A proteomic approach to identification of plutonium-binding proteins in mammalian cells

Baikuntha P. Aryal, Tatjana Paunesku, Gayle E. Woloschak, Chuan He, Mark P. Jensen*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Plutonium can enter the body through different routes and remains there for decades; however its specific biochemical interactions are poorly defined. We, for the first time, have studied plutonium-binding proteins using a metalloproteomic approach with rat PC12 cells. A combination of immobilized metal ion chromatography, 2D gel electrophoresis, and mass spectrometry was employed to analyze potential plutonium-binding proteins. Our results show that several proteins from PC12 cells show affinity towards Pu 4+-NTA (plutonium bound to nitrilotriacetic acid). Proteins from seven different spots in the 2D gel were identified. In contrast to the previously known plutonium-binding proteins transferrin and ferritin, which bind ferric ions, most identified proteins in our experiment are known to bind calcium, magnesium, or divalent transition metal ions. The identified plutonium interacting proteins also have functional roles in downregulation of apoptosis and other pro-proliferative processes. MetaCore™ analysis based on this group of proteins produced a pathway with a statistically significant association with development of neoplastic diseases.

Original languageEnglish (US)
Pages (from-to)1505-1514
Number of pages10
JournalJournal of Proteomics
Issue number5
StatePublished - Feb 16 2012


  • 2-D gel electrophoresis
  • GO process
  • IMAC
  • LC-MS/MS
  • PC12 cells
  • Plutonium-binding proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry


Dive into the research topics of 'A proteomic approach to identification of plutonium-binding proteins in mammalian cells'. Together they form a unique fingerprint.

Cite this