A Case of 48, XYY, +21

A 3 month-old boy with a karyotype of 48, XYY, + 21 is reported. The patient had the typical features of Down syndrome and normal male genitalia. Analysis of Q- and R-banded chromosome heteromorphisms of the patient and the parents showed that two of the three chromosomes 21 in the patient originated as a result of failure of the paternal second meiotic division. Therefore both additional chromosomes in the patient resulted from nondisjunction at paternal meiosis II

高齢者における身体組成とメタボリックシンドロームとの関連についての臨床的研究

学位の種別: 課程博士審査委員会委員 : (主査)東京大学教授 大須賀 穣, 東京大学准教授 北中 幸子, 東京大学准教授 山中 崇, 東京大学講師 下澤 達雄, 東京大学講師 鈴木 亮University of Tokyo(東京大学

FACTOR ANALYSIS OF SANDBAR DEFOMATION PROCESSES IN THE MIDDLE REACHES OF YOSHINO RIVER

The Yoshino River, Japan, is rich in water resources, but simultaneously possesses high risk of flood disaster. River improvement works to reduce damage from the floods have been conducted which attain increase of the discharge capacity. On the other hand, local sediment deposition and scouring are growing concern by the repeated floods, decreasing of sediment supply and construction of river structure. In order to resolve these problems, it is necessary to understand the effects of natural and artificial impacts on the river channel. In this paper, the channel transition processes were studied in the Middle Yoshino River using aerial photo, morphology data. Natural and artificial impacts on those processes were evaluated from sandbar deformation, fluctuation of bed elevation and volume in low-water channel. As a result, sandbar deformation by the floods and revetment works was confirmed. The floods and dam construction affected fluctuation of river channel with the sediment deposition and scouring

Structural insights into the G protein selectivity revealed by the human EP3-Gi signaling complex

熱、炎症などに関与するプロスタグランジン受容体EP3シグナリング複合体の可視化 --緑内障、高眼圧症治療薬の合理的設計に貢献--. 京都大学プレスリリース. 2022-09-15.Prostaglandin receptors have been implicated in a wide range of functions, including inflammation, immune response, reproduction, and cancer. Our group has previously determined the crystal structure of the active-like EP3 bound to its endogenous agonist, prostaglandin E₂. Here, we present the single-particle cryoelectron microscopy (cryo-EM) structure of the human EP3-Gi signaling complex at a resolution of 3.4 Å. The structure reveals the binding mode of Gi to EP3 and the structural changes induced in EP3 by Gi binding. In addition, we compare the structure of the EP3-Gi complex with other subtypes of prostaglandin receptors (EP2 and EP4) bound to Gs that have been previously reported and examine the differences in amino acid composition at the receptor-G protein interface. Mutational analysis reveals that the selectivity of the G protein depends on specific amino acid residues in the second intracellular loop and TM5