CA 15–3 Assay for the Detection of Episialin

Hilkens, John

doi:10.1007/978-1-4612-0401-5_12

Cited by 3 publications

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“…In patients with breast and other carcinomas, shed episialin from the cancer cells can be detected in the circulation by the CA 15-3 assay, which is presently used for monitoring the course of breast cancer and for early detection of recurrent disease. 15 The cell-cell adhesion molecule, E-cadherin, linked by its cytoplasmic part via ␤-catenin or plakoglobin and ␣-catenin to the actin cytoskeleton, acts as an invasion suppressor. 16 The E-cadherin/catenin complex is often disturbed in cancer cells at various levels, namely by mutations in the cadherin or catenin genes, reduced stability of mRNAs, tyrosine phosphorylation of ␤-catenin, intra-and extracellular associations with other proteins, steric hindrance of enlarged proteoglycans and by ectodomain shedding of histidine alanine valine (HAV)-containing E-cadherin-specific peptides.…”

Section: -O-octadecyl-2-o-methyl-glycerophosphocholine (Et-18-ome)mentioning

confidence: 99%

Alkyl-lysophospholipid 1-O-octadecyl-2-O-methyl- glycerophosphocholine induces invasion through episialin-mediated neutralization of E-cadherin in human mammary MCF-7 cellsin vitro

et al. 2001

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1-O-octadecyl-2-O-methyl-glycerophosphocholine (ET-18 Key words: alkyl-lysophospholipid; E-cadherin; episialin; adhesion; invasion1-O-octadecyl-2-O-methyl-glycerophosphocholine (ET-18-OMe) interacts with cell membranes, thereby modulating phospholipid metabolism, interfering with signal transduction, inducing apoptosis and differentiation and regulating invasion. 1 On solid substrate, the E-cadherin/catenin complex is implicated in the cell-cell adhesion of 2 variants of the MCF-7 human breast cancer cell line family, coined MCF-7/AZ and MCF-7/6. In suspension, however, MCF-7/6 cells are adhesion-deficient while MCF-7/AZ cells are adhesion-proficient. Treatment with ET-18-OMe caused antithetic effects on the 2 types of MCF-7 cells. ET-18-OMe restored the E-cadherin function in the adhesiondeficient MCF-7/6 cells, whereas it caused a decrease in cellular aggregation of the adhesion-proficient MCF-7/AZ cells. The latter effects could not be explained by changes in sialylation of Ecadherin. 2 Antithetic effects on invasion have also been reported: ET-18-OMe inhibited invasion of constitutively invasive cells, [3][4][5][6] whereas it induced invasion of otherwise noninvasive cells. 7,8 Inhibition of invasion in the presence of ET-18-OMe was explained by induction of host tissue resistance, 9 but the antithetic effects on cell-cell adhesion and the invasion-promoting effect of ET-18-OMe have not been explained.Adhesion and invasion are the result of a balance between promoter and suppressor molecules modulated by multiple intraand extracellular factors. The presence of the anti-adhesion molecule episialin on the 2 types of MCF-7 cells was observed in a previous study. 2 The aim of our study was to see whether ET-18-OMe affects invasion and adhesion through modulation of episialin and E-cadherin.Episialin is a heterodimeric molecule composed of a membrane anchor and an extracellular moiety. The membrane anchor consists of a cytoplasmatic domain of 68 amino acids and a transmembrane domain. The extracellular moiety consists of a large mucin domain containing a large number of O-linked glycans. 10 The carbohydrate side chains carry many sialic acid residues conveying a highly negative charge upon episialin. 11 Episialin is located at the apical surface of most glandular epithelial cells; it is over-expressed in carcinomas, often distributed over the entire cell surface. 11 Overexpression of episialin inhibits integrin-mediated cell adhesion to

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Section: -O-octadecyl-2-o-methyl-glycerophosphocholine (Et-18-ome)mentioning

confidence: 99%

Alkyl-lysophospholipid 1-O-octadecyl-2-O-methyl- glycerophosphocholine induces invasion through episialin-mediated neutralization of E-cadherin in human mammary MCF-7 cellsin vitro

et al. 2001

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Cell surface associated mucins: Structure and effects on cell adhesion

Hilkens

Wesseling

Vos

et al. 1995

Biochemistry of Cell Membranes

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Carcinoma-Associated MUC1 Detected by Immunoradiometric Assays

Norum¹,

Varaas²,

Kierulf³

et al. 1998

Tumor Biol

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Fifty-four anti-MUC1 antibodies submitted to the International Society for Oncodevelopmental Biology and Medicine (ISOBM) Workshop (TD-4) were evaluated in immunoradiometric assays, using sera from carcinoma patients and healthy donors. The carcinoma serum pool contained sera from 30 patients with advanced cancer (10 breast, 10 colon, and 10 ovarian). This serum pool contained 696 kU/l MUC1, 770 µg/l CEA, and 3,700 kU/l CA 125. The reference serum pool was obtained from 10 healthy women combined with 20 sera from pregnant women, of which half had elevated CA 125 (range 82–254 kU/l). The reference serum pool contained 13 kU/l MUC1, 2 µg/l CEA, and 65 kU/l CA 125. The Workshop antibodies were tested both as solid-phase antibodies and as tracer antibodies with the carcinoma serum pool. Twenty-two tracer antibodies and 38 solid-phase antibodies gave at least one combination with >10% binding of the tracer antibody for a total of 836 combinations. These were tested further with the reference serum pool. Antibodies used as tracers could be separated into three categories: Group 1 antibodies, MF06, MF11, B27.29, MF30, and Ma552, gave mainly ‘carcinoma-specific’ assays in combinations with the solid-phase antibodies, i.e. binding ratio between carcinoma MUC1 and reference MUC1 >10. Group 2 antibodies, DF3, 7540MR, A76-A/C7, BC4N154, M38, 7539MR, B12, GP1.4, 232A1, Mc5, and Ma695 gave both ‘specific’ and ‘nonspecific’ binding ratios depending on the solid-phase antibody used. Group 3 antibodies, 214D4, BC4E549, E29, BCP8, BC3, and 3E1.2, gave mainly ‘nonspecific’ combinations, i.e. ratios ≤10. All antibodies used to capture MUC1 on the solid phase gave both ‘specific’ and ‘nonspecific’ combinations depending on the tracer antibody used. Ten antibodies were clearly more efficient as solid-phase capture antibodies; Ma695, B12, M38, GP1.4, 214D4, MF06, B27.29, A76-A/C7, BC3, and KC4. Our findings indicate that the ability to detect ‘carcinoma-specific MUC1’ cannot be deduced from epitope specificity alone.

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CA 15–3 Assay for the Detection of Episialin

Cited by 3 publications

References 50 publications

Alkyl-lysophospholipid 1-O-octadecyl-2-O-methyl- glycerophosphocholine induces invasion through episialin-mediated neutralization of E-cadherin in human mammary MCF-7 cellsin vitro

Alkyl-lysophospholipid 1-O-octadecyl-2-O-methyl- glycerophosphocholine induces invasion through episialin-mediated neutralization of E-cadherin in human mammary MCF-7 cellsin vitro

Cell surface associated mucins: Structure and effects on cell adhesion

Carcinoma-Associated MUC1 Detected by Immunoradiometric Assays

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