Expression of fully and under-glycosylated forms of MUC1 mucin in gastric carcinoma

Reis, Celso A.; David, Leonor; Seixas, Mário; Burchell, Joy; Sobrinho‐Simöes, Manuel

doi:10.1002/(sici)1097-0215(19980821)79:4<402::aid-ijc16>3.0.co;2-6

Cited by 106 publications

(86 citation statements)

References 20 publications

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“…On the other hand, though the expression of MUC1 was not significantly associated with the metastasis and depth of invasion (P>0.05), it still had the tendency toward higher expression in advanced stage of cancer. However, we failed to find that MUC1 had the prognostic role in gastric cancer patients, which is different with Ustsunomiya's conclusion [9] , but consistent with Reis's conclusion [14] . These contradictory results might be due to our relatively small number of follow-up patients after operation.…”

Section: Discussioncontrasting

confidence: 56%

Expression of mucins and E-cadherin in gastric carcinoma and their clinical significance

Zhang

Zhang²,

Zhao³

et al. 2004

WJG

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AIM:To investigate the expression of three types of mucin (MUC1, MUC2, MUC5AC) and E-cadherin in human gastric carcinomas and their clinical significance. METHODS:Ninety-four gastric cancer specimens were classified according to WHO criteria and detected by immunohistochemical assay of expression of mucins and E-cadherin. RESULTS:The positive expression rates of MUC1, MUC2, MUC5AC and E-cadherin were 82% (77/94), 84% (79/94), 40% (38/94) and 56% (53/94) respectively. MUC1 expression was significantly correlated with the types of cancer (the positive rates of MUC1 in well and moderately differentiated tubular adenocarcinoma, poorly differentiated adenocarcinoma, signet-ring cell carcinoma and mucinous carcinoma were 91%, 87%, 71%, 71%, respectively, P<0.05), age of patients (the positive rates of it among the people who are younger than 40 years, between 40-60 years and over 60 year were 74%, 81%, 89%, P<0.05), lymph nodes involvement (the positive rates in the non-interfered group and the interfered group were 78%, 85%, P<0.05) and tumor size (the positive rates in the tumors with the size less than 3 cm, 3-6 cm and larger than 6 cm were 69%, 92%, 69%, P<0.05); MUC2 expression was significantly associated with types of cancers and had the strongest expression in mucinous carcinomas (the positive rates of MUC2 in well and moderately differentiated tubular adenocarcinoma, poorly differentiated adenocarcinoma, signet-ring cell carcinoma and mucinous carcinoma were 94%, 70%, 81%, 100%, P<0.05), but it had no obvious relation to age, gender, tumor location, lymph nodes involvement, depth of invasion and metastasis to extra-gastric organs (P>0.05); MUC5AC expression was not related to any of the characteristics investigated except that it had relation to gender, whereas MUC5AC showed the tendency to higher expression in less invasive lesions and lower expression in advanced stage cancers (P>0.05); No significant difference was found for E-cadherin expression. There were strong positive relationships between the expression of MUC1 and E-cadherin, MUC2 and E-cadherin, MUC1 and MUC2 (R = 0.33, R = 0.22, R = 0.32, respectively, P<0.05). According to the COX proportional hazards model, older patients, involvement of lymph nodes, different types of gastric cancer and MUC2 expression were significantly associated with poorer outcome of gastric carcinoma patients (β = 0.08, β = 3.94, β = 1.33, β = 0.75, respectively, P<0.05).CONCLUSION: MUC1 and MUC2 are good markers of different types of gastric cancer. MUC2 is especially a good marker of mucinous carcinoma. MUC1, MUC2 may interfere with the function of E-cadherin in gastric carcinomas, and have synergic effect on progression of gastric cancers.Zhang HK, Zhang QM, Zhao TH, Li YY, Yi YF. Expression of mucins and E-cadherin in gastric carcinoma and their clinical significance.

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Section: Discussioncontrasting

confidence: 56%

Expression of mucins and E-cadherin in gastric carcinoma and their clinical significance

Zhang

Zhang²,

Zhao³

et al. 2004

WJG

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“…MUC1 is a large highly glycosylated membrane-associated protein expressed in the apical surface of normal epithelial cells (Kufe, 2009). Aberrant expression of MUC1 has been associated to poor prognosis in several types of cancer (Reis et al, 1998;Sipaul et al, 2011), including canine mammary cancer and human breast cancer (de Oliveira et al, 2009;Kufe, 2009). An abnormal under-glycosylated form of MUC1 is overexpressed in scattered distribution throughout the membrane of cancer cells (Kufe, 2009).…”

Section: Introductionmentioning

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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“…MUC1 is distributed apically on normal glandular epithelial tissue (4,5) and its glycosylation patterns have been observed to be tissue specific (3). MUC1 expression has been correlated with a worse patient outcome in studies of several cancers (6)(7)(8)(9)(10)(11)(12)(13)(14) and is thought to play a role in progression and metastasis (3,15). Higher expression of aberrant forms of the MUC1 glycoprotein have been observed in a number of cancers (15)(16)(17)(18)(19)(20).…”

Section: Introductionmentioning

confidence: 99%

Characterization of MUC1 glycoprotein on prostate cancer for selection of targeting molecules

Burke

Gregg²,

Bakhtiar³

et al. 2006

Int J Oncol

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Abstract. MUC1 glycoprotein that is overexpressed in aberrant forms in epithelial cancers has been used for diagnosis, staging and therapy. As normal prostate and prostate cancer tissues express MUC1, it represents a potential target, but MUC1 epitopes specific to prostate cancer have not been well characterized. In order to assess MUC1 epitopes in prostate cancer, and their correlation with Gleason grades, binding of 7 wellcharacterized anti-MUC1 monoclonal antibodies (MAbs) (BrE-3, SM3, BC2, EMA, B27.29, HMFG-1 and NCL MUC1 core), were studied on a prostate tissue microarray. This microarray contained 197 prostate tissue cores representing: i) normal/benign prostate; ii) prostatic intraepithelial neoplasia and Gleason grades 1 and 2; and iii) Gleason grades 3-5. These MAbs bind the MUC1 extracellular domain, but have variable sensitivity to MUC1 glycosylation. To further characterize the effect of glycosylation on their binding, MAb reactivities with unglycosylated MUC1 core peptide and breast and prostate cancer cell lysates were compared. These studies demonstrated strong binding of BrE-3, BC2 and EMA to the peptide core and recognition by BrE-3, SM3, BC2 and EMA of hypoglycosylated MUC1. The results for the microarray indicated that higher Gleason grades were associated with markedly increased cellular staining by MAbs that preferentially recognize less glycosylated MUC1 p<0.001; SM3, p<0.004; EMA, p=0.009; and BC2, p<0.001

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Expression of fully and under-glycosylated forms of MUC1 mucin in gastric carcinoma

Cited by 106 publications

References 20 publications

Expression of mucins and E-cadherin in gastric carcinoma and their clinical significance

Expression of mucins and E-cadherin in gastric carcinoma and their clinical significance

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

Characterization of MUC1 glycoprotein on prostate cancer for selection of targeting molecules

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