42 research outputs found
Effect of COVID-19 vaccination on viral clearance and antibody production in older patients with SARS-CoV-2 infection
Whether coronavirus disease 2019 (COVID-19) vaccination promotes viral clearance in older patients has not been reported. We performed a retrospective review of patients hospitalized with COVID-19. This study included 24 patients with COVID-19 admitted to Hiroshima City Funairi Citizens Hospital between June 1 and July 10, 2021. Nine patients who were vaccinated (median age: 72 years) were compared with 15 patients who were not vaccinated (median age: 70 years). Viral clearance was confirmed by SARS-CoV-2 reverse transcription polymerase chain reaction (RT-PCR). Antibody titers were measured to assess vaccination efficacy. The vaccinated group had a higher negative conversion rate than that in the non-vaccinated group on RT-PCR testing before discharge (83% vs. 36%, P = 0.064). Antibody titers on admission and 10 ± 2 days after onset were significantly higher in the vaccinated group than those in the non-vaccinated group (35 vs. 0 binding antibody units (BAU)/mL, P = 0.012; and 114 vs. 7 BAU/mL, P = 0.032, respectively). Stimulating antibody production by vaccination may promote faster viral clearance in older patients who develop COVID-19.This research was funded by “Advanced study aim to contribute creating new evidence in COVID-19 based on the local government-academia collaboration research system in Hiroshima”: AMED Research Program on Emerging and Re-emerging Infectious Diseases, Grant Number JP20fk0108453
Magnetic properties of surficial sediments in Lake Ogawara on the Pacific coast of northeastern Japan: spatial variability and correlation with brackish water stratification
To examine limnological conditions in Lake Ogawara on the Pacific coast of northwestern Japan, we investigated the magnetic properties of dredged bottom sediment originally collected from the lake in the summer of 2011. We used non-destructive methods to measure the low-field magnetic susceptibility shortl after sampling, and anhysteretic remanent magnetization (ARM) was assessed in 2012 and 2015. The ARM acquisition and demagnetization curves from littoral sites showed several patterns that reflect the provenance of the sediments. At water depths below 10 m, the magnetic susceptibility and ARM of greenish black mud with high organic content decreased considerably with the increase in water depth, but ARM increased slightly at water depths greater than 16 m. We also found that the magnetic concentrations of mud samples were reduced markedly during a period of storage for about 3 years. We attributed these reductions to diagenetic loss of magnetic minerals, which had been enhanced at deeper sites. It is possible that the ARM carriers in deeper areas were derived from authigenic formation of iron sulfide or from deposition of suspended matter in the hypolimnion water. We propose that the magnetic properties of surficial sediments are controlled by limnological stratification of the brackish lake water, thus possibly providing an analog for down-core variations of magnetic parameters associated with the modification of magnetic minerals during reductive diagenesis
Nutrient-induced FNIP degradation by SCFβ-TRCP regulates FLCN complex localization and promotes renal cancer progression.
Folliculin-interacting protein 1 and 2 (FNIP1 and FNIP2) play critical roles in preventing renal malignancy through their association with the tumor suppressor FLCN. Mutations in FLCN are associated with Birt-Hogg-Dubé (BHD) syndrome, a rare disorder with increased risk of renal cancer. Recent studies indicated that FNIP1/FNIP2 double knockout mice display enlarged polycystic kidneys and renal carcinoma, which phenocopies FLCN knockout mice, suggesting that these two proteins function together to suppress renal cancer. However, the molecular mechanism functionally linking FNIP1/FNIP2 and FLCN remains largely elusive. Here, we demonstrated that FNIP2 protein is unstable and subjected to proteasome-dependent degradation via β-TRCP and Casein Kinase 1 (CK1)-directed ubiquitination in a nutrition-dependent manner. Degradation of FNIP2 leads to lysosomal dissociation of FLCN and subsequent lysosomal association of mTOR, which in turn promotes the proliferation of renal cancer cells. These results indicate that SCFβ-TRCP negatively regulates the FLCN complex by promoting FNIP degradation and provide molecular insight into the pathogenesis of BHD-associated renal cancer.福岡歯科大学2016年
The Pilot Study for Health Check-Ups System at Elementary School in Cambodia
Background: In Cambodia, there is no national health check-ups system for the schoolchildren and the general population. This pilot study aimed to promote a school health check-ups system in collaboration with the government of Cambodia.
Method: From 2016 to 2017, we conducted a survey in an elementary school in Siem Reap province, Cambodia. Two hundred and ninety-two students were eligible for data analysis. Physical examination, questionnaire and urinalysis were conducted using the Japanese school health check-ups model. Anthropometry was measured using the World Health Organization’s growth reference data for school-age children.
Results: Among 292 schoolchildren, 88.7% were diagnosed as healthy. Based on the evaluation criteria of health examination in the study, two (0.7%) students with rale, one (0.3%) student with abnormal urinalysis, and another 27 students complaining of cardiopulmonary symptoms were recommended for further consultation at hospital. The prevalence of overweight (15.1%) was higher than that of underweight (8.6%). According to parents’ questionnaires responses, the coverage rate of the National Immunization Program varied from 41.8% to 79.8% depending on each particular vaccine.
Conclusion: In this pilot study, we showed the prevalence of healthy among Cambodian schoolchildren and detected the students having possibility of health problem through this health check-ups and then recommended for further hospital visit. Based on the results, we assume that health check-ups system in elementary school as a whole Cambodia will be effective to assess the current health status in ordinary time and possibility of early detection of disease
Erratum to: 36th International Symposium on Intensive Care and Emergency Medicine
[This corrects the article DOI: 10.1186/s13054-016-1208-6.]
Five cases of childhood-onset Graves’ disease treated with either surgery or radio-iodine therapy
Magnetic properties of surficial sediments in Lake Ogawara on the Pacific coast of northeastern Japan: spatial variability and correlation with brackish water stratification
Primary Structure and Conformation of a Tetrodotoxin-Binding Protein in the Hemolymph of Non-Toxic Shore Crab <i>Hemigrapsus sanguineus</i>
Tetrodotoxin (TTX)-binding proteins are present in toxic TTX-bearing animals, such as pufferfish and gastropods. These may prevent autotoxicity. However, TTX-binding proteins are also found in the nontoxic marine shore crab, Hemigrapsus sanguineus. Here, we isolated the TTX-binding protein, HSTBP (Hemigrapsus sanguineus TTX-binding protein), from the hemolymph of H. sanguineus and elucidated its primary structure using cDNA cloning. HSTBP, a 400 kDa acidic glycoprotein by gel filtration high-performance liquid chromatography, comprises 3 subunits, 88 kDa (subunit-1), 65 kDa (subunit-2), and 26 kDa (subunit-3) via sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reduced conditions. The open reading frame of the cDNA comprises 5049 base pairs encoding 1683 amino acid residues, and the mature protein contains 1650 amino acid residues from Arg34 to Ser1683. The three subunits are arranged in tandem in the following order: subunit-3 (Arg34-Gln261), subunit-1 (Asp262-Phe1138), and subunit-2 (Val1139-Ser1683). A BLAST homology search showed weak similarity of HSTBP to clotting proteins of crustaceans (29–40%). SMART analysis revealed a von Willebrand factor (vWF)-type (⇒delete hyphen) D domain at Phe1387-Gly1544. We confirmed that the recombinant protein of HSTBP subunit-2 containing the vWF-type (⇒delete hyphen) D domain bound to TTX at a molecular ratio of 1:1