Effect of estradiol and raloxifene on MUC1 expression and adhesive properties of Ishikawa cells

Paszkiewicz-Gadek, A; Porowska, Halina; Pietruczuk, Mirosława; Haczyński, Józef; Kisiel, Dariusz G.; Wołczyński, Sławomir

doi:10.3892/or.14.2.583

Cited by 6 publications

(8 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Flow cytometric analysis. To determine MUC1 expression on the cell membranes, fluorescein isothiocyanate (FITC)conjugated mouse anti-human MUC1 monoclonal antibody and mouse IgG1-FITC antibody as a negative control was used, according to the method described in our earlier study (14). Flow cytometric analysis was performed by Coulter Epics XL.…”

Section: Sds-page and Western Blottingmentioning

confidence: 99%

The influence of N- and O-glycosylation inhibitors on the glycosylation profile of cellular membrane proteins and adhesive properties of carcinoma cell lines

Paszkiewicz-Gadek¹,

Porowska²,

Lemancewicz³

et al. 2006

Int J Mol Med

Self Cite

View full text Add to dashboard Cite

The effects of N-and O-glycosylation inhibitors on the expression of membrane proteins (MUC1 and some integrins) were evaluated in human endometrial (Ishikawa) and breast (MCF-7) cancer cells. Subconfluent cells were treated with 1-3 mg% concentration of tunicamycin and 2-10 mM of benzyl-N-acetyl-•-galactosaminide for 1-2 days, and used for flow cytometry, immunohistochemical staining, adhesion test and Western blotting. Benzyl-N-acetyl-•-galactosaminide inhibits MUC1 expression on the surface of breast more than endometrial cancer cells. Tunicamycin reduces MUC1 concentration on the cellular surface more than benzylglycoside, and greatly reduces glycosylation of glycoproteins, causing an increase in cell adhesion in both types of cancer cells. The expression of •2ß1 integrins on the surface of these cells was weak and decreased after treatment with inhibitors. Two different glycoforms of MUC1 proteins in endometrial cells and three in breast cancer cells were expressed and their molecular weights were reduced after treatment with glycosylation inhibitors. It was confirmed with lectin detection of carbohydrate epitopes (Tn and T) in MUC1 proteins. These observations show that glycosylation inhibitors altered the N-and O-glycan patterns in a sufficient manner, and positively modified the biological features of cancer cells.

show abstract

Section: Sds-page and Western Blottingmentioning

confidence: 99%

The influence of N- and O-glycosylation inhibitors on the glycosylation profile of cellular membrane proteins and adhesive properties of carcinoma cell lines

Paszkiewicz-Gadek¹,

Porowska²,

Lemancewicz³

et al. 2006

Int J Mol Med

Self Cite

View full text Add to dashboard Cite

show abstract

“…TAM activated 17 regions with ER-α in these cancer cells; in contrast, RAL activated only two regions, explaining their different effects on endometrium and suggesting that TAM is a nonselective ER subtype SERM, whereas RAL is a relatively ER-β-selective SERM (Ball et al, 2009). Paszkiewicz-Gadek et al (2005) examined the effect of RAL or E2 on the expression of MUC1 (a transmembrane protein with a large mucin-like extracellular domain protruding above the cell surface), which plays a crucial role in cancer progression and metastasis. RALtreated Ishikawa cells showed increased MCU1 biosynthesis and an increase in the MCU1 level on the cell surface (Paszkiewicz-Gadek et al, 2005).…”

Section: Williams-brown Et Al (2011) Used the Nonmalignant Immortalimentioning

confidence: 97%

“…Paszkiewicz-Gadek et al (2005) examined the effect of RAL or E2 on the expression of MUC1 (a transmembrane protein with a large mucin-like extracellular domain protruding above the cell surface), which plays a crucial role in cancer progression and metastasis. RALtreated Ishikawa cells showed increased MCU1 biosynthesis and an increase in the MCU1 level on the cell surface (Paszkiewicz-Gadek et al, 2005).…”

Section: Williams-brown Et Al (2011) Used the Nonmalignant Immortalimentioning

confidence: 99%

Could in-vitro studies on Ishikawa cell lines explain the endometrial safety of raloxifene? Systematic literature review and starting points for future oncological research

Gizzo

Noventa²,

Gangi³

et al. 2015

European Journal of Cancer Prevention

View full text Add to dashboard Cite

To evaluate all the in-vitro raloxifene (RAL) mechanisms of action on normal, Ishikawa, and different endometrium-derived cell lines to explain the in-vivo RAL endometrial effects, a systematic literature search was performed in the electronic databases MEDLINE, EMBASE ScienceDirect, and the Cochrane Library for the time period between 2002 and 2012. Outcomes were considered in relation to in-vitro stimulatory, inhibitory, or neutral actions of RAL in Ishikawa cell lines compared with different endometrial-derived cell lines (both cancerous and normal endometrium). We also considered all the RAL molecular mechanisms responsible for the in-vitro effects observed. More than 150 articles were available in the scientific database literature, but only 21 fulfilled our selection criteria. Although in-vitro studies appear to yield conflicting results, most evidence has shown that RAL seems to induce endometrial cell mitochondria-mediated apoptosis, and to inhibit estrogen-related cell proliferation and endometrial carcinogenesis by inducing antiangiogenic factors, and reducing cytoskeletal reorganization. If the endometrial safety profile of RAL is confirmed, in the near future, selective estrogen receptor modulators could represent an efficient alternative adjuvant treatment to tamoxifen (TAM) in women with breast cancer considered to be at an increased risk of endometrial disease. The confirmation of the endometrial safety profile could enable the proposal of RAL by clinicians as the most appropriate treatment for BRCA1-2 patients after prophylactic salpingo-oophorectomy.

show abstract

“…Cells were detached from tissue culture flasks with 0.2% EDTA in PBS, pH 7.4 and washed in PBS containing 1% BSA and 0.1% NaN 3 (PBS/1% BSA). To determine MUC1 expression on cell surface, the detached cells were incubated with fluorescein isotiocyanate (FITC)-conjugated mouse anti-human MUC1 monoclonal antibody, according to the method described for Ishikawa cell line in our earlier study [18]. Mouse IgG1-FITC antibody was used as a negative control.…”

Section: Quantitative Determination Of Muc1 By Measurement Of Incorpomentioning

confidence: 99%

“…Adhesion assay was performed with control and TNF-α stimulated cells, according to the method described earlier [18]. Fibronectin coated plates (BD Pharmingen, 96-well) and plates coated with collagen type I (100 μg/ml) were blocked for 90 min at 37°C with 1% heat-denatured BSA.…”

Section: Quantitative Determination Of Muc1 By Measurement Of Incorpomentioning

confidence: 99%

Expression of MUC1 mucin in human umbilical vein endothelial cells (HUVEC).

Porowska

Paszkiewicz-Gadek²,

Wosek³

et al. 2010

Folia Histochem Cytobiol.

Self Cite

View full text Add to dashboard Cite

Mucin 1 (MUC1) is a membrane-bound glycoprotein that is expressed by various epithelial cell types. MUC1 functions include modulation of cell adhesion, signal transduction, lubrication and hydration of epithelial surfaces, and their protection from infection. In this study we demonstrated that MUC1 is expressed in human umbilical vein endothelial cells (HUVECs) and could be released/shed from cellular membrane. MUC1 presence in these cells was verified using three methods: Western blotting, flow cytometry and metabolic labeling. We also showed that mucin expression is stimulated by proinflammatory cytokines: about a 2-fold increase was observed after TNF-α treatment and lower after IFN-γ alone and in combination with TNF-α treatment. It can be assumed that the presence of MUC1 in endothelial cells may have an important role in the interactions with different cell types in physiological and pathological processes.

show abstract

Effect of estradiol and raloxifene on MUC1 expression and adhesive properties of Ishikawa cells

Cited by 6 publications

References 0 publications

The influence of N- and O-glycosylation inhibitors on the glycosylation profile of cellular membrane proteins and adhesive properties of carcinoma cell lines

The influence of N- and O-glycosylation inhibitors on the glycosylation profile of cellular membrane proteins and adhesive properties of carcinoma cell lines

Could in-vitro studies on Ishikawa cell lines explain the endometrial safety of raloxifene? Systematic literature review and starting points for future oncological research

Expression of MUC1 mucin in human umbilical vein endothelial cells (HUVEC).

Contact Info

Product

Resources

About