Epithelial glycoprotein is a member of a family of epithelial cell surface antigens homologous to nidogen, a matrix adhesion protein.

Simon, Babette; Podolsky, Daniel K.; Moldenhauer, Gerhard; Isselbacher, Kurt J.; Gattoni‐Celli, Sebastiano; Brand, Stephen

doi:10.1073/pnas.87.7.2755

Cited by 99 publications

(74 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…TACSTD1, which was induced 20-fold in the liver and 22-fold in the inguinal lymph nodes with melanoma, encodes a carcinomaassociated antigen that functions as a homotypic calciumindependent cell adhesion molecule (Simon et al, 1990). The induced expression of TACSTD1 was confirmed by qRT-PCR (Table 6).…”

Section: Differential Gene Expression In Melanoma Compared With Normamentioning

confidence: 86%

Gene expression in Sinclair swine with malignant melanoma

Okomo-Adhiambo

Rink

Rauw

et al. 2012

Animal

View full text Add to dashboard Cite

Sinclair swine develop an aggressive form of melanoma, which, in many cases, spontaneously regresses after a complete metastatic phase. We used Affymetrix GeneChip R Porcine Genome Arrays consisting of 24 123 probe sets to compare gene expression in white blood cells (WBCs) and various tissues including the liver, lungs, inguinal lymph nodes and spleen harvested from a Sinclair piglet afflicted by melanoma at birth and exhibiting metastatic lesions at weaning (6 weeks) with those from a full-sibling piglet that showed no incidence of melanoma at birth and weaning. The highest number (3489; ,14%) of significantly upregulated transcripts (fold change in gene expression >2.0 and t-test P-value r0.05) was observed in the liver, while the spleen exhibited the lowest number of upregulated transcripts (528; ,2%). Among significantly downregulated genes, the highest numbers were observed in the inguinal lymph nodes (3651; ,15%) and the least in WBCs (730; ,3%). Differentially expressed transcripts included genes involved in melanoma pathogenesis including SILV, TYR and RAB28. SILV was over-expressed 784-, 430-and 164-fold, while TYR was over-expressed 138-, 81-and 28-fold in the liver, lungs and inguinal lymph nodes, respectively. Quantitative real-time RT-PCR (qRT-PCR) confirmed the microarray data of 12 selected differentially expressed sequences. These results suggest that significant changes in gene expression occur during metastasis of malignant melanoma in the Sinclair swine model. In addition, qRT-PCR analysis of the above 12 differentially expressed sequences was carried out on liver samples collected from 22 pigs (12 of which had melanoma during the first 6 weeks of life), and an ANOVA test contrasting absolute RNA expression between pigs with regressing, progressing and without tumors was significant for TYR, TACSTD1, MATP, GPNMB and CYP4A22, with P-values of 0.034, 0.015, 0.007, 0.050 and 0.022, respectively.

show abstract

Section: Differential Gene Expression In Melanoma Compared With Normamentioning

confidence: 86%

Gene expression in Sinclair swine with malignant melanoma

Okomo-Adhiambo

Rink

Rauw

et al. 2012

Animal

View full text Add to dashboard Cite

show abstract

“…C4.4A is a phophatidyl-inositol anchored molecule with partial sequence homology to uPAR (RoÈ sel et al, 1998). Here we report on the cloning and characterization of a molecule, named D5.7A, the ortholog to the murine and human panepithelial antigen EGP314, also known as EGP40, GA733-2, ESA, KSA, 17-1A antigen and Ep-CAM (Bergsagel et al, 1992;Bjork et al, 1993;Bumol et al, 1988;Edwards et al, 1986;Fernsten et al, 1990;GoÈ ttlinger et al, 1986;Lando et al, 1993;Larson et al, 1988;de Leij et al, 1994;Momburg et al, 1987;Nelson et al, 1996;Perez and Walker, 1989;Ross et al, 1984;Simon et al, 1990;Spurr et al, 1986;Stein et al, 1994;Strnad et al, 1989;Szala et al, 1990b). As revealed by transfection of non-metastasizing tumor cells, D5.7A appears to be a cell-cell adhesion molecule which may facilitate tumor progression by its growth promoting capacity upon ligand interaction.…”

Section: Introductionmentioning

confidence: 99%

Metastasis-association of the rat ortholog of the human epithelial glycoprotein antigen EGP314

Würfel

Rösel

Seiter³

et al. 1999

Oncogene

View full text Add to dashboard Cite

Screening for surface molecules expressed by metastasizing rat tumors had revealed evidence for metastasisassociation of a molecule also expressed on epithelial cells. The similarity to the expression pro®le of the panepithelial glycoprotein EGP314 prompted us to isolate and sequence the gene and to explore functional features of the molecule in transfected tumor lines. The molecule D5.7A, named according to the antibody, D5.7, used for selection, indeed, is the ortholog of EGP314 with 92% and 80% identity to the murine and the human molecules. Like EGP314, D5.7A has a particular cleavage site, a small cleavage product being resolved under reducing conditions from the membrane anchored part of the molecule. Transfection of a low metastasizing ®brosarcoma, pheochromoblastoma and adenocarcinoma revealed that expression of D5.7A facilitates tumor progression. Depending on the origin of the tumor, D5.7A transfectants either metastasized via the lymphatic system (pheochromoblastoma, adenocarcinoma) or hematogeneously (®brosarcoma). Particularly after proteolytic cleavage, D5.7A facilitated cell ± cell adhesion and provided a proliferative signal upon crosslinking. Thus, the rat ortholog of EGP314 is involved in metastasis formation. Importantly, its functional activities apparently rely on proteolytic cleavage. These ®ndings provide a ®rst evidence on how a panepithelial marker can be involved in tumor progression.

show abstract

“…The resultant PCR product was 515 bases. Because the primer sequences were obtained from the published cDNA sequence (Simon et al, 1990), the exon(s) amplified are unknown. At the beginning of our study, we tested whether the genomic DNA could be amplified with these primers.…”

Section: Pcrmentioning

confidence: 99%

“…The last approach is not restricted to one or a few tumour types, and is useful for the detection of tumour cells from many, as well as unknown, sites of origin in fluids or tissues. Recent reports indicate that epithelial glycoprotein 2 (EGP-2) is expressed on the surface of most epithelial cells and tumours (Simon et al, 1990;de Leji et al, 1994), but not by mesothelial cells (Latza et al, 1990). Although several different nomenclatures have been used for the gene and its protein product, we use the term EGP-2 as proposed by de Leij et al (1994).…”

mentioning

confidence: 99%

Development of a sensitive, specific reverse transcriptase polymerase chain reaction-based assay for epithelial tumour cells in effusions

et al. 1999

View full text Add to dashboard Cite

SummaryWe developed a sensitive and specific method for the detection of epithelial cancer cells in effusions with a two-stage molecularbased assay which combined enrichment for cancer cells by immunomagnetic bead selection and reverse transcriptase polymerase chain reaction (RT-PCR) detection of epithelial glycoprotein 2 (EGP-2) RNA. Preliminary experiments indicated that immunobead selection was essential to avoid occasional false-positive RT-PCR results, and this method detected ten breast cancer cells electively added to 10 7 cytologically negative effusion cells. We studied 110 cases of pleural (n = 68) and peritoneal (n = 42) effusions (30 from patients with known carcinoma and 80 from those without known carcinoma), and the results were compared with cytological findings. Of 18 effusions that were cytologically positive or suspicious for malignant cells, 17 (94%) were positive for EGP-2 RNA (the one negative sample was from a patient who recently received combination chemotherapy). Of 92 cytologically negative samples, 11 (12%) were positive for EGP-2, including six patients with a history of previous or current carcinoma. Our method appears to be highly specific and increases the sensitivity of detection of malignant cells; it may be a useful adjunct to routine cytopathological examination.

show abstract

Epithelial glycoprotein is a member of a family of epithelial cell surface antigens homologous to nidogen, a matrix adhesion protein.

Cited by 99 publications

References 34 publications

Gene expression in Sinclair swine with malignant melanoma

Gene expression in Sinclair swine with malignant melanoma

Metastasis-association of the rat ortholog of the human epithelial glycoprotein antigen EGP314

Development of a sensitive, specific reverse transcriptase polymerase chain reaction-based assay for epithelial tumour cells in effusions

Contact Info

Product

Resources

About