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Ito, Natsuki,Takeuchi, Ichiro,Kyodo, Reiko,Hirano, Yuri,Sato, Takuro,Usami, Masaaki,Shimizu, Hirotaka,Shimizu, Toshiaki,Arai, Katsuhiro The Korean Society of Pediatric Gastroenterology 2021 Pediatric gastroenterology, hepatology & nutrition Vol.24 No.4
Purpose: A change in diagnosis from ulcerative colitis (UC) to Crohn's disease (CD) has been reported in pediatric inflammatory bowel disease; however, only a few clinical characteristics and predictors of this diagnostic change have been reported. We aimed to describe the clinical characteristics of patients with UC who underwent a change in diagnosis to CD and identify variables associated with the change. Methods: The medical records of pediatric patients with UC who were followed up at the National Center for Child Health and Development between 2006 and 2019 were retrospectively reviewed. Clinical data on disease phenotype, laboratory parameters, endoscopic findings, and treatment of patients whose diagnosis changed to CD (cCD) were compared to those of patients whose diagnosis remained UC (rUC). Results: Among the 111 patients initially diagnosed with UC, 11 (9.9%) patients were subsequently diagnosed with CD during follow-up. There was no significant difference between the cCD and rUC groups in terms of sex, age at initial diagnosis, and the extent and severity of disease at initial diagnosis. Albumin and hemoglobin levels were significantly lower in the cCD group than in the rUC group. The proportion of patients who required biologics was significantly higher in the cCD group than in the rUC group (p<0.05). Conclusion: Approximately 10% children initially diagnosed with UC were subsequently diagnosed with CD. Hypoalbuminemia and anemia at initial diagnosis and use of biologics could be predictors of this diagnostic change.
Iron deficiency regulated OsOPT7 is essential for iron homeostasis in rice
Bashir, Khurram,Ishimaru, Yasuhiro,Itai, Reiko Nakanishi,Senoura, Takeshi,Takahashi, Michiko,An, Gynheung,Oikawa, Takaya,Ueda, Minoru,Sato, Aiko,Uozumi, Nobuyuki,Nakanishi, Hiromi,Nishizawa, Naoko K. Springer-Verlag 2015 Plant Molecular Biology Vol. No.
Phospholipid-dependent regulation of the motor activity of myosin X
Umeki, Nobuhisa,Jung, Hyun Suk,Sakai, Tsuyoshi,Sato, Osamu,Ikebe, Reiko,Ikebe, Mitsuo Nature Publishing Group, a division of Macmillan P 2011 Nature structural & molecular biology Vol.18 No.7
Myosin X is involved in the reorganization of the actin cytoskeleton and protrusion of filopodia. Here we studied the molecular mechanism by which bovine myosin X is regulated. The globular tail domain inhibited the motor activity of myosin X in a Ca<SUP>2+</SUP>-independent manner. Structural analysis revealed that myosin X is monomeric and that the band 4.1-ezrin-radixin-moesin (FERM) and pleckstrin homology (PH) domains bind to the head intramolecularly, forming an inhibited conformation. Binding of phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P<SUB>3</SUB>) to the PH domain reversed the tail-induced inhibition and induced the formation of myosin X dimers. Consistently, disruption of the binding of PtdIns(3,4,5)P<SUB>3</SUB> attenuated the translocation of myosin X to filopodial tips in cells. We propose the following mechanism: first, the tail inhibits the motor activity of myosin X by intramolecular head-tail interactions to form the folded conformation; second, phospholipid binding reverses the inhibition and disrupts the folded conformation, which induces dimer formation, thereby activating the mechanical and cargo transporter activity of myosin X.