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In 14 patients with breast cancer the results of radioimmunoscintigraphy with 123I-labeled b-12 monoclonal antibody fragments were correct in more than two thirds of the patients.
Our purpose in conducting this study was to evaluate the efficacy of an 111In-labeled murine monoclonal antibody directed against a high-molecular-weight glycoprotein in localizing metastatic melanoma in 15 patients with previously documented disease and to determine the effect of antibody mass (2.5, 5.0, and 10.0 mg) on blood clearance, biodistribution, and lesion detection. Five mCi of 111In-antibody were infused over 1 hour, and patients were scanned at 24 and 72 hours after injection without computer enhancement or background subtraction techniques. No significant differences in the organ distribution, urine excretion, or plasma disappearance curves were noted at the three antibody dose levels. There were no acute reactions. The scan detected tumor in 9 of 12 (75%) patients with active disease, and 26 of 33 (79%) lesions greater than 1 cm. Patient management in 3 of 15 (20%) of patients studied was changed as a result.
Tumor uptake of 125I- and 131I-radiolabeled anti-CEA antibodies was compared in female Swiss nude mice, each bearing a CEA-producing human colon adenocarcinoma xenografted in one flank. Counts from the tumor and contralateral flank were recorded with a manipulatable, cadmium-telluride crystal gamma detector at 24, 48, and 72 hours following injection. The animals were killed, and the tumors and other organs were removed, weighed, and then assessed in an automatic gamma counter. The cadmium-telluride counter was more efficient at counting 125I-labeled antibodies than 131I antibodies. The tumor to contralateral flank ratios improved with the use of a monoclonal anti-CEA and polyclonal anti-CEA in combination compared with the single antibodies. The investigation of the external counting characteristics of the portable gamma detector demonstrated the potential of the adjunctive use of intraoperative detection with external radioimmunoscintigraphy for detection and localization of gastrointestinal tumors.
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The ability of radiolabeled monoclonal antibodies to accumulate in and image small human tumors growing in the spleen of athymic mice was assessed. The antibodies B6.2 and B72.3, which reacted against human breast (Clouser) and colon (LS174T) tumor cells in vitro and in vivo, respectively, and the isotype matched anti-horseradish peroxidase antibody which did not bind to these tumors were used in pharmacokinetic and imaging experiments. Human melanoma cells and tumors (A375) which did not react with any of the three antibodies were used as additional controls. Radioiodinated "tumor specific" and non-specific antibodies were injected i.v. into athymic mice bearing intrasplenic tumors and the mice were sacrificed at various times to assess the specificity of uptake of these antibodies into tumor and normal host tissues. The accumulation of B6.2 in the Clouser tumor was maximal at 24 h as indicated by a localization index (specific/nonspecific antibody in tumor divided by the same ratio in blood) of about 4.0. The uptake of B72.3 in LS174T tumor increased with time with a localization index of about 12.0 observed at 50 h post-antibody injection. Localization indices for the control A375 tumor and for all normal mouse tissues, including the uninvolved portion of the tumor bearing spleen, were between 0.8 and 1.0, thus indicating no specific antibody accumulation. The relative blood flows of the Clouser and A375 tumors, as determined by the 86RbCl method, were similar. The results suggested that immunospecificity was a major factor in antibody localization in vivo. Specific images of approximately 100-mg Clouser tumors with radiolabeled B6.2 and of LS174T tumor with radiolabeled B72.3 were seen by 24 h after antibody injection. Images of smaller (about 20 mg) LS174T tumors were seen by 48 h following B72.3 injection. The control antibody, anti-horseradish peroxidase, did not image either Clouser or LS174T tumor. Also the control tumor was not imaged with any of the three antibodies tested. The data generated with this novel animal model support the concept of using radiolabeled monoclonal antibodies for detecting and possibly treating small metastatic visceral tumors in cancer patients.
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Twenty-five patients, having either unilateral ovarian tumors of unknown etiology or suspected of having ovarian cancer recurrence were investigated by the method of immunoscintigraphy to rule out primary and/or metastatic tumor sites. Four-hundred micrograms of the tumor-associated monoclonal mouse antibody HMFG-2, raised against human milk fat globulin membranes and labeled with 123I, were used for each patient to display the tumor sites by external scintigraphy. The dose ranged between 0.5 and 2.2 mCi, the specific activity between 1.25 and 5.5 mCi per mg of antibody. Nineteen of the patients underwent operations a few days after immunoscintigraphy. The remaining six patients were investigated by transmission computed tomography (TCT) to establish the presence or absence of tumor of the imaging. In 22 of the 25 cases the scintigraphic results correlated with the situation found at the subsequent operation, or by TCT, respectively, as well as with the histological diagnosis of the tumor type. Overall, there were just two false-negative and one false-positive scan report, the latter due to faulty reading of the scintigrams. Sixteen out of 18 tumor sites in 25 patients could be revealed by immunoscintigraphy, the smallest one being 1.5 cm in diam. In four of the patients immunoscintigraphy was the only noninvasive investigation method that could reveal the malignant tumor sites prior to the operation.
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In seven women with carcinoma of the breast I-131-labeled antibodies to carcinoembryonic antigen (CEA) were administered subcutaneously in the finger webs. Subsequent scintigraphic immages demonstrated localization of radioactivity in the ipsilateral axillary metastases of all patients and in the contralateral axillae of three. Fifteen patients with either gastrointestinal or genitourinary cancers were studied as controls; in 12 both the hands and feet were injected with antibodies to CEA and in the other three either the hands or feet. Radioactivity was observed in the inquinal nodes of four control patients with tumors below the diaphragm and in the axillary nodes of one patient with a tumor above the diaphragm. The concentration of antibody in lymph node metastases from breast carcinoma was 100% specific. In those lymph nodes that presumably contained no metastatic tumor but demonstrated localization of labeled antibody, retention of CEA in the nodes from tumor drainage is postulated as the receptor site for the antibody.
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Mouse IgG2a monoclonal antibodies with specific binding reactivity in vitro to human tumors of the gastrointestinal tract were radioiodinated and injected into immunosuppressed mice xenografted with human colon carcinoma tumors. The antibodies preferentially localized in tumor tissue compared to normal mouse tissue, as determined by differential tissue counting of radioactivity. Preferential antibody localization in tumor tissue was greatly enhanced when F(ab')2 fragments of the antibodies were used, and the fragments localized specifically only in those tumors that bind the antibodies in vitro and not in unrelated tumors. Radiolabeled fragments of an anti-hepatitis virus monoclonal antibody of the same isotype as the specific antibody did not localize in tumors. Tumors could be located by whole-body gamma-scintigraphy with radiolabeled specific antibody F(ab')2 fragments without background subtraction.
Monoclonal antibody B72.3 binds to a glycoprotein complex with a molecular weight of 220,000 to 400,000. B72.3 reacts with approximately 50% of human mammary carcinomas and to 80% of the colon carcinomas tested but does not react appreciably with normal mammary tissue, with normal colon, or to a variety of normal adult human tissues tested using immunohistochemical techniques. B72.3 immunoglobulin G was purified and radiolabeled with 125I without significant loss in its reactivity to tumor extracts. The radiolabeled B72.3 immunoglobulin G was shown to efficiently localize human colon carcinoma xenografts in athymic mice. Tumor:tissue ratios of the localized antibody rose over the 7-day period studied, with tumor:liver, tumor:spleen, or tumor:kidney ratios of approximately 18:1 at Day 7 and a tumor:blood ratio of approximately 5:1 at Day 7. Tumor:muscle or tumor:brain ratios rose to over 100:1. The amount of radioactivity in the tumor increased for the first 2 days postinoculation of antibody and stayed constant over a 19-day period of study. Thus, there was no appreciable loss of radioiodine from the tumor over the study interval. No localization was seen in mice bearing a B72.3 antigen-negative human melanoma xenograft or with an isotype-identical control immunoglobulin G in mice bearing colon tumor xenografts. Gamma camera imaging with a pinhole collimator confirmed the ability of the radiolabeled antibody to detect the presence of colon carcinoma xenografts less than 0.5 cm in diameter over a 19-day period. The potential use of this system as a model for radioimmunotherapy will be discussed.
A monoclonal antibody 791T/36 prepared against human osteogenic sarcoma has been used to detect primary and metastatic colorectal carcinomas by external imaging of patients following injection of 131I-labelled antibody. In 10 of 11 patients radiolabelled 791T/36 antibody localized in tumours, the tumour: non tumour ratio of radioactivity ranging from 1.5:1 to 8.1. 791T/36 antibody was also evaluated for its potential for targeting anti-tumour agents including cytotoxic drugs (Vindesine) and immunomodulating agents (interferon0. Vindesine-791T/36 conjugates were preferentially cytotoxic in vitro for target cells expressing the 791T/36 antibody defined antigen. Also interferon conjugated to 791T/36 antibody, like free interferon activated peripheral blood natural killer cell activity. These in vitro tests together with related studies on antibody localization in vivo indicate the potential of monoclonal antibody targeting of anti-tumour agents.
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