Open Access Research article

Differential profiling of breast cancer plasma proteome by isotope-coded affinity tagging method reveals biotinidase as a breast cancer biomarker

Un-Beom Kang13, Younghee Ahn1, Jong Won Lee4, Yong-Hak Kim2, Joon Kim3, Myeong-Hee Yu2, Dong-Young Noh4* and Cheolju Lee1*

Author Affiliations

1 Life Sciences Division, Korea Institute of Science and Technology, Seoul 136-791, Korea

2 Functional Proteomics Center, Korea Institute of Science and Technology, Seoul 136-791, Korea

3 School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea

4 Cancer Research Institute, Seoul National University College of Medicine, Seoul 110-744, Korea

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BMC Cancer 2010, 10:114  doi:10.1186/1471-2407-10-114

Published: 26 March 2010

Additional files

Additional file 1:

Plasma proteins identified and quantified by ICAT method. Table of all plasma proteins identified and quantified by ICAT method including IPI database accession number, protein coverage, number of unique peptides and ICAT fold-ratio.

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Additional file 2:

Peptides identified by ICAT and LC-MS/MS. List of peptides identified by LC-MS/MS and SEQUEST database search.

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Additional file 3:

MS spectra and chromatograms of three typical proteins which showed no significant changes in breast cancer. MS/MS spectra of unique peptides (left panels) and their ICAT-labeled parent ion chromatograms (right panels). Heavy and light ICAT-labeled peptides are shown with gray- and black-colored peaks, respectively. (A) Alpha-2-HS-glycoprotein with unique peptide sequence, C§NLLAEK. (B) A vitamin D-binding protein with VC+SQYAAYGEK. (C) A histidine-rich glycoprotein with VSPTDC+SAVEPEAEK. C§ and C+ are cysteines labeled with a heavy 13C-reagent and a light 12C-reagent, respectively.

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