Proteomic analysis of human lung fibroblast cells exposed to diesel particulate matter using Tribrid mass spectrometer
- Proteomic analysis of human lung fibroblast cells exposed to diesel particulate matter using Tribrid mass spectrometer
- 박현미; 이지은; 지미정; 박예은; 신종환; 백지현; 조윤진; 정혁
- Diesel Particulate Matter; Particulate matter; Tribrid mass spectrometer; Tandem mass tag
- Issue Date
- 제 20회 KHUPO 온라인 학술대회
- Proteomic analysis of human lung fibroblast cells exposed
to diesel particulate matter using Tribrid mass spectrometer
Jong Hwan Shin1, Yoon Jin Cho2,3, Mi Jung Ji1, Ji Hyun Back2,4, Yae Eun Park2,
Hyuk Jeong3, Ji Eun Lee2*, and Hyun-Mee Park 1*
1Advanced Analysis Center, Korea Institute of Science and Technology
2Center for Theragnosis, Korea Institute of Science and Technology
3Department of chemistry, Sookmyung Women's University
4Department of Biotechnology, Korea University
Particulate matter (PM) is known as carcinogen to humans. The International Agency for Research on Cancer (IARC) classified PM as potential toxicants, which are carcinogenic to humans. It is known that small-sized PM enters the human body through the both respiratory tract and causes disease. In order to explore the differentially expressed proteins associated with exposure of the PM, we pursued proteomic analysis of human lung fibroblast cells exposed to Diesel Particulate Matter (DPM) obtained from National Institute of Standards and Technology using Tribrid Orbitrap Eclipse mass spectrometry consisting of functioning mass analyzers, Quadrupole, ion trap and, orbitrap technology. Each mass analyzer must be able to work sequentially with the others which capable of performing CID, HCD or optional ETD fragmentations at any MSn stage with fragment ion detection in either ion trap or orbitrap.
In the current study, human lung fibroblast cells (CCD-8Lu) were first exposed to different concentrations of DPM solutions (0, 100, 200, and 400 μg/mL in cell culture media) for 24 hrs and 48 hrs, respectively. Then, each condition of the human lung fibroblast cells were lysed followed by tryptic digestion. The tryptic peptides obtaind from each condition were then labeled with tandem mass tag (TMT) 10-plex, and equal amounts of the labeled peptides were combined and fractionaed using high pH reversed-phase liquid chro
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