SCLC-cluster-2 antibodies detect the pancarcinoma/epithelial glycoprotein EGP-2

Leij, de Louis; Helrich, W; Stein, Rhona; Mattes, M. Jules

doi:10.1002/ijc.2910570713

Cited by 83 publications

(45 citation statements)

References 29 publications

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“…in the bone marrow and in ascitic¯uid (Bjork et al, 1993;de Leij et al, 1994;Momburg et al, 1987;Shetye et al, 1988;Stein et al, 1994). Yet, it has not been known, whether the molecule may be actively involved in tumor progression.…”

Section: Discussionmentioning

confidence: 99%

“…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%

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

Würfel

Rösel

Seiter³

et al. 1999

Oncogene

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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.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Würfel

Rösel

Seiter³

et al. 1999

Oncogene

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“…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). Several antibodies to EGP-2 cell-surface protein have been described, but the most widely utilized is the monoclonal antibody Ber-EP4 (Latza et al, 1990).…”

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confidence: 99%

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

et al. 1999

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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.

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“…Antibodies used to activate myeloid cells included the EGP-2-specific mouse MAbs MOC31 (IgG1) and MOC181 (IgG2a), 24 which recognize the same epitope on EGP-2. As isotype-matched control antibodies with irrelevant specificity MAbs R73 (mouse antirat TcR, IgG1) and WT32 (mouse antihuman CD3, IgG2a) were used.…”

Section: Antibodiesmentioning

confidence: 99%

“…This latter observation in particular opens up possibilities to exploit this concept clinically in a 2-phase treatment setting. The high-affinity anti-EGP-2-directed mouse IgG1 antibody MOC31 24,26 could thus be used to attain optimal tumor localization without premature binding of the antibody to circulating FcR-positive cells in the blood. Subsequently applied human antimouse Ig will deposit specifically on MOC31-opsonized tumor tissue, thereby providing optimal conditions for local activation of myeloid cells.…”

mentioning

confidence: 99%

Tumor‐targeted immune complex formation: Effects on myeloid cell activation and tumor‐directed immune cell migration

Kroesen¹,

McLaughlin²,

Schuilenga-Hut

et al. 2002

Intl Journal of Cancer

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The effectiveness of cellular immunotherapy of solid tumors is often hampered by the lack of specific infiltration of immune effector cells into the tumor mass. Therefore, we studied the potential of tumor antigen-specific antibodies to elicit tumor-specific myeloid cell activation, to induce or enhance tumor infiltration by immune cells. To this end, we developed an in vitro model system using the human myeloid cell line MonoMac-6. Incubation of IFN-␥-primed MonoMac-6 cells with serum-opsonized zymosan or EGP-2-directed, mouse IgG2a-opsonized, EGP-2-positive tumor cells resulted in the production of ROS and TNF-␣ and induced E-selectin and ICAM-1 expression on HUVECs. FcR-mediated MonoMac-6 cell activation was strictly dependent on the activation of MonoMac-6 cells with IFN-␥. In addition, no myeloid cell activation was observed in the presence of human serum or using tumor antigen-specific mouse antibody subclasses other than IgG2a, suggesting the crucial involvement of CD64 (Fc␥R1) in the effects observed. However, serum-inhibited myeloid cell activation was completely restored employing a 2-step targeting approach in which tumor cell opsonization with mouse anti-EGP-2 antibodies was followed by incubation with human antimouse Ig antibodies. Moreover, using this 2-step approach, not only anti-EGP-2-directed mouse IgG2a but also mouse IgG1 antibodies effectively induced tumor-specific myeloid cell activation. In conclusion, we describe a method to induce efficient and tumorspecific activation of myeloid cells based on the sequential use of mouse tumor antigen-specific and human antimouse Ig antibodies. Targeted myeloid cell activation may provide a means to aid in the induction of a tumor-directed immune response and as such, the method described here could be of clinical significance.

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SCLC-cluster-2 antibodies detect the pancarcinoma/epithelial glycoprotein EGP-2

Cited by 83 publications

References 29 publications

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

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

Tumor‐targeted immune complex formation: Effects on myeloid cell activation and tumor‐directed immune cell migration

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