An immunosorbent assay for blood group I antigens in breast carcinoma

Dube, Volker E.; Kallio, Patricia; Chmiel, Joan S.; Haid, Max; Hakim, Anwar A.

doi:10.1016/0090-1229(87)90034-1

Cited by 4 publications

(1 citation statement)

References 31 publications

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“…Interestingly, I antigen was also found to be present in the soluble glycoproteins in various body fluids including milk, saliva, plasma, urine, and ovarian cyst fluid (39, 40). Specifically, potential roles for GCNT2 in human breast cancers are also suggested by the observation made more than 20 years ago that I antigens in the sera of breast cancer patients were increased and the I antigen levels correlated with the breast carcinoma stages (41-43). The results of our study thus provide direct biological explanation for the long-standing observation and suggest that the overexpression of GCNT2 , along with breast cancer progression, lead to the abundant expression of protein with I antigen.…”

Section: Discussionmentioning

confidence: 96%

Engagement of I-Branching β-1, 6-N-Acetylglucosaminyltransferase 2 in Breast Cancer Metastasis and TGF-β Signaling

Zhang

Meng

et al. 2011

Cancer Research

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In this study, we have showed that GCNT2, a gene-encoding glucosaminyl (N-acetyl) transferase 2, I-branching enzyme, is overexpressed in highly metastatic breast cancer cell lines of human and mouse origin and basal-like breast tumor samples. GCNT2 expression is also significantly correlated to the metastatic phenotype in breast tumor samples. Functional studies showed that ectopic expression of GCNT2 enhances cell detachment, adhesion to endothelial cells, cell migration and invasion in vitro, and lung metastasis of breast cancer cells in vivo. Knockdown of GCNT2 expression decreases cell migration and invasion in vitro and lung metastasis in vivo. We have further shown the involvement of GCNT2 in the epithelial-to-mesenchymal transition (EMT). Specifically, the expression of E-cadherin is significantly changed upon GCNT2 expression at the protein level but not at the RNA level. Moreover, we have shown that GCNT2 is a direct target of the TGF-β–smad pathway and that change in GCNT2 expression modulates EMT induced by TGF-β1 treatment. Finally, we have shown that diminution of the glycosyltransferase activity of I-branching β-1, 6-N-acetylglucosaminyl transferase 2 (GCNT2) abrogates its cell migration and invasion-promoting function and synergistic effect with TGF-β to induce EMT. Our study for the first time showed that GCNT2 is a novel gene contributing to breast cancer metastasis with preferential expression in basal-like breast cancer. Moreover, we discovered that involvement of GCNT2 in EMT and TGF-β signaling, and further glycosylation modification of E-cadherin by GCNT2, are the underlying integrative mechanisms for breast cancer metastasis, implying that blocking TGF-β/GCNT2 signaling is a promising approach for targeting metastatic breast cancer.

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