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AIMS AND OBJECTIVES: This study aims to analyse the trends in the incidence, prevalence and medical costs of pressure injuries (PIs) among genders in Taiwan. BACKGROUND: The treatment of PIs is complex and costly, often leading to complications and increased mortality. This issue significantly impacts healthcare quality and incurs substantial medical and social costs, warranting attention. METHODS: A retrospective cohort study was conducted using data from Taiwan's National Health Insurance Database to obtain and calculate the incidence, prevalence, and medical costs of PIs in the country between 2001 and 2015 as well as to analyse high-risk groups and the medical care utilisation of patients following the STROBE reporting guidelines. RESULTS: Between 2001 and 2015, 15,327 incident case of PIs were diagnosed. During the study period, the prevalence rate of PIs per 100,000 population rose from 26.3 to 189.6, with approximately 11.5%-16.3% of patients undergoing surgical debridement. The PIs prevalence rate increased by 7.2-fold, and hospitalisation costs accounted for 91.7%-96.0% of the total medical costs. Patients with older age, comorbidities, poorer financial status and lower education levels were found to be likely to develop PIs. These predisposing factors differed between males and females. The prevalence of PIs was higher in patients ≥75 years old than in patients from other age groups. Moreover, PI-related medical expenses have been increasing annually. CONCLUSIONS: In Taiwan, the rising incidence of PIs is driving up medical costs. Effective care and prevention of PIs necessitate a comprehensive plan from the entire healthcare system. RELEVANCE TO CLINICAL PRACTICE: This research fills a gap in the available data on the incidence, prevalence, and medical costs of PIs in Taiwan and Asia. PATIENT OR PUBLIC CONTRIBUTION: The findings can be used to help develop clinical guidelines for preventive education and treatment of PIs.
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Introduction: Coronavirus disease-2019 (COVID-19) has affected more than 608 million people and has killed 6.5 million people in the world. A few studies showed traditional Chinese medicine can be beneficial for COVID-19 treatment. An herbal preparation Jin Si Herbal Tea (JS) was formulated with herbal extracts known for their potential to decrease spike protein and ACE2 interaction, 3CL, and TRPMSS2 protease activity, and thus aimed to evaluate the clinical course of JS co-treatment along with the usual treatment schedule given for severe COVID-19 patients. Methods: This retrospective cohort study included patients with severe COVID-19 admitted to Hualien Tzu Chi Hospital between June and July 2021. All the patients were co-treated with JS and the primary outcome was death. The secondary outcomes included laboratory exam, Ct value, clinical course, and hospital stays. There were 10 patients recruited in this study and divided into < 70 years and ⧠70 years groups (n = 5 in each group). Results: Older patients (â§70 years) had a higher Charlson Comorbidity Index, VACO index, and lower hemoglobin levels than < 70 years patients. The trend of lymphocyte count, LDH, D-dimer, and Ct value of non-survivors was not consistent with previous studies. The death rate was 20% and the recovery rate to mild illness in 14 days was 40%. Conclusion: In conclusion, this is the first clinical study of JS co-treatment in severe COVID-19 patients. JS co-treatment might reduce death rate and recovery time. Further large-scale clinical trials would be expected.
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Diabetic foot ulcer (DFU) is one of the common complications of diabetes. DFU can cause a huge medical and financial burden due to infections, compromise the quality of life, and increase the mortality rate in patients. However, the consumption of medical resources for DFU is rarely mentioned. A retrospective cohort study was performed. Data were obtained from the National Health Insurance Research Database of Taiwan, and the prevalence and medical utilization data for DFU in 2001-2015 were extracted, followed by the analysis for high-risk populations. Between 2001 and 2015, there were 7511 new DFU patients. A higher proportion in these patients was male, elderly with a low education level, and low income. Between 2001 and 2015, the prevalence of DFU was 0.5-0.8%, and the number of DFU patients showed stable growth. Every year, 12.6-19.3% and 1.2-7.0% of patients underwent debridement and amputation, respectively. The hospitalization fees increased year on year. Our study showed that the DFU prevalence increased year on year, and the DFU medical expenditure increased. DFU tends to occur in males, patients with low socioeconomic status, low education level, those with multiple comorbidities, and old age. Therefore, DFU care and prevention require the entire healthcare system to jointly formulate a prevention plan.
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Diabetes Mellitus , Pie Diabético , Anciano , Estudios de Cohortes , Pie Diabético/epidemiología , Pie Diabético/terapia , Humanos , Masculino , Prevalencia , Calidad de Vida , Estudios Retrospectivos , Taiwán/epidemiologíaRESUMEN
OBJECTIVE: This study was conducted to better understand the pervasive gender barriers obstructing the progression of women in surgery by synthesising the perspectives of both female surgical trainees and surgeons. METHODS: Five electronic databases, including Medline, Embase, PsycINFO, CINAHL and Web of Science Core Collection, were searched for relevant articles. Following a full-text review by three authors, qualitative data was synthesized thematically according to the Thomas and Harden methodology and quality assessment was conducted by two authors reaching a consensus. RESULTS: Fourteen articles were included, with unfavorable work environments, male-dominated culture and societal pressures being major themes. Females in surgery lacked support, faced harassment, and had unequal opportunities, which were often exacerbated by sex-blindness by their male counterparts. Mothers were especially affected, struggling to achieve a work-life balance while facing strong criticism. However, with increasing recognition of the unique professional traits of female surgeons, there is progress towards gender quality which requires continued and sustained efforts. CONCLUSION: This systematic review sheds light on the numerous gender barriers that continue to stand in the way of female surgeons despite progress towards gender equality over the years. As the global agenda towards equality progresses, this review serves as a call-to-action to increase collective effort towards gender inclusivity which will significantly improve future health outcomes.
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Equidad de Género , Sexismo , Cirujanos , Lugar de Trabajo , Movilidad Laboral , Femenino , Humanos , Masculino , Madres , Mujeres TrabajadorasRESUMEN
By promoting personal hygiene and improving comfort, bed baths can decrease the risk of infection and help maintain skin integrity in critically ill patients. Current bed-bathing practices commonly involve the use of either soap and water (SAW) or disposable wipes (DWs). Previous research has shown both bed-bathing methods are equally effective in removing dirt, oil, and microorganisms. This experimental study compared the cost, staff satisfaction, and effects of two bed-bathing practices on critically ill patients' vital signs. We randomly assigned 138 participants into 2 groups: an experimental group that received bed baths using DWs and a control group that received bed baths using SAW. We compared the bath duration, cost, vital sign trends, and nursing staff satisfaction between the two groups. We used the chi-square test and t-test for the statistical analysis, and we expressed the quantitative data as mean and standard deviation. Our results showed the bed baths using DWs had a shorter duration and lower cost than those using SAW. There were no significant differences in the vital sign trends between the two groups. The nursing staff preferred to use DWs over SAW. This study can help clinical nursing staff decide which method to use when assisting patients with bed baths.
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Enfermedad Crítica , Personal de Enfermería , Baños , Humanos , Jabones , Signos VitalesRESUMEN
INTRODUCTION: Peritoneal carcinomatosis is difficult to treat. Pressurized Intra-Peritoneal Aerosolised Chemotherapy (PIPAC) is a novel method of delivering chemotherapy to the peritoneal cavity, aiming for homogenous and deeper drug distribution. To date, limited chemotherapeutics have been used with promising results. Here, we evaluate the pharmacokinetics, peritoneal tissue drug concentration, penetration, and short-term safety of PIPAC using solvent-based paclitaxel in swine to guide clinical trials. MATERIALS AND METHODS: PIPAC solvent-based paclitaxel was administered at 60, 30, and 15mg/m2 for 3 cohorts. Each PIPAC procedure was followed by intravenous (IV) administration of the same dose of solvent-based paclitaxel on Day 7, serving as control for pharmacokinetic comparison in the same pig. Safety and toxicity were evaluated by clinical assessment, blood counts and biochemistry. Blood samples were taken for pharmacokinetic analysis. Peritoneal biopsies were taken to measure tissue paclitaxel concentrations and distribution. RESULTS: 12 Yorkshire x Landrace pigs underwent trial procedures. With PIPAC, there was linear pharmacokinetics and lower systemic exposure to paclitaxel compared to IV administration. MALDI-MSI demonstrated concentration of paclitaxel at the peritoneal surface, with estimated 2 mm penetration. PIPAC paclitaxel had favorable toxicity profile. The most significant adverse event was neutropenia which was dose dependent, with absolute neutrophil count <1.0 × 103/µL seen at the highest dose. One pig developed grade 2 hypersensitivity reaction during IV infusion and one death occurred during the PIPAC procedure, likely from anaphylaxis; these are known potential adverse events mandating standard precautions and monitoring. CONCLUSION: PIPAC paclitaxel at 15mg/m2 may be considered for a Phase I study.
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Quimioterapia Intraperitoneal Hipertérmica , Paclitaxel/farmacocinética , Neoplasias Peritoneales/tratamiento farmacológico , Animales , Biopsia , Modelos Animales de Enfermedad , Femenino , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , PorcinosRESUMEN
O-Acetylserine sulfhydrylase catalyzes the final step of the biosynthesis of L-cysteine, the replacement of the beta-acetoxy group of O-acetyl-L-serine (OAS) by a thiol. The enzyme undergoes a conformational change to close the site upon formation of the external Schiff base (ESB) with OAS. Mutation of K120 to Q was predicted to destabilize the closed form of the ESB and decrease the rate. The K120Q mutant enzyme was prepared and characterized by UV-visible absorbance, fluorescence, visible CD, and 31P NMR spectral studies, as well as steady state and pre-steady state kinetic studies. Spectra suggest a shift in the tautomeric equilibrium toward the neutral enolimine and an increase in the rate of interconversion of the open and closed forms of the enzyme. A decrease in the rate of both half reactions likely reflects the stabilization of the ESB as a result of the increased rate of equilibration of the open and closed forms of the enzyme along the reaction pathway. Data suggest a role of K120 in helping to stabilize the closed conformation by participating in a new hydrogen bond to the backbone carbonyl of A231.
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Proteínas Bacterianas/genética , Cisteína Sintasa/genética , Lisina/genética , Mutación , Salmonella typhimurium/enzimología , Secuencia de Aminoácidos , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Sitios de Unión/genética , Dicroismo Circular , Cisteína Sintasa/química , Cisteína Sintasa/metabolismo , Estabilidad de Enzimas , Concentración de Iones de Hidrógeno , Cinética , Lisina/química , Lisina/metabolismo , Espectroscopía de Resonancia Magnética , Datos de Secuencia Molecular , Estructura Molecular , Mutagénesis Sitio-Dirigida , Conformación Proteica , Estructura Secundaria de Proteína , Estructura Terciaria de Proteína , Homología de Secuencia de Aminoácido , Espectrometría de Fluorescencia , Espectrofotometría UltravioletaRESUMEN
O-Acetylserine sulfhydrylase catalyzes the final step of the biosynthesis of l-cysteine, the replacement of the beta-acetoxy group of O-acetyl-l-serine (OAS) by a thiol. The 5'-phosphate of the PLP cofactor is very tightly bound to the enzyme; it accepts 8 hydrogen bonds from enzyme side chains and a pair of water molecules, and is in close proximity to a helix dipole. Histidine-152 (H152) is one of the residues that, via a water molecule, is responsible for positioning the 5'-phosphate. Mutation of H152 to alanine was predicted to increase the freedom of the 5'-phosphate, and as a result the cofactor, giving a decrease in the overall rate of the reaction. The H152A mutant enzyme was thus prepared and characterized by UV-visible absorbance, fluorescence, visible CD, and (31)P NMR spectral studies, as well as steady state and pre-steady state kinetic studies. UV-visible absorbance and visible CD spectra are consistent with a shift in the ketoeneamine to enolimine tautomeric equilibrium toward the neutral enolimine in the internal Schiff base of the free enzyme (ISB), the amino acid external Schiff base (ESB), and the alpha-aminoacrylate intermediate (AA). (31)P NMR spectra clearly indicate the presence of two conformers (presumably open and closed forms of the enzyme) that interconvert slowly on the NMR time scale in the ISB and ESB. Kinetic data suggest the decreased rate of the enzyme likely reflects a decrease in the amount of active enzyme as a result of an increased flexibility of the cofactor which results in substantial nonproductive binding of OAS in its external Schiff base, and a stabilization of the external Schiff bases of OAS and S-carboxynitrophenyl-l-cysteine. The nonproductive binding and stabilization of the external Schiff bases are thus linked to the shift in the tautomeric equilibrium and increase in the rate of interconversion of the open and closed forms of the enzyme. The location of the 5'-phosphate in the cofactor-binding site determines additional interactions between the cofactor and enzyme in the closed (ESB) form of the enzyme, consistent with an increased rate of interconversion of the open and closed forms of the enzyme upon increasing the rate of flexibility of the cofactor.
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Proteínas Bacterianas/química , Cisteína Sintasa/química , Histidina/química , Fosfato de Piridoxal/metabolismo , Secuencia de Aminoácidos , Proteínas Bacterianas/genética , Sitios de Unión , Dicroismo Circular , Cisteína Sintasa/genética , Cisteína Sintasa/metabolismo , Histidina/genética , Enlace de Hidrógeno , Cinética , Espectroscopía de Resonancia Magnética , Datos de Secuencia Molecular , Mutación , Conformación Proteica , Bases de Schiff/química , Espectrometría de Fluorescencia , Espectrofotometría UltravioletaRESUMEN
By serving as a microbial substrate for epithelial cell transglutaminase, Hwp1 (Hyphal wall protein 1) of Candida albicans participates in cross-links with proteins on the mammalian mucosa. Biophysical properties of the transglutaminase substrate domain were explored using a recombinant protein representative of the N-terminal domain of Hwp1 and were similar to other transglutaminase substrates, the small proline-rich proteins of cornified envelopes found in stratified squamous epithelia. Recombinant Hwp1 lacks alpha and beta structures by circular dichroism and likely exists as a disulfide-cross-linked coiled-coil. The transglutaminase substrate property prompted a unique approach for investigating the features of surface Hwp1 on germ tubes. A lysine analog, 5-(biotinamido)pentylamine, was cross-linked to germ tubes catalyzed by transglutaminase 2 prior to cell fractionation, immunoprecipitation, and detection with streptavidin conjugates. The majority of the transglutaminase-modifiable Hwp1 was covalently attached to the beta-glucan of hyphae by the C terminus of Hwp1 via a glycosylphosphatidylinositol remnant anchor. A putative precursor of cell wall forms of Hwp1 was identified in the cell extract and in the culture medium. Hwp1 was modified by relatively short N-linked glycans, and the molecular size of the protein was reduced by hypomannosylation when expressed in O-glycosylation mutant strains. Hwp1 combines features of mammalian transglutaminase substrate proteins with characteristics of fungal cell wall proteins to form an unconventional adhesin at the hyphal wall of C. albicans.
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Biotina/análogos & derivados , Candida albicans/enzimología , Proteínas Fúngicas/química , Glicosilfosfatidilinositoles/química , Glicoproteínas de Membrana/química , Transglutaminasas/química , Aminas/química , Animales , Fenómenos Biofísicos , Biofisica , Biotina/química , Western Blotting , Adhesión Celular , Pared Celular/química , Pared Celular/metabolismo , Dicroismo Circular , Disulfuros/química , Electroforesis en Gel de Poliacrilamida , Células Epiteliales/metabolismo , Proteínas Fúngicas/metabolismo , Proteínas de Unión al GTP/química , Glicósido Hidrolasas/metabolismo , Glicosilación , Cobayas , Hígado/metabolismo , Lisina/química , Glicoproteínas de Membrana/metabolismo , Mutación , Sistemas de Lectura Abierta , Fosfatidilinositoles/química , Pichia/metabolismo , Pruebas de Precipitina , Prolina/química , Proteína Glutamina Gamma Glutamiltransferasa 2 , Estructura Terciaria de Proteína , Proteínas Recombinantes/química , Espectrometría de Fluorescencia , Estreptavidina/química , Fracciones Subcelulares , Compuestos de Sulfhidrilo/química , Transglutaminasas/metabolismoRESUMEN
O-Acetylserine sulfhydrylase catalyzes the synthesis of l-cysteine from O-acetyl-l-serine (OAS) and inorganic bisulfide. An anti-E2 mechanism has been proposed for the OASS-catalyzed elimination of acetate from OAS (Tai, C.-H., and Cook, P. F. (2001) Acc. Chem. Res. 34, 49-59). Site-directed mutagenesis was used to change S272 to alanine, which would be expected to eliminate the hydrogen bond to N1 of PLP or to aspartate, which would be expected to enhance the hydrogen-bonding interaction. Both mutant enzymes catalyze the overall reaction and are in fact still good enzymes, consistent with the proposed anti-E2 mechanism. Data suggest that hydrogen bonding to the pyridine ring does not play a significant role in the alpha,beta-elimination reaction catalyzed by OASS-A. The V/K(OAS), which reflects the first half-reaction, is identical to the wild-type enzyme in the case of the S272D mutant enzyme and is decreased by only a factor of 3 in the case of the S272A mutant enzyme. In the case of the alanine mutation, and to a lesser extent the aspartate mutation, a decrease in the rate of the elimination is compensated by an increase in affinity for OAS, leading to the observed second-order rate constant, V/K. The decrease in the rate of the elimination is proposed to result from a change in the orientation of the bound cofactor, as might be expected since one of the ligands that determines the position of the bound PLP has been changed. Consistent with a change in the orientation of the cofactor are the results from a number of the spectral probes. The visible CD data for the internal Schiff base have a molar ellipticity 50% that of wild-type enzyme, and the alpha-aminoacrylate intermediate has a molar ellipticity 25% that of wild-type enzyme. The alpha-aminoacrylate intermediate can be formed from l-cysteine and l-serine with the S272A,D mutant enzymes, but not with the wild-type enzyme, and taken together with the increased K(d) for the serine external Schiff base is consistent with a change in cofactor orientation in the active site. The long wavelength fluorescence emission for the S272A mutant enzyme, attributed to Förster resonance energy transfer (McClure, G. D., Jr., and Cook, P. F. (1994) Biochemistry 33, 1647-1683) has an intensity near zero, as compared to significant fluorescence for the wild-type enzyme.