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Pyloric Gland Adenoma of the Esophagus Treated by Endoscopic Submucosal Dissection: A Case Report
Park Kwangbeom,Kim Do Hoon,Lee Sung Duck,Lee Hyun,Jung Hwoon-Yong 거트앤리버 소화기연관학회협의회 2022 Gut and Liver Vol.16 No.3
A pyloric gland adenoma is a rare neoplasm that occurs most frequently in the stomach and should be removed because of its precancerous potential. Although there have been case reports of pyloric gland adenomas in extragastric areas such as the duodenum, pancreas, and bile duct, esophageal pyloric gland adenoma has never been reported in Korea. Herein, we report a case of esophageal pyloric gland adenoma that was successfully treated by endoscopic submucosal dissection.
Cho Gahyang,Hyun Kwangbeom,Choi Jieun,Shin Eunji,Kim Bumsoo,Kim Hail,Kim Jaehoon,Yong-Mahn Han 생화학분자생물학회 2023 Experimental and molecular medicine Vol.55 No.-
Neurogenin 3 (NGN3) is a key transcription factor in the cell fate determination of endocrine progenitors (EPs) in the developing pancreas. Previous studies have shown that the stability and activity of NGN3 are regulated by phosphorylation. However, the role of NGN3 methylation is poorly understood. Here, we report that protein arginine methyltransferase-1 (PRMT1)-mediated arginine 65 methylation of NGN3 is required for the pancreatic endocrine development of human embryonic stem cells (hESCs) in vitro. We found that inducible PRMT1-knockout (P-iKO) hESCs did not differentiate from EPs into endocrine cells (ECs) in the presence of doxycycline. Loss of PRMT1 caused NGN3 accumulation in the cytoplasm of EPs and decreased the transcriptional activity of NGN3. We found that PRMT1 specifically methylates NGN3 arginine 65 and that this modification is a prerequisite for ubiquitin-mediated degradation. Our findings demonstrate that arginine 65 methylation of NGN3 is a key molecular switch in hESCs permitting their differentiation into pancreatic ECs.
Multiple RPAs make WRN syndrome protein a superhelicase
Lee, Mina,Shin, Soochul,Uhm, Heesoo,Hong, Heesun,Kirk, Jaewon,Hyun, Kwangbeom,Kulikowicz, Tomasz,Kim, Jaehoon,Ahn, Byungchan,Bohr, Vilhelm A,Hohng, Sungchul Oxford University Press 2018 Nucleic acids research Vol.46 No.9
<P><B>Abstract</B></P><P>RPA is known to stimulate the helicase activity of Werner syndrome protein (WRN), but the exact stimulation mechanism is not understood. We use single-molecule FRET and magnetic tweezers to investigate the helicase activity of WRN and its stimulation by RPA. We show that WRN alone is a weak helicase which repetitively unwind just a few tens of base pairs, but that binding of multiple RPAs to the enzyme converts WRN into a superhelicase that unidirectionally unwinds double-stranded DNA more than 1 kb. Our study provides a good case in which the activity and biological functions of the enzyme may be fundamentally altered by the binding of cofactors.</P>