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INTRODUCTION: This study aimed to examine the educational challenges faced by perfusionists in Japan. Although Japan has over 400 cardiovascular surgery centers, it performs fewer surgeries than by countries such as Germany and the United States. We focused on challenges related to varying caseloads and working conditions. METHODS: We conducted an online survey containing 24 questions using Google Forms from January to June 2022, targeting perfusionists in Japan. The 24-question survey spanned various educational topics and was approved by the Morinomiya University of Medical Sciences Ethics Committee. RESULTS: Responses were received from 129 perfusionists across 77 institutions. Approximately 70% of these centers managed less than 200 cardiopulmonary bypass (CPB) cases per year, with a similar proportion of perfusionists handling under 50 CPB cases annually. Challenges in Japanese perfusionist education include enhancing communication and troubleshooting skills and the need for instructors with a broad teaching experience. CONCLUSIONS: This study emphasizes the significant differences in caseload and work environments for perfusionists among Japanese institutions. Perfusionists, who often work in clinical engineering, have various responsibilities. These findings highlight the need for improved communication, problem-solving skills, and the implementation of modern teaching technologies. Additionally, this study highlights the complexities of training Japanese perfusionists and underscores the need for more practical, technology-driven educational methods. Addressing these issues is crucial for improving Japan's healthcare standards and could influence global perfusionist education.
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Anticoagulantes , Antitrombinas , Resistência a Medicamentos , Heparina , Proteínas Recombinantes , Humanos , Heparina/efeitos adversos , Heparina/administração & dosagem , Anticoagulantes/efeitos adversos , Anticoagulantes/administração & dosagem , Antitrombinas/uso terapêutico , Antitrombinas/efeitos adversos , Proteínas Recombinantes/administração & dosagem , Proteínas Recombinantes/efeitos adversos , Proteínas Recombinantes/uso terapêutico , Resistência a Medicamentos/fisiologia , Fator Xa , Masculino , Inibidores do Fator Xa/efeitos adversos , Feminino , IdosoRESUMO
Objectives: In minimally invasive cardiac surgery, it can be difficult at times to maintain adequate oxygenation with single-lung ventilation after weaning from cardiopulmonary bypass (CPB), and intermittent double-lung ventilation is required during hemostasis. Venovenous extracorporeal membrane oxygenation (VV-ECMO) after weaning from CPB eliminates the necessity of overinflation of the left lung and intermittent double-lung ventilation and enables secure and fast hemostasis. We investigated the effectiveness and safety of temporary VV-ECMO in MICS. Methods: Between May 2018 and March 2021, 149 patients underwent temporary VV-ECMO during minimally invasive cardiac surgery in our institutions. After weaning from CPB, the arterial circuit was reconnected to the right internal jugular venous cannula, the femoral venous cannula was pulled down by 20 cm, and VV-ECMO was established using the CPB machine and cannulas. After starting VV-ECMO, we administered protamine and performed hemostasis. Operative data and outcomes were retrospectively reviewed. Results: The mean VV-ECMO time and flow were 26 ± 13 minutes and 2.38 ± 0.40 L/m2, respectively. There was no thrombus in the CPB circuit, including the oxygenator. The trans-oxygenator pressure gradient index at the end of VV-ECMO significantly correlated with that at the start of VV-ECMO (r = 0.88; 95% CI, 0.79-0.94; P = .01). The 30-day mortality rate was 2.0%. The incidences of unilateral pulmonary edema, prolonged ventilation, and re-exploration for bleeding were 2.7%, 5.4%, and 2.0%, respectively. Conclusions: Temporary VV-ECMO is safe and useful to maintain single-lung ventilation without overinflation after weaning from CPB for secure and fast hemostasis in minimally invasive cardiac surgery. No thrombotic event was found during temporary VV-ECMO without heparinization.
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It has been reported that a single-dose cardioplegia interval is useful, but the safe interval doses are not clear. We aimed to investigate the impact of the cardioplegia interval on myocardial protection using the modified St. Thomas solution. We included consecutive isolated minimally invasive mitral valvuloplasty procedures (n = 229) performed at a hospital and medical center from January 2014 to December 2020. We compared postoperative peak creatine kinase MB and creatine kinase levels and other indicators between the short (Group S, n = 135; maximum myocardial protection interval <60 minutes) and long (Group L, n = 94; maximum myocardial protection interval ≥60 minutes) interval groups. Propensity score matching was used to adjust for confounders between the two groups. After propensity score matching, Groups S and L contained 47 patients each. Groups S and L did not differ significantly in peak creatine kinase MB (45.8 ± 26.3 IU/L and 41.5 ± 27.9 IU/L, respectively; p = .441) and creatine kinase levels (1,133 ± 567 IU/L and 1,100 ± 916 IU/L, respectively; p = .837) after admission to the intensive care unit on the day of surgery based on propensity score matching. In multivariate analysis, a cardioplegia dosing interval ≥60 minutes was not significantly associated with the maximum creatine kinase MB level after admission to the intensive care unit on the day of surgery (p = .354; 95% confidence interval: -1.67 to 4.65). Using the antegrade modified St. Thomas solution, the long interval dose method is useful and safe in minimally invasive mitral valvuloplasty.
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Soluções Cardioplégicas , Valva Mitral , Soluções Cardioplégicas/uso terapêutico , Creatina Quinase Forma MB , Parada Cardíaca Induzida/métodos , Humanos , Valva Mitral/cirurgia , Cloreto de PotássioRESUMO
Coenzyme Q10 (CoQ10) is a key component of the mitochondrial electron transfer chain and is one of the most important cellular antioxidants. We previously reported that glycoprotein saposin B (SapB) binds CoQ10 in human cells. To elucidate the physiological role of SapB and its precursor, prosaposin (Psap), we prepared stable transfectants of HepG2 that overexpress wild-type human Psap (Wt-Tf). We also established a SapB domain mutated Psap (Mt-Tf) in which cysteine(198) was replaced with serine to disrupt three dimensional protein structure by the loss of S-S bridging. Psap knockdown (KD) strains were also examined. Western blotting analysis confirmed overexpression or knockdown of Psap in these HepG2 cells. The cellular ratios of CoQ10 to free cholesterol (FC) significantly decreased in the order of Wt-Tf>parental>Mt-Tf>KD. Additionally, the ratios of CoQ10/FC in mitochondrial fractions decreased in the order of Wt-Tf>parental>KD. These data indicate that Psap and/or SapB regulate CoQ10 levels in HepG2 cells, especially in their mitochondria.