Examining proximity to death and health care expenditure by disease: a Bayesian-based descriptive statistical analysis from the National Health Insurance database in Japan.

Background: Japan is one of the Organization for Economic Co-operation and Development (OECD) countries where population aging and increasing health care expenditures (HCE) are urgent issues. Recent studies have identified factors other than age, such as proximity to death and morbidity, as contributing factors to the increase in medical costs. It is important to assess HCE by disease and analyze their factors to estimate and improve future HCE.

Data Resource Profile of Shizuoka Kokuho Database (SKDB) Using Integrated Health- and Care-insurance Claims and Health Checkups: The Shizuoka Study.

Background: Analyzing real-world data, including health insurance claims, may help provide insights into preventing and treating various diseases. We developed a database covering Shizuoka Prefecture (Shizuoka Kokuho Database [SKDB]) in Japan, which included individual-level linked data on health- and care-insurance claims and health checkup results.

Methods: Anonymized claims data on health insurance (National Health Insurance [age <75 years] and Latter-Stage Elderly Medical Care System [age ≥75 years]), care insurance, subscriber lists, annual health checkups, and all dates of death were collected from 35 municipalities in Shizuoka Prefecture.

Impact of hyperuricaemia on the chronic kidney disease-associated risk factors in a community-based population.

Aim: Hyperuricaemia is a common finding in subjects with lifestyle related diseases. This study was performed to examine its association with chronic kidney disease (CKD) in relation to other risk factors in a community-based population.

Methods: Data from 187 914 participants, excepting CKD stage 5, of the health check-up were included in this analysis.

Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum.

1,2-alpha-L-fucosidase (AfcA), which hydrolyzes the glycosidic linkage of Fucalpha1-2Gal via an inverting mechanism, was recently isolated from Bifidobacterium bifidum and classified as the first member of the novel glycoside hydrolase family 95. To better understand the molecular mechanism of this enzyme, we determined the x-ray crystal structures of the AfcA catalytic (Fuc) domain in unliganded and complexed forms with deoxyfuconojirimycin (inhibitor), 2'-fucosyllactose (substrate), and L-fucose and lactose (products) at 1.12-2.