International Journal of Oral Biology

  • 제34권1호
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  • Pages.29-36
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  • 2009
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  • 1226-7155(pISSN)
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  • 2287-6618(eISSN)
대한구강생물학회 (The Korean Academy of Oral Biology)
권호 표지

Proteomic Analysis of Rat PC12 Cells Exposed to Cyclosporin A

  • Jung, Ji-Yeon (Department of Oral Physiology, Dental Science Research Institute, Brain Korea 21 Project, School of Dentistry Chonnam National University) ;
  • Seol, Kwang (Department of Oral Physiology, Dental Science Research Institute, Brain Korea 21 Project, School of Dentistry Chonnam National University) ;
  • Jeong, Yeon-Jin (Department of Oral Physiology, Dental Science Research Institute, Brain Korea 21 Project, School of Dentistry Chonnam National University) ;
  • Kim, Won-Jae (Department of Oral Physiology, Dental Science Research Institute, Brain Korea 21 Project, School of Dentistry Chonnam National University) ;
  • Oh, Sang-Jin (School of Biological Sciences and Technology, Chonnam National University)
  • 발행 : 2009.03.31
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초록

Cyclosporin A (CsA) has been used clinically as an immunosuppressive drug to prevent organ transplant rejection and in basic research as a mitochondrial permeability blocker. It has been reported that CsA has a protective role in severed neurons and a neurotrophic effect in neuronal cells. However, the molecular mechanisms underlying the stimulation of neuronal cell proliferation by CsA have not yet been elucidated. In our current study, we investigated CsA responsive proteins in PC12 cells using a systematic proteomic approach. The viability of these cells following CsA treatment increased in a dose- and time-dependent manner. Proteins in the CsA-treated PC12 cells were profiled by two-dimensional gel electrophoresis (2-DE) and identified by matrix-assisted laser desorption ionization time-of flight (MALDI-TOF) and electrospray ionization quadupole time-of-flight mass spectrometries (EIQ-TOFMS). This differential expression analysis showed significant changes for 10 proteins (6 up-regulated and 4 down-regulated) upon CsA treatment that were related to cell proliferation, metabolism and the stress response. These proteomics data further our understanding of the proliferation mechanisms of PC12 cells exposed to CsA and demonstrate that our methodology has potential to further elucidate the mechanisms and pathways involved.

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