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Profiling and Comparative Analysis of Glycoproteins in Hs578BST and Hs578T and Investigation of Prolyl 4-Hydroxylase Alpha Polypeptide II Expression and Influence in Breast Cancer Cells

Peng Wei Pan1,2, Qi Zhang1*, Fang Bai1, Jie Hou1, and Gang Bai1,2

1College of Pharmacy, State Key Laboratory of Medicinal Chemical Biology and Tianjin Key Laboratory of Molecular Drug Research, Nankai University, Tianjin 300071, China; fax: +86-2223-508-371; E-mail: qizhang@nankai.edu.cn

2College of Life Sciences, Nankai University, Tianjin 300071, China

* To whom correspondence should be addressed.

Received February 17, 2012; Revision received March 2, 2012
To identify potential cancer related glycoproteins in breast cancer cells, we enriched N-linked glycoproteins by lentil lectin from the human breast cancer cell line Hs578T and the normal breast cell line Hs578BST for proteomic comparison. Glycoproteins were separated and compared by two-dimensional electrophoresis. Twenty-four glycoproteins were identified that expressed remarkably differently, among which nine were involved in the progress of collagen synthesis. Prolyl 4-hydroxylase alpha polypeptide II (P4HA2) expression and influence in breast cancer was further investigated. Immunohistochemistry revealed that P4HA2 was upregulated in breast tumor cells compared with its adjacent normal tissues. Moreover, overexpression and RNA interference of P4HA2 showed that P4HA2 expression suppressed cell proliferation and migration in Hs578T in vitro.
KEY WORDS: glycoproteomics, lectin, breast cancer, P4HA2

DOI: 10.1134/S000629791205015X