Search

With a median follow-up of 2.5 months, 31 of 34 patients (91%) reported complete or partial improvement of dysphagia, with 3 experiencing dysphagia. 1 Types and percentages of revisional surgical procedures performed Results We identified 35 patients with new-onset dysphagia following fundoplication. [Extracted from the article]

Surgical training has undergone substantial change in the last few decades. As technology and patient complexity continues to increase, demands for novel approaches to ensure competency have arisen. Virtual reality systems augmented with machine learning represents one such approach. The ability to offer on-demand training, integrate checklists, and provide personalized, surgeon-specific feedback is paving the way to a new era of surgical training. Machine learning algorithms that improve over time as they acquire more data will continue to refine the education they provide. Further, fully immersive simulated environments coupled with machine learning analytics provide real-world training opportunities in a safe atmosphere away from the potential to harm patients. Careful implementation of these technologies has the potential to increase access and improve quality of surgical training and patient care and are poised to change the landscape of current surgical training. Herein, we describe the current state of virtual reality coupled with machine learning for surgical training, future directions, and existing limitations of this technology. [ABSTRACT FROM AUTHOR]

Abstract: Objective: To assess insulin resistance postoperatively in patients with (DM) and without (nonDM) a prior diagnosis of diabetes. Research Design and Methods: Following cardiac surgery, 122 nonDM and 33 DM were treated with insulin infusions to obtain glucose levels <110 mg dl−1. Glucose levels, insulin infusion rates, and insulin infusion rate/glucose ratios were calculated to assess insulin resistance. Results: The average blood glucose at insulin drip initiation (209 vs. 173 mg dl−1; P<.001) and during the first 12 h (146 vs. 135 mg dl−1; P<.05) was higher in DM, but during Hours 12–24 glucose levels were not different. The peak (5.7 vs. 4.1 U h−1; P<.001) and average insulin drip rates (3.7 vs. 2.9 U h−1; P<.01) were higher in DM. Insulin resistance (insulin drip rate/glucose ratio) was higher in DM during Hours 1–12 (0.029 vs. 0.022 U h−1 mg−1 dl−1; P<.001), but not during Hours 12–24 (P=.57). To eliminate glucotoxicity as a cause of the insulin resistance, 23 DM patients were pair matched with 23 nonDM patients based first on glucose levels at drip initiation then by body mass index (BMI) and then catecholamine use to maintain blood pressure. The average blood glucose levels, insulin drip rates, and insulin resistance ratios were not significantly different between the pair-matched groups at all time points. Conclusions: When matched for initial glucose levels, insulin resistance is not different between DM and nonDM following cardiac surgery, likely due to the overwhelming stress response. Insulin drip protocols used postoperatively do not have to be modified for those with a prior diagnosis of diabetes. [Copyright &y& Elsevier]

The chemokine receptor CXCR4, a G rotein-coupled receptor (GPCR) capable of heteromerizing with other GPCRs, is involved in many processes, including immune responses, hematopoiesis, and organogenesis. Evidence suggests that CXCR4 activation reduces thrombin/protease-activated receptor 1 (PAR1)- induced impairment of endothelial barrier function. However, the mechanisms underlying cross-talk between CXCR4 and PAR1 are not well-understood. Using intermolecular bioluminescence resonance energy transfer and proximity ligation assays, we found that CXCR4 heteromerizes with PAR1 in the HEK293T expression system and in human primary pulmonary endothelial cells (hPPECs). A peptide analog of transmembrane domain 2 (TM2) of CXCR4 interfered with PAR1:CXCR4 heteromerization. In HTLA cells, the presence of CXCR4 reduced the efficacy of thrombin to induce β-arrestin-2 recruitment to recombinant PAR1 and enhanced thrombin-induced Ca2+ mobilization. Whereas thrombin-induced extracellular signal-regulated protein kinase 1/2 (ERK1/2) phosphorylation occurred more transiently in the presence of CXCR4, peak ERK1/2 phosphorylation was increased when compared with HTLA cells expressing PAR1 alone. CXCR4-associated effects on thrombin- induced b-arrestin-2 recruitment to and signaling of PAR1 could be reversed by TM2. In hPPECs, TM2 inhibited thrombin-induced ERK1/2 phosphorylation and activation of Ras homolog gene family member A. CXCR4 siRNA knockdown inhibited thrombin-induced ERK1/2 phosphorylation. Whereas thrombin stimulation reduced surface expression of PAR1, CXCR4, and PAR1:CXCR4 heteromers, chemokine (CXC motif) ligand 12 stimulation reduced surface expression of CXCR4 and PAR1:CXCR4 heteromers, but not of PAR1. Finally, TM2 dose-dependently inhibited thrombin-induced impairment of hPPEC monolayer permeability. Our findings suggest that CXCR4:PAR1 heteromerization enhances thrombin-induced G protein signaling of PAR1 and PAR1-mediated endothelial barrier disruption. [ABSTRACT FROM AUTHOR]