Publications by authors named "Yumiko Ueda"

Rapid defibrillation and high-quality cardiopulmonary resuscitation (CPR) are necessary for patients with cardiopulmonary arrest, one of the most serious and frequently encountered complications in cardiac catheterization laboratories. However, when the catheterization table is withdrawn from its neutral position for fluoroscopy, it is unstable and unsuitable for resuscitation because of its cantilever structure. To stabilize the table in its withdrawn position, the use of a table-stabilizing stick might improve CPR quality.

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Soil bacterial community structures in terraced rice fields and abandoned lands in a hilly and mountainous area were analyzed using 16S rRNA gene sequences. The DGGE band patterns of each soil were similar. Based on pyrosequencing data, the richness and diversity of bacterial species were slightly higher in paddy fields than in other soils.

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Newly synthesized secretory proteins are folded and assembled in the endoplasmic reticulum (ER), where an efficient protein quality control system performs a critically important function. When unfolded or aggregated proteins accumulate in the ER, certain signaling pathways such as the unfolded protein response (UPR) and ER-overload response (EOR) are functionally active in maintaining cell homeostasis. Recently we prepared Chinese hamster ovary (CHO) cells expressing mutant antithrombin (AT)(C95R) under control of the Tet-On system and showed that AT(C95R) accumulated in Russell bodies (RB), large distinctive structures derived from the ER.

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Article Synopsis
  • The endoplasmic reticulum (ER) can change its size and structure in response to environmental changes, leading to the formation of Russell bodies (RBs) that contain misfolded proteins.
  • Research focused on Chinese hamster ovary (CHO) cells expressing a mutant protein showed that RBs can form under controlled conditions and have unique structural properties, being distinct from regular ER membranes.
  • The study revealed that RBs maintain their integrity during cell division, contain ribosomes, and synthesize mutant proteins, suggesting they form due to the interaction between misfolded proteins and specific ER-shaping proteins.
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