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김양신 ( Yangsin Kim ),오재우 ( Jaewoo Oh ) 사단법인 아시아문화학술원 2021 인문사회 21 Vol.12 No.2
본 연구는 졸업을 앞둔 간호대학생의 투약오류를 중심으로 투약안전 역량에 관한 서술적 조사 연구이다. 자료수집 기간은 2020년 12월 9일부터 12월 31일까지이며, 경상·충청지역 소재 대학의 간호학과 4학년 재학생 141명을 대상으로 설문조사하였다. 수집된 자료의 분석은 IBM SPSS/Win 25.0을 이용하였으며, 서술통계, t-test, ANOVA, Pearson 상관관계와 다중회귀분석을 하였다. 연구결과 투약안전 역량은 환자이해도(r=.56, p<.001)와 정적 상관관계를 나타내었으며, 환자이해도와 전공만족도가 투약안전 역량에 대해 총 38.1%를 설명하였다. 전공만족도가 높고 환자이해도가 높을수록 투약안전 역량이 높다는 본 연구결과를 바탕으로 입학부터 졸업시까지 전공만족도 향상을 위한 대학 및 학과 차원에서의 비교과 교육과정 개발이 필요하며, 환자이해도 증진을 위한 교육프로그램 개발과 적용방안이 마련되어야 할 것으로 생각된다. This study is a descriptive research study for identifying the medication safety capabilities of nursing students who are about to graduate, focusing on medication errors. The period of data collection was from Dec. 9, 2020 to Dec. 31, 2020, and the survey was conducted for 141 students in the 4th grade of department of nursing at universities located in Gyeongsang and Chungcheong provinces. The collected data were analyzed using IBM SPSS/Win 25.0, and descriptive statistics, t-test, ANOVA, Pearson correlation and multiple regression analysis were performed. As a result of the study, the medication safety capabilities showed a positive correlation with the patient understanding level (r=.56, p<.001), and the patient understanding level and major satisfaction level explained a total of 38.1% of the medication safety capabilities. It is considered that it is necessary to develop a nonsubject curriculum at the university and department level to improve major satisfaction level from admission to graduation, and that educational program development and application plan should be prepared to improve the patient understanding level, based on the results of this study that the higher the major satisfaction level and the patient understanding level, the higher the medication safety capabilities.
O-GlcNAc modification is essential for the regulation of autophagy in Drosophila melanogaster.
Park, Sujin,Lee, Yangsin,Pak, Jin Won,Kim, Hanbyeol,Choi, Hyeonjin,Kim, Jae-woo,Roth, Jü,rgen,Cho, Jin Won Birkhäuser ; Springer 2015 Cellular and molecular life sciences Vol.72 No.16
<P>O-GlcNAcylation is a dynamic post-translational modification that takes place on ser/thr residues of nucleocytoplasmic proteins. O-GlcNAcylation regulates almost all cellular events as a nutrient sensor, a transcriptional and translational regulator, and a disease-related factor. Although the role of O-GlcNAcylation in insulin signaling and metabolism are well established, the relationship between O-GlcNAcylation and autophagy is largely unknown. Here, we manipulated O-GlcNAcylation in Drosophila and found that it regulates autophagy through Akt/dFOXO signaling. We demonstrate that O-GlcNAcylation and the levels of O-GlcNAc transferase (OGT) are increased during starvation. Furthermore, Atg proteins and autolysosomes are increased in OGT-reduced flies without fasting. Atg proteins and autophagosomes are reduced in OGT-overexpressing flies. Our results suggest that not only autophagy gene expression but also autophagic structures are regulated by OGT through Akt and dFOXO. These data imply that O-GlcNAcylation is important in modulating autophagy as well as insulin signaling in Drosophila.</P>
Protein N-Glycosylation, Protein Folding, and Protein Quality Control
Jürgen Roth,Christian Zuber,박수진,Insook Jang,Yangsin Lee,Katarina Gaplovska Kysela,Valérie Le Fourn,Roger Santimaria,Bruno Guhl,조진원 한국분자세포생물학회 2010 Molecules and cells Vol.30 No.6
Quality control of protein folding represents a funda-mental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.
Nephrin expression in human epidermal keratinocytes and its implication in poor wound closure
( Ji Young Kim ),( Eun Jung Lee ),( Jimyung Seo ),( Yangsin Lee ),( Yuri Ahn ),( Sujin Park ),( Yu Jeong Bae ),( Jinu Lee ),( Beom Jin Lim ),( Doyoung Kim ),( Jin Won Cho ),( Sang Ho Oh ) 대한피부과학회 2022 대한피부과학회 학술발표대회집 Vol.74 No.1
Specific autophagy and ESCRT components participate in the unconventional secretion of CFTR
Noh, Shin Hye,Gee, Heon Yung,Kim, Yonjung,Piao, He,Kim, Jiyoon,Kang, Chung Min,Lee, Gahyung,Mook-Jung, Inhee,Lee, Yangsin,Cho, Jin Won,Lee, Min Goo Informa UK (TaylorFrancis) 2018 AUTOPHAGY Vol.14 No.10
<P>The most common mutation in cystic fibrosis patients is a phenylalanine deletion at position 508 (Delta F508) in the CFTR (cystic fibrosis transmembrane conductance regulator) gene. This mutation impairs cell-surface trafficking of CFTR. During cellular stress, core-glycosylated CFTR Delta F508 is transported to the cell surface from the endoplasmic reticulum (ER) via an unconventional route that bypasses the Golgi. However, the mechanisms for this unconventional secretory pathway of CFTR are not well delineated. Here, we report that components of the macroautophagy/autophagy and ESCRT (endosomal sorting complex required for transport) pathways are involved in unconventional secretion of CFTR. In mammalian cells, we found that autophagic pathways were modulated by conditions that also stimulate unconventional secretion, namely ER stress and an ER-to-Golgi transport blockade. Additionally, we found that knockdown of early autophagy components, ATG5 and ATG7, and treatment with pharmacological autophagy inhibitors, wortmannin and 3-methyladenine, abolished the unconventional secretion of CFTR that had been stimulated by ER stress and an ER-to-Golgi blockade. Interestingly, immunoelectron microscopy revealed that GORASP2/GRASP55, which mediates unconventional CFTR trafficking, is present in multivesicular bodies (MVB) and autophagosomal structures under ER stress conditions. A custom small-interfering RNA screen of mammalian ESCRT proteins that mediate MVB biogenesis showed that silencing of some ESCRTs, including MVB12B, inhibited unconventional CFTR Delta F508 secretion. Furthermore, MVB12B overexpression partially rescued cell-surface expression and Cl- channel function of CFTR Delta F508. Taken together, these results suggest that components involved in early autophagosome formation and the ESCRT/MVB pathway play a key role in the stress-induced unconventional secretion of CFTR.</P>