CEA-related proteins on human urothelial cell lines of different transformation grades

Krop‐Watorek, Anna; Laskowska, Anna; Salwa, J; Kl̶opocki, Arkadiusz G.; Fritz, Günter; Ugorski, Maciej

doi:10.1016/s0304-3835(98)00363-2

Cancer Letters

1999

DOI: 10.1016/s0304-3835(98)00363-2

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CEA-related proteins on human urothelial cell lines of different transformation grades

Anna Krop‐Watorek

Anna Laskowska

J Salwa

et al.

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Cited by 5 publications

(1 citation statement)

References 22 publications

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“…Carcinoembryonic antigen (CEA) is an oncofoetal glycoprotein present in normal foetal gastrointestinal tissues and in some tumours of epithelial origin (Gold & Freedman, 1965;Chu et al, 1972;Fritsche & Mach, 1977;Nap et al, 1988;Jothy et al, 1993). The elevated levels observed in colon, lung, breast and ovarian adenocarcinomas in comparison with normal adult tissues suggest that CEA could play an important role in cancer progression and embryogenesis (von Kleist et al, 1986;Wagner et al, 1992;Eidelman et al, 1993;Jessup et al, 1999;Krop-Watorek et al, 1999).…”

mentioning

confidence: 99%

Adhesive properties of carcinoembryonic antigen glycoforms expressed in glycosylation-deficient Chinese hamster ovary cell lines.

Krop‐Watorek

Kl̶opocki²,

Czerwiński³

et al. 2002

Acta Biochim Pol

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Carcinoembryonic antigen (CEA) is an oncofoetal cell surface glycoprotein that serves as an important tumour marker for colorectal and some other carcinomas. Its immunoglobulin-like structure places CEA within the immunoglobulin superfamily. CEA functions in several biological roles including homotypic and heterotypic (with other CEA family members) cell adhesion. Cell-cell interaction can be modulated by different factors, e.g., post-translational modifications such as glycosylation. The purpose of this study was to examine whether changes in carbohydrate composition of CEA oligosaccharides can influence homotypic (CEA-CEA) interactions. In order to modulate glycosylation of CEA we used two different glycosylation mutants of Chinese hamster ovary (CHO) cells, Lec2 and Lec8. Lec2 cells should produce CEA with nonsialylated N-glycans, while Lec8 cells should yield more truncated sugar structures than Lec2. Parental CHO (Pro5) cells and the glycosylation deficient mutants were stably transfected with CEA cDNA. All three CEA glycoforms, tested in a solid-phase cell adhesion assay, showed an ability to mediate CEA-dependent cell adhesion, and no qualitative differences in the adhesion between the glycoforms were observed. Thus, it may be assumed that carbohydrates do not play a role in homotypic adhesion, and the interactions between CEA molecules depend solely on the polypeptide structure. Vol. 49 No. 1/2002273-283 QUARTERLY . Abbreviations: CEA, carcinoembryonic antigen; CHO cells, Chinese hamster ovary cells; PBS (-) , phosphate-buffered saline lacking Ca +2 and Mg +2 .

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mentioning

confidence: 99%

Adhesive properties of carcinoembryonic antigen glycoforms expressed in glycosylation-deficient Chinese hamster ovary cell lines.

Krop‐Watorek

Kl̶opocki²,

Czerwiński³

et al. 2002

Acta Biochim Pol

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Two new synthetic peptides from the N‐domain of CEACAM1 (CD66a) stimulate neutrophil adhesion to endothelial cells

Skubitz

2011

Biopolymers

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Four members of the carcinoembryonic antigen family, CEACAMs 1, 3, 6, and 8, are expressed on human neutrophils and can trigger an activation signal that increases neutrophil adhesion to human umbilical vein endothelial cell (HUVEC) monolayers. To identify active sites on CEACAM1, we previously performed molecular modeling using IgG and CD4 as models, and 28 peptides of 14 amino acids in length were synthesized that were predicted to be present at loops and turns between β-sheets. Three peptides, each from the N-terminal domain, increased neutrophil adhesion to HUVEC monolayers and upregulated cell-surface CD11b/CD18 expression on neutrophils. In our earlier study, one N-domain peptide (CD66a-7) was not successfully synthesized, and another N-domain peptide (CD66a-6) was not soluble in the assay system. In the present study, we have now successfully synthesized CD66a-7, and a new peptide (CD66a-6L), that is a modification of the peptide that was insoluble in the earlier study. Both of these new peptides increased neutrophil adhesion to HUVEC monolayers. Importantly, the amino acid sequence of CD66a-7 is identical to the homologous peptides from CEACAMs 3, 5, and 6, but differs from the homologous peptide of CEACAM8, which was not active in this system. CD66a-6L is identical to the homologous peptide from CEACAM6. The data suggest that peptide motifs from at least five regions of the N-terminal domain of CEACAM1 are involved in the interaction of CEACAM1 with other ligands and can initiate signal transduction in neutrophils. Some of these active peptides are identical to homologous regions of other CEACAMs.

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In vitro and in vivo studies on antitumor effects of gossypol on human stomach adenocarcinoma (AGS) cell line and MNNG induced experimental gastric cancer

Gunassekaran

Priya

Gayathri

et al. 2011

Biochemical and Biophysical Research Communications

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CEA-related proteins on human urothelial cell lines of different transformation grades

Cited by 5 publications

References 22 publications

Adhesive properties of carcinoembryonic antigen glycoforms expressed in glycosylation-deficient Chinese hamster ovary cell lines.

Adhesive properties of carcinoembryonic antigen glycoforms expressed in glycosylation-deficient Chinese hamster ovary cell lines.

Two new synthetic peptides from the N‐domain of CEACAM1 (CD66a) stimulate neutrophil adhesion to endothelial cells

In vitro and in vivo studies on antitumor effects of gossypol on human stomach adenocarcinoma (AGS) cell line and MNNG induced experimental gastric cancer

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