Please use this identifier to cite or link to this item:
Title: Novel breast cancer metastasis-associated proteins
Authors: Ho, J. 
Kong, J.-W.-F.
Choong, L.-Y. 
Loh, M.-C.-S.
Toy, W. 
Chong, P.-K. 
Wong, C.-H.
Wong, C.-Y.
Shah, N.
Lim, Y.-P. 
Keywords: Breast cancer
Tissue microarray
Issue Date: Feb-2009
Citation: Ho, J., Kong, J.-W.-F., Choong, L.-Y., Loh, M.-C.-S., Toy, W., Chong, P.-K., Wong, C.-H., Wong, C.-Y., Shah, N., Lim, Y.-P. (2009-02). Novel breast cancer metastasis-associated proteins. Journal of Proteome Research 8 (2) : 583-594. ScholarBank@NUS Repository.
Abstract: With the use of the breast cancer metastatic model, which comprises four isogenic cell lines, iTRAQ- based ESI-LC/MS/MS proteomics was employed to catalog protein expression changes as cancer cells acquire increasing metastatic potential. From more than 1000 proteins detected, 197 proteins, including drug-targetable kinases, phosphatases, proteases and transcription factors, displayed differential expression when cancer cells becomes more metastatic. Overall, the number of protein expression changes was evenly distributed across mildly (∼30%), moderately (∼40%) and aggressively (∼30%) metastatic cancer cells. Some changes were found to be specific to one while others were required for two or more phenotypes. KEGG Orthology suggests major reprogramming in cell metabolism and to smaller extents in genetic and environmental information processing. Ten novel metastasis-associated proteins were identified and the iTRAQ-based expression profiles of 7 proteins were verified to be congruent with antibody-based methods. With the use of tissue microarrays comprising 50 matched cases of invasive and metastatic lesions, the expression profiles of SH3GLB1 and SUB1, SND1, TRIM28 were validated to be down- and up-regulated, respectively, during clinical progression of carcinoma in situ to invasive and metastatic carcinomas. Our study has unraveled proteome-wide molecular aberrations and potentially new players in breast cancer metastasis. © 2009 American Chemical Society.
Source Title: Journal of Proteome Research
ISSN: 15353893
DOI: 10.1021/pr8007368
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.