Glycoproteomics analysis of breast cancer using in vivo model

8^th Euro Global Summit on Cancer Therapy

November 03-05, 2015 Valencia, Spain

Yin-Ling Wong1, Aik-Aun Tan2 and Yeng Chen1

1University of Malaya, Malaysia
2Universiti Sains Malaysia, Malaysia

Posters-Accepted Abstracts: J Cancer Sci Ther

Abstract :

Glycosylation is a post-translational modification processes that play a crucial role in many biological processes such as proteinprotein interactions and cell adhesion. Aberrant glycosylation of proteins was found to be associated with cancer progression. Characterization of protein glycosylation profiles may identify potential biomarkers for the diagnosis and prognosis of cancer. This study aimed to elucidate the serum protein profile and protein glycosylation profile (N- and O-linked glycosylation) in the breast cancer progression using mouse 4T1 breast tumour model. The female BALB/c mice were injected with 4T1 tumour cells in the mammary fat pad. The mice sera samples were collected weekly (up to four weeks) and subjected to two-dimensional electrophoresis (2D-E) coupling with glycan-binding lectins and further analysed through mass spectrometry. Analysis of protein profiles identified eight differentially expressed proteins (A2M, AAT, AHS, APOA4, CON, HP, KNG and PRO), of which AAT, CON, HP and KNG were significantly up-regulated in mice sera from week 1 to week 4 after 4T1 cells injection. Aberrantly N-glycosylated PRO was detected in all the mice sera from week 1 to week 4 after the injection. As for the O-glycosylated protein detection, A2M, AHS, CON and HP were aberrantly expressed in mice sera after injection, of which A2M, CON and HP were detected on week 1 and week 2, while AHS and CON were detected on week 3 and week 4. Combination of 2D-E with lectin-based analysis were effective to identify various biomarkers that could serve as potential diagnostic and prognostic markers for breast cancer.

Biography :

Email: wyl_1230@yahoo.com