생명과학연구소 제551회 정기세미나_장재락 교수님(아주대)
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작성자 : 관리자 날짜 : 작성일22-05-31 09:43 조회 : 3,380회본문
일시: 2022년 5월 19일(목) 오후5시
zoom link: https://kangwon-ac-kr.zoom.us/j/97702509525?pwd=MWROSFZROHJma3RNMXJraUtKUkVEQT09
제551회 생명과학연구소 세미나 2022. 5. 19 (목) 오후 5시, 온라인 https://kangwon-ac-kr.zoom.us/j/97702509525?pwd=MWROSFZROHJma3RNMXJraUtKUkVEQT09 |
Autophagic clearance of protein aggregates associated with neurodegenerative diseases
장재락 교수(아주대학교 의과대학)
Accumulation of various types of abnormal/unwanted intracellular substances is one of the main causes of the development of neurodegenerative diseases including Alzheimer's disease and Parkinson's disease. Autophagy is a fundamental intracellular process for clearance of unwanted or damaged materials accumulated in the cell. The autophagic process is initiated by the formation of phagophore mediated by sequential recruitment of specific protein complexes. The phagophore matures into the autophagosome which engulfs autophagic cargos such as cytoplasmic proteins and organelles. Autophagy is finally completed by the degradation of the materials at the autolysosome which is formed by the fusion of the autophagosome and the lysosome. Tripartite motif (TRIM) proteins are a subfamily of the RING-type E3 ubiquitin ligase family and various functional domains of TRIM proteins including the RING domain enable the proteins to play critical roles in a wide range of biological processes. In this presentation, I will discuss the roles of a TRIM protein in autophagic clearance which might be linked to the onset or progression of neurodegenerative diseases.
학력 및 약력
2002 B.S. School of Biological Sciences, Seoul National University
2009 Ph.D. School of Biological Sciences, Seoul National University, Korea
2010-2011 Visiting Fellow, National Cancer Institute/NIH, Bethesda, MD, USA
2011-2016 Visiting Fellow/Research Fellow, National Institute of Neurological Disorders and Stroke/ NIH, USA
2016-present Assistant, Associate Professor, Ajou University School of Medicine, Suwon, Korea
주요발표논문 (최근)
1. Identification of Cathepsin D as a Plasma Biomarker for Alzheimer's Disease. Kim JW*, Jung SY*, Kim Y, Heo H, Hong CH, Seo SW, Choi SH, Son SJ, Lee S, Chang J. Cells. 2021 Jan 12;10(1):E138. doi: 10.3390/cells10010138.
2. Identification of BAG2 and Cathepsin D as Plasma Biomarkers for Parkinson's Disease. Kang J*, Kim JW*, Heo H, Lee J, Park KY, Yoon JH, Chang J. Clin Transl Sci. 2021 Mar;14(2):606-616. doi: 10.1111/cts.12920. Epub 2020 Nov 22.
3. Hereditary spastic paraplegia SPG8 mutations impair CAV1-dependent, integrin-mediated cell adhesion. Lee S*, Park H, Zhu PP, Jung SY, Blackstone C, Chang J. Sci Signal. 2020 Jan 7;13(613):eaau7500. doi: 10.1126/scisignal.aau7500. Selected as a cover paper of the issue.
4. Cerebrospinal Fluid Levels of β-Amyloid 40 and β-Amyloid 42 are Proportionately Decreased in Amyloid Positron-Emission Tomography Negative Idiopathic Normal-Pressure Hydrocephalus Patients. Kim HJ*, Lim TS, Lee SM, Kim TS, Kim Y, An YS, Youn YC, Park SA, Chang J, Moon SY. J Clin Neurol. 2019 Jul;15(3):353-359. doi: 10.3988/jcn.2019.15.3.353.
5. Lung fibroblasts may play an important role in clearing apoptotic bodies of bronchial epithelial cells generated by exposure to PHMG-P-containing solution. Park EJ*, Park SJ, Kim S, Lee K, Chang J. Toxicol Lett. 2018 Apr;286:108-119. doi: 10.1016/j.toxlet.2018.01.003. Epub 2018 Jan 5.
6. Methylisothiazolinone may induce cell death and inflammatory response through DNA damage in human liver epithelium cells. Park EJ*, Kim S, Chang J. Environ Toxicol. 2018 Feb;33(2):156-166. doi: 10.1002/tox.22503. Epub 2017 Nov 7.