in this yeast. In this strain, at pH 3.5 (encountered in industrial processes), L-malic acid uptake involves Mae1p-mediated transport of the monoanionic form of the acid (apparent kinetic parameters: Vmax = 8.7 nmol/mg/min; Km = 1.6 mM) and some simple diffusion of the undissociated L-malic acid (Kd = 0.057 min(-1)). As total L-malic acid transport involved only low levels of diffusion, the Mae1p permease was further characterized in the recombinant strain. L-Malic acid transport was reversible and accumulative and depended on both the transmembrane gradient of the monoanionic acid form and the DeltapH component of the proton motive force. Dicarboxylic acids with stearic occupation closely related to L-malic acid, such as maleic, oxaloacetic, malonic, succinic and fumaric acids, inhibited L-malic acid uptake, suggesting that these compounds use the same carrier. We found that increasing external pH directly inhibited malate uptake, resulting in a lower initial rate of uptake and a lower level of substrate accumulation. In S. pombe, proton movements, as shown by internal acidification, accompanied malate uptake, consistent with the proton/dicarboxylate mechanism previously proposed. Surprisingly, no proton fluxes were observed during Mae1p-mediated L-malic acid import in S. cerevisiae, and intracellular pH remained constant. This suggests that, in S. cerevisiae, either there is a proton counterflow or the Mae1p permease functions differently from a proton/dicarboxylate symport.

Distribution of the flocculation protein, flop, at the cell surface during yeast growth: the availability of flop determines the flocculation level.

The yeast FLO genes encode cell surface proteins which are expected to play a major role in the control of flocculation. We have assessed the availability of the Flo proteins at the cell surface during the growth of two flocculent strains, ABXL-1D (FLO1) and STX347-1D (FLO5) using immunological approaches, enzyme-linked immunosorbent assays and immunofluorescence. Our data show that they are not permanently present at the cell surface but that their amount increases during growth. With both strains the flocculation level is tightly correlated to the amount of Flop antigen detected, suggesting that it is the availability of the Flo proteins at the cell surface which determines the flocculation level. Our data are consistent with the idea that the Flo proteins correspond to the flocculation lectins. The differences of flocculation pattern among strains could originate from variations in the regulation of the expression of the FLO genes. Monitoring of the distribution of the Flo proteins during cellular development revealed that they are incorporated essentially in the cell wall of growing buds. Incorporation of the Flo proteins in the cell wall displays a highly polarized aspect, at the bud tip and at the mother-daughter neck junction, which can persist in mature cells. Such a localization could be relevant to constraints of the cell wall incorporation of the mannoproteins. Depending on the regulation of Flop expression and on the incorporation of the proteins in the cell wall, a yeast population can be highly heterogeneous in Flo protein equipment.

Localization and cell surface anchoring of the Saccharomyces cerevisiae flocculation protein Flo1p.

The Saccharomyces cerevisiae FLO1 gene encodes a large 1,536-amino-acid serine- and threonine-rich protein involved in flocculation. We have assessed the localization of Flo1p by immunoelectron microscopy, and in this study we show that this protein is located in the external mannoprotein layer of the cell wall, at the plasma membrane level and in the periplasm. The protein was also visualized in the endoplasmic reticulum and in the nuclear envelope, indicating that it was secreted through the secretory pathway. The protein was detected by Western blotting in cell wall extracts as a high-molecular-mass (>200 kDa) polydisperse material obviously as a result of extensive N and probably O glycosylation. Flo1p was extracted from cell walls in large amounts by boiling in sodium dodecyl sulfate, suggesting that it is noncovalently anchored to the cell wall network. The membranous forms of Flo1p were shown to be solubilized by phosphatidylinositol-phospholipase C treatment, suggesting that Flo1p is glycosyl phosphatidylinositol (GPI) anchored to this organelle. The expression of truncated forms with the hydrophobic C-terminal domain deleted led to the secretion of the protein in the culture medium. The hydrophobic C terminus, which is a putative GPI anchoring domain, is therefore necessary for the attachment of Flo1p in the cell wall. Deletion analysis also revealed that the N-terminal domain of Flo1p was essential for cellular aggregation. On the whole, our data indicate that Flo1p is a true cell wall protein which plays a direct role in cell-cell interaction.

Metabolic analysis of S. cerevisiae strains engineered for malolactic fermentation.

A complete malolactic fermentation was achieved using Saccharomyces cerevisiae strains coexpressing the genes mleS and mae1 coding for the Lactococcus lactis malolactic enzyme and the Schizosaccharomyces pombe malate permease under the control of yeast promoters. The expression level of mae1 greatly influences the kinetics of the reaction by controlling the rate of malate uptake meanwhile a high expression level of mleS induces a partial consumption of malate derived from glucose by the malolactic enzyme. A strain expressing several copies of mae1 and one copy of mleS degrades 3 g/l of malate almost exclusively through the malolactic pathway in 4 days under enological conditions, without metabolic side effects.

The Saccharomyces cerevisiae FLO1 flocculation gene encodes for a cell surface protein.

The sequencing of a 6619 bp region encoding for a flocculation gene previously cloned from a strain defined as FLO5 (Bidard et al., 1994) has revealed that it was a FLO1 gene. The FLO1 gene product has been localized at the cell surface of the yeast cell by immunofluorescent microscopy. The Flo1 protein contains four regions with repeated sequences which account for about 70% of the amino acids of this protein. A functional analysis of the major repeated region has revealed that it plays an important role in determining the flocculation level. A gene disruption experiment has shown that FLO5 strain STX 347-1D contains at least two flocculation genes of the FLO1 type but that they are supposed to be inactive and do not contribute to its flocculation. However, enzyme-linked immunosorbent assays performed on intact cells have revealed that a protein expressed at the cell surface of the FLO5 strain STX 347-1D is antigenically related to Flo1p. A deletion analysis of the 5' region of the FLO1 gene has shown that the expression is submitted to controls which depend on the genetic background of the strain.