The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum

Storr, Sarah J.; Royle, Louise; Chapman, Caroline; Hamid, Umi Marshida Abd; Robertson, John F.R.; Murray, Andrea; Dwek, Raymond A.; Rudd, Pauline M.

doi:10.1093/glycob/cwn022

Cited by 128 publications

(102 citation statements)

References 30 publications

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“…The spot T2 corresponding to MUC1 mucin from the breast cancer cell line T47D showed a relatively simple glycan profile, which contains (NeuAc)(Hex)(HexNAc) as a major glycan component. The result is in agreement with previous reports that MUC1 from T47D has the sialyl-T antigen NeuAcα2-3Galβ1-3GalNAc as the major glycan (31)(32)(33). The other four spots showed a complicated glycan profile consisting of a variety of glycans.…”

Section: C-4 Characterization Of Mucins Produced By Cell Linessupporting

confidence: 93%

Recent Advances in Electrophoresis of Mucins

Kameyama

Matsuno

2012

TIGG

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Section: C-4 Characterization Of Mucins Produced By Cell Linessupporting

confidence: 93%

Recent Advances in Electrophoresis of Mucins

Kameyama

Matsuno

2012

TIGG

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“…The detection reagents are organized according to primary specificities, although some specificities are more complex or diverse than indicated here. See Table I for lectin abbreviations. glycans on MUC1 expressed by cancer cells, resulting in the exposure of the TF and Tn (GalNAc-O-Ser/Thr) antigens (1,23,(31)(32)(33)(34)(35). The exposure of these antigens has been found in the tissue of about 90% of all carcinomas (36), whereas we found it on MUC5AC in 65% of the cancer patients (using jacalin detection).…”

Section: Discussionmentioning

confidence: 65%

The Prevalence and Nature of Glycan Alterations on Specific Proteins in Pancreatic Cancer Patients Revealed Using Antibody-Lectin Sandwich Arrays

Yue

Goldstein

Hollingsworth

et al. 2009

Molecular & Cellular Proteomics

112

114

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Changes to the glycan structures of proteins secreted by cancer cells are known to be functionally important and to have potential diagnostic value. However, an exploration of the population variation and prevalence of glycan alterations on specific proteins has been lacking because of limitations in conventional glycobiology methods. Here we report the use of a previously developed antibody-lectin sandwich array method to characterize both the protein and glycan levels of specific mucins and carcinoembryonic antigen-related proteins captured from the sera of pancreatic cancer patients (n ‫؍‬ 23) and control subjects (n ‫؍‬ 23). The MUC16 protein was frequently elevated in the cancer patients (65% of the patients) but showed no glycan alterations, whereas the MUC1 and MUC5AC proteins were less frequently elevated (30 and 35%, respectively) and showed highly prevalent (up to 65%) and distinct glycan alterations. The most frequent glycan elevations involved the ThomsenFriedenreich antigen, fucose, and Lewis antigens. An unexpected increase in the exposure of ␣-linked mannose also was observed on MUC1 and MUC5ac, indicating possible N-glycan modifications. Because glycan alterations occurred independently from the protein levels, improved identification of the cancer samples was achieved using glycan measurements on specific proteins relative to using the core protein measurements. The most significant elevation was the cancer antigen 19-9 on MUC1, occurring in 19 of 23 (87%) of the cancer patients and one of 23 (4%) of the control subjects. This work gives insight into the prevalence and protein carriers of glycan alterations in pancreatic cancer and points to the potential of using glycan measurements on specific proteins for highly effective biomarkers.

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“…This being so, at least two explanations are plausible and reflect existing pathophysiological mechanisms 1) cells expressing unmasked galectin-3 ligands have invasion advantage and 2) mainly applicable to vessel-invading cells and cells in vessel surroundings, sialidases of serum and immune cell origin can cleave the a-bound sialic acid from tumour cells, several studies have demonstrated that galectin-3 interacts with MUC1 by binding the T antigen (Yu et al, 2007). Neverthless its sialylated form, is one of the dominant glycoforms of MUC1 in breast cancer patients (Storr et al, 2008). For this reason, we assessed and compared the expression of the T antigen and its sialylated form in CMMT.…”

Section: B C D a B Amentioning

confidence: 99%

Sialylation regulates galectin-3/ligand interplay during mammary tumour progression - a case of targeted uncloaking

Oliveira¹,

Matos²,

Santos³

et al. 2011

Int. J. Dev. Biol.

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Galectin-3 is involved both in facilitating detachment of cells from primary tumour sites and favouring cancer cell adhesion and survival to anoikis in the blood stream. The mechanisms behind these apparently contradictory roles of the lectin have not yet been resolved. In order to investigate possible interplays between galectin-3 and its ligands underlying their role in the metastatic process, we examined mucin-1 (MUC1) and epidermal growth factor receptor (EGFR), well-known galectin-3 ligands, as well as galectin-3-binding site expression in a series of spontaneous canine malignant mammary tumours (CMMT) and a metastatic CMMT cell line. Despite the fact that CMMT cells expressed MUC1 and EGFR homogeneously over their plasma membrane, intravascular tumour cells, positive for galectin-3, expressed MUC1 and EGFR in a more focal membrane localization. Moreover, MUC1 overexpression in primary CMMT was present in parallel with down-regulation of galectin-3. Furthermore, in the CMT-U27 cell line, galectin-3 knock-down led to increased MUC1 expression, while MUC1 knock-down led to down-regulation of the lectin. Finally, removal of sialic acid from both CMMT and CMT-U27 xenograft samples exposed galectin-3-ligands throughout the tumour tissue, whereas these ligands were only present in galectin-3-positive invading cells in untreated samples. Interestingly indeed, we show that in vessel-invading cells, there is interaction between galectin-3 and the T antigen in vivo. We therefore hypothesized that loss of galectin-3 and sialylation-related masking of its ligands, in conjunction with their overexpression in specific tumour cell subpopulations, are crucial in regulating adhesive/de-adhesive events in the progression and invasive capacity of metastatic cells.

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The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient's serum

Cited by 128 publications

References 30 publications

Recent Advances in Electrophoresis of Mucins

Recent Advances in Electrophoresis of Mucins

The Prevalence and Nature of Glycan Alterations on Specific Proteins in Pancreatic Cancer Patients Revealed Using Antibody-Lectin Sandwich Arrays

Sialylation regulates galectin-3/ligand interplay during mammary tumour progression - a case of targeted uncloaking

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