99Tcm-labelled anti-CEA monoclonal antibody for tumour immunoscintigraphy

Baum, R. P.; Hertel, A.; Lorenz, M.; Schwarz, A.; Encke, A.; G, Hör

doi:10.1097/00006231-198905000-00005

Cited by 96 publications

(27 citation statements)

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“…The apparent tumor specificity is thought to be a reflection of the restricted ability of the antibody to gain access to luminal spaces and hence the normal mucosa, whereas the disrupted tissue architecture associated with tumor growth allows access of the antibody to its target antigen. The in vivo and in vitro properties of PR1A3 differentiated it from other antibodies used for colorectal tumor imaging, especially anti-carcinoembryonic antigen (CEA) antibodies (4,5). These differences included the observations that 59 of 60 tumors studied bound PR1A3 (1), in contrast to a clinical study where only 70% of colorectal tumors were imaged by an anti-CEA antibody (6).…”

mentioning

confidence: 99%

An epitope on carcinoembryonic antigen defined by the clinically relevant antibody PR1A3.

Durbin

Young

Stewart

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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The monoclonal antibody PR1A3 has been used successfully for in vivo imaging of colorectal cancers, and several properties associated with this antibody, including minimal reactions of the antibody with circulating antigen in patients' sera, differentiate it from anti-carcinoembryonic antigen (CEA) antibodies used in similar studies. However, the antigen bound by PR1A3 was identified as CEA by analysis of somatic cell hybrids and by antigen expression from yeast artificial chromosomes, cosmids, and cDNA clones. The molecular weight, presence of a glycosyl-phosphatidylinositol anchor, elevation of surface expression by y-interferon, and N-terminal amino acid sequence all confirmed the antigen identification as CEA. A series of biiary glycoprotein-CEA hybrid proteins was produced which demonstrated that the epitope bound by the antibody was at the site of membrane attachment and involved parts of the glycosyl-phosphatidylinositol anchor and the B3 domain of CEA to form a conformational epitope. Access to this epitope, although possible when the antigen was on the cell surface, appeared to be blocked when CEA was released from the cell. The nature and location of the epitope on CEA are proposed to be responsible for the unique properties of the antibody.

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mentioning

confidence: 99%

An epitope on carcinoembryonic antigen defined by the clinically relevant antibody PR1A3.

Durbin

Young

Stewart

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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“…6) in contrast to normal lung tissue. CEA is a tumor-associated antigen (49), also present in vivo in colorectal (50)(51)(52)(53)(54), breast (36,54,55), urinary bladder (56) and medullary thyroid cancers (57), tumors that-according to observations made by us and others (50-57)-can be visulaized with the radioantibody used in the present study.…”

Section: Discussionmentioning

confidence: 67%

Radioimmunoimaging of Non-Small Cell Lung Cancer with¹¹¹In- and^99MTc-Labeled Monoclonal Anti-Cea-Antibodies

et al. 1993

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“…Serum samples obtained from five patients who received 9'Tc-labelled murine MAb against CEA, designated BW431/126 (Baum et al, 1989) were used as control in the measurement of serum levels of HAMA and human anti-chimera antibody (HACA).…”

Section: Materids and Methodsmentioning

confidence: 99%

Different biodistribution of 99mTc-labelled chimeric mouse-human monoclonal antibody between athymic mice model and human

Oriuchi

Watanabe²,

Sugiyama³

et al. 1996

Br J Cancer

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Sinary Biodistribution of chimeric mouse/human monoclonal antibody against non-specific cross-reacting antigen (chNCA Ab) was studied in athymic mice and patients with metastatic bone disease. 9=-rc-chNCA Ab showed a high labelling efficiency, stability and also a high binding ratio to human granulocytes. Since NCA showed cross-reactivity with carcinoembryonic antigen (CEA), animal experiments showed that 99"c-chNCA Ab was accumulated in the xenografted tumour which expressed CEA, suggesting the preserved immunoreactivity of labelled materials. In the clnical study, injected 99rc-chNCA Ab formed a high molcular weight complex immediately after intravenous aministration and was trapped mainly in liver. The first-phase plasma half-life was 6.4+ 1. Locher et al., 1986; CourtenayLuck et al., 1984). Production of the human anti-murine antibody (HAMA) is one of the most serious problems as far as murine MAbs are concerned. HAMA, produced in the sera of patients who received murine MAbs repeatedly, may result in the neutralisation of infused MAb or in allergic reactions (Schroff et al., 1985;Shawler et al., 1985). Recent developments in genetic engineering enable us to use chimeric mouse-human MAbs which are expected to decrease the HAMA production, since chimeric MAbs consist of mouse variable regions and human constant regions (Boulianne et al., 1984). However, there has been a report which describes the production of HAMA in serum samples of metastatic colorectal cancer patients after administration of chimeric MAb designated B72.3 (Khazaeli et al., 1991).Non-specific cross-reacting antigen (NCA) is expressed on the surface of human granulocytes and cross-reacts with carcinoembryonic antigen (CEA) (von Kleist et al., 1972). Therefore, radiolabelled anti-NCA Ab has been successfully used for the diagnosis of infectious diseases and bone metastases of malignancies, although the distinction would not be made between sites of inflammation and sites of cancer expressing CEA (Locher et al., 1986;Reuland et al., 1991;Munz et al., 1990).In this study, chimenrc antibody against the NCA (chNCA Ab) was labelled with 9Tc pertechnetate, since 99'Tc was an ideal radionuclide for radioimmunodetection, and administered into tumour-beanng athymic mice and patients to compare the biodistribution. Patients with bone metastasis from prostate cancer were chosen for the clinical application, since prostate cancer often shows osteogenic metastasis, which could be imaged as a photopenic area on the immunoscintigraphy using radiolabelled anti-NCA Ab. Materids and methodsMurine and chimeric mouse-human anti-NCA antibodies Murine anti-NCA Ab (mNCA Ab), IgG, isotype, was purified from ascites of Balb/c mouse inoculated intraperitoneally with hybridoma cells that were produced by the fusion of mouse myeloma cells and anti-NCA Ab-producing B-cells derived from Balb/c mouse immunised with CEA. Derived mNCA Ab reacted to NCA 50 and NCA 90. chNCA Ab was prepared by the method previously reported (Koga et al., 1990). VY(VK) gene, isolated from hybr...

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99Tcm-labelled anti-CEA monoclonal antibody for tumour immunoscintigraphy

Cited by 96 publications

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An epitope on carcinoembryonic antigen defined by the clinically relevant antibody PR1A3.

An epitope on carcinoembryonic antigen defined by the clinically relevant antibody PR1A3.

Radioimmunoimaging of Non-Small Cell Lung Cancer with¹¹¹In- and^99MTc-Labeled Monoclonal Anti-Cea-Antibodies

Different biodistribution of 99mTc-labelled chimeric mouse-human monoclonal antibody between athymic mice model and human

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99Tcm-labelled anti-CEA monoclonal antibody for tumour immunoscintigraphy

Cited by 96 publications

References 0 publications

An epitope on carcinoembryonic antigen defined by the clinically relevant antibody PR1A3.

An epitope on carcinoembryonic antigen defined by the clinically relevant antibody PR1A3.

Radioimmunoimaging of Non-Small Cell Lung Cancer with111In- and99MTc-Labeled Monoclonal Anti-Cea-Antibodies

Different biodistribution of 99mTc-labelled chimeric mouse-human monoclonal antibody between athymic mice model and human

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Radioimmunoimaging of Non-Small Cell Lung Cancer with¹¹¹In- and^99MTc-Labeled Monoclonal Anti-Cea-Antibodies