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Multicenter Study of Immunoscintigraphy with Radiolabeled Monoclonal Antibodies in Patients with Melanoma1

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Multicenter Study of Immunoscintigraphy with Radiolabeled Monoclonal Antibodies in Patients with Melanoma1 [CANCER RESEARCH 46, 4817-4822, September 1986] Multicenter Study of Immunoscintigraphy with Radiolabeled Monoclonal Antibodies in Patients with Melanoma1 A. G. Siccardi,2 G. L. Buraggi, L. Callegaro, G. Mariani, P. G. Natali, A. Abbati, M. Bestagno, V. Caputo, L. Mansi, R. Masi, G. Panini-Ili, P. Riva, M. Salvatore, M. Sanguinati, L. Troncone, G. L. Turco, G. A. Scassettati, and S. Terrone Dipartimento di Biologia e Genetica, Università di Milano, Milano [A. G. S.J; Istituto Nazionale Tumori, Milano fG. L. B.J; Centro Ricerche-SORIN Biomedica, Saluggia [L. C..G.A. S.J; Istituto di Fisiologia Clínicadel Consiglio Nazionale delle Ricerche, Pisa [G. M.]; Istituto Tumori Regina Elena, Roma [P. G. N.]; Departments of Nuclear Medicine of Ospedale Maggiore, Bologna [A. A.], Spedali Civili, Brescia [M. B.], Università "La Sapienza", Roma [V. C.], Istituto Pascale, Napoli [L. M., M. Sai.], Ospedale di Careggi, Firenze fR. M.], Ospedale Bufalini-Cesena [G. P., P. R.J, Ospedali Galliera-Genova [M. San.], Università Cattolica, Roma [L. T.], Università di Torino, Torino [G. L. T.], Italy; and Department of Microbiology and Immunology, New York Medical College (S. F.], Valhalla, New York 10595 ABSTRACT in multiple metastatic lesions from different anatomic sites (9); A multicenter study was performed to analyze the efficacy of "Tc- (c) it is undetectable in normal tissues except in hair bulbs and and '"In-labeled F(ab')2 fragments of monoclonal antibody (MoAb) in limited areas of the Malpighian layer (7, 10); (d) it is present only in minute amounts in serum even in patients with advanced 225.28S (reactive with a high molecular weight melanoma associated antigen) to radioimage malignant lesions in patients with melanoma. A disease (11); (?) it has a high density on melanoma cells (12); total of 254 melanoma patients, carrying 412 documented melanoma (/) it is not susceptible to modulation by antibody (12); and (g) lesions, were studied in 10 nuclear medicine departments. A total of 377 it shows only a limited susceptibility to modulation by interfer lesions were visualized in 206 patients; in particular (a) 250 of 412 known ons (13). The anti-HMW-MAA MoAb 225.28S has an affinity higher than 10~8mol/liter (12), and when labeled with I25I,has lesions were visualized in 159 of 191 patients known to carry melanoma lesions; (b) 95 occult lesions were visualized in 61 patients of the same been shown to localize in human melanomas transplanted into group; and (c) 32 lesions were visualized in 15 of 63 patients without nude mice (14). diagnosed lesions. The melanomic nature of 101 of 127 radioimaged Previous studies performed at the Istituto Nazionale Tumori occult lesions was confirmed by clinical criteria and/or by additional in Milan have shown that (a) the injection of radiolabeled laboratory investigations. These results indicate that immunoscintigraphy with radiolabeled I (ali' )•fragmentsof MoAb 225.28S can provide clin MoAb 225.28S into melanoma patients results in specific lo calization of radioactivity in métastases(6), (b) F(ab')2 frag ically useful information. Analysis of the variables influencing the outcome of immunoscintig ments are markedly superior to the whole immunoglobulin (6), raphy with "Te- and '"In-labeled F(ab')z fragments of MoAb 225.28S and (c) I31I,I23I,"'In, and "Te are useful isotopes for labeling confirmed the role of size, anatomic site, and level of high molecular this MoAb for immunoscintigraphy (15). The localization of weight melanoma associated antigen in melanoma lesions. Such analysis radioactivity in metastatic lesions was shown to be antigen also showed, for the first time, the influence (a) of the isotope used to specific by "double tracer" experiments with a second radiola radiolabel the antibody fragments and (b) of the clinical stage of the beled MoAb of the same isotype and of irrelevant specificity (6, patients. The present study has shown good agreement in the results 15). Some of these conclusions are in agreement with results obtained by the 10 nuclear medicine departments, suggesting that im munoscintigraphy with radiolabelled !•(ab ' ); fragments of MoAb 225.28S recently reported by Larson et al. (16), who have used Fab fragments of a MoAb to an antigen with structural properties is a reliable procedure. similar to those of the HMW-MAA. To assess the clinical usefulness of melanoma immunoscin INTRODUCTION tigraphy by means of radiolabeled MoAbs and the degree of variability of results obtained in various nuclear medicine de The analysis of human tumors with monoclonal antibodies partments, F(ab')2 fragments of MoAb 225.28S were routinely has ¡(Imiitici]a variety of tumor-associated antigens (for review, prepared in the radiopharmaceuticals manifacturing facilities see Refs. 1-3). The restricted tissue distribution of some of of Sorin Biomedica (Saluggia, Italy) and distributed to 10 these antigens and the high degree of specificity of the corre nuclear medicine departments either labeled with '"In or as an sponding monoclonal antibodies have been exploited for ini "instant kit" for "Tc labeling. The aim of the present paper munoradioimaging procedures to visualize lesions in patients is to report the results of this multicenter study, which has with solid tumors (for review, see Refs. 4-6). Among the MoAb3-defined MAAs, the "high molecular investigated more than 250 patients. Preliminary results were weight" MAA (7) appears to meet the criteria of a useful marker presented at the European Symposium on Immunoscintigraphy (Saariselka, Finland, August 1984) (17). for immunoscintigraphy procedures in melanoma patients: Because previous studies (11) had not shown significantly HMW-MAA (a) is expressed by at least 90% of melanoma higher levels of HMW-MAA in the sera of melanoma patients lesions (8); (b) it displays only a limited degree of heterogeneity of any clinical stage, the serum level of HMW-MAA was not Received 2/10/86; revised 5/22/86; accepted 5/29/86. measured. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1This work was supported by several grants of the Consiglio Nazionale delle MATERIALS AND METHODS Ricerche Special Project "Technologie Biomediche e Sanitarie" and by USPHS grant CA 37959 (S. F.). 2 To whom requests for reprints should be addressed, at Dipartimento di Patients. A total of 254 informed patients, who signed a written Biologia e Genetica, Via Viotti 3/5, 20133 Milano, Italy. consent form, was studied in 10 Nuclear Medicine departments (Table 3 The abbreviations used are: MoAb, monoclonal antibody; DTPA, diethylene- 1). The clinical stage of the disease was defined according to the triamine pentaacetic acid; HMW, high molecular weight; MAA, melanoma classification of Stehlin et al. (18) and was distributed as follows: stage associated antigen; ISG, immunoscintigraphy; PBS, phosphate buffered saline; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; ISG-FN, I, 17%; stage II, 3%; stage III, 43%; stage IV, 37%. Documented immunoscintigraphy false negative; ISG-TN, immunoscintigraphy true negative; melanoma lesions (for a total of 412, 55% of which were readily i.d., intradermal(ly). accessible, being located in skin or in superficial lymph nodes) were 4817 Downloaded from cancerres.aacrjournals.org on October 2, 2021. © 1986 American Association for Cancer Research. ISG OF MELANOMA present in 191 patients No lesions had been detected in the remaining Scans were obtained by standardized techniques, as described (6); as 63 patients at the time of the study. an example, in Milan, scans were obtained with a double head whole- Monoclonal Antibodies and F(ab')z Fragments. The MoAbs 225.28S body gamma camera (KR7/LB/Gamma/Cat 2; SELO, Milan, Italy) (reactive with HMW-MAA) and 4C4 (reactive with hepatitis B virus connected with a computer (PDP 11/34; Digital Equipment Corpora surface antigen), both of the 7-2a isotype, are described elsewhere (7, tion, Maynard, MA); the gamma camera was equipped with a medium- 19). The MoAbs were purified from asci lie fluid using the caprilic acid high energy parallel-hole collimator setting at 364 keV, with a 30% precipitation procedure (20) and F(ab')2 fragments were generated by window. Similar equipment was used in the other nuclear medicine digestion of purified IgG using pepsin, as described (6, 21). Digested departments. In some patients, image enhancement was achieved by proteins were concentrated to 100 mg/ml, and F(ab')2 fragments were subtraction of the background radioactivity, as described by De Land purified by applying 1000 mg of protein in 10 ml to a Sephadex G-200 et al. (24). SF (Pharmacia Fine Chemicals, Uppsala, Sweden) column (5.0 x 100 The imaging studies were interpreted by two physicians in each cm) equilibrated with 0.01 M PBS, pH 7.4. The protein components in nuclear medicine department and subsequently reviewed by members the peaks were analyzed by SDS-PAGE. The pool containing F(ab')2 of other departments participating in the multicenter study. Confir fragments was applied to a Protein A-Sepharose CL6B column (1.0 x mation of occult lesions detected by immunoscintigraphy was obtained 10 cm) equilibrated with PBS. The effluent containing F(ab')2 frag by clinical examination, computed tomography, ultrasound, planar ments (approximate yield, 1 mg of F(ab')2/10 mg of intact IgG) was radiography, and histology tests on biopsy or autopsy. concentrated by ultrafiltration to approximately 2.5 mg/ml and stored Immunocytochemistry. Indirect immunoperoxidase analysis was per at -30*C until use. Purity of F(ab')2 fragments was demonstrated by formed as described (6) using the Vectastain ABC kit (Vector Labora SDS-PAGE. tories, Burlingame, CA). Peroxidase activity was detected using 3- Radiolabeling of l-'(al>')..Fragments.
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