Tumor Localization of Radio-Labeled Antibodies against Carcinoembryonic Antigen in Patients with Carcinoma

Mach, Jean‐Pierre; Carrel, S; Forni, M.; Ritschard, J; Donath, A; Alberto, P.

doi:10.1056/nejm198007033030102

Cited by 369 publications

(78 citation statements)

References 8 publications

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“…Recent reports have demonstrated variable removal of covalently bound 125I from injected proteins, raising the possibility of inaccuracies in t/2 measurements for the relevant proteins (40,41). In view of this, experiments were performed to evaluate the proportions of 1251 counts circulating in free form, and protein-bound, as judged by gel filtration of samples obtained sequentially after injection.…”

Section: Resultsmentioning

confidence: 99%

Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

et al. 1988

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Section: Resultsmentioning

confidence: 99%

Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

et al. 1988

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“…Immunoscintigraphy of from ascites by affinity chromatography on a protein Atumours in patients has primarily been successful in Sepharose column (Pharmacia, Uppsala, Sweden). F(ab')2 melanoma (Larson et al, 1985;Siccardi et al, 1986), fragments of TP-1 were obtained by digestion with pepsin colorectal cancer (Mach et al, 1980;Mach et al, 1983; for 8 h using a pepsin/IgG ratio of 3/100 (weight/weight) Chatal et al, 1985), and ovarian cancer (Epenetos et al, (Parham, 1983. So far less work has been reported on the The purity of the antibody preparations was checked by disgnostic use of MoAbs in sarcoma patients (Armitage et polyacrylamide gel electrophoresis (Laemmli, 1970), and by al., 1986;Greager et al, 1986).…”

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confidence: 99%

Selective localisation of two radiolabelled anti-sarcoma monoclonal antibodies in human osteosarcoma xenografts

Bruland¹,

Fodstad²,

Skretting³

et al. 1987

Br J Cancer

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Two mouse monoclonal antibodies (MoAbs), TP-1 and TP-3, previously shown in immunohistochemical studies to react with osteosarcomas, were labelled with 125I or 131I and evaluated for their ability to localise to human osteogenic sarcoma xenografts after intravenous injection. The radiolabelled TP-1 and TP-3 MoAbs had immunoreactive fractions of 70% and 67%, respectively, and bound to target cells with binding constants of 8.5 X 10(8) M-1 and 4.0 X 10(9) M-1, respectively. After injection of labelled TP-3 IgG, approximately 16% of the dose X g-1 tissue was found in the tumour after 24 hours. Maximum tumour/blood radioactivity ratios of 6-7 were achieved 3-4 days after antibody injection, while the ratios for the normal tissues were less than 1. The tumours could be clearly visualised by whole-body gamma scintigraphy without the need for subtraction techniques. The TP-1 IgG accumulated to a large extent also in the spleen. Hence, with this antibody the tumour was less well delineated from the adjacent normal tissues. However, the F(ab')2 fragments, derived from the TP-1 IgG, gave tumour/blood ratios up to approximately 40 after 3-4 days and yielded sharp gamma scintigrams of the tumour. Specificity of the antibody localisation was indicated by the lack of accumulation in a contralateral melanoma xenograft and the failure of 2 isotype-matched irrelevant MoAbs to localise to the sarcomas. With the F(ab')2 fragments satisfactory images could be obtained already after 16 hours. The results suggest that this preparation may be useful in clinical radioimmunodetection of osteogenic sarcomas.

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“…Radiolabelled monoclonal antibodies (MAbs) are used for the diagnosis and the therapy of cancer and some benign diseases (Mach et al, 1980;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.…”

Section: Model; Immunoscintigraphymentioning

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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Tumor Localization of Radio-Labeled Antibodies against Carcinoembryonic Antigen in Patients with Carcinoma

Cited by 369 publications

References 8 publications

Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

Selective localisation of two radiolabelled anti-sarcoma monoclonal antibodies in human osteosarcoma xenografts

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

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