Abstract
Peanut lectin (PNA) has been shown to have a high affinity for Thomsen-Friedenreich (T) antigen, which is associated with the membrane of many solid tumour cells. PNA labelled with 131I was used as a tumour-imaging substance in patients with known metastatic cancer. Serial gamma scintiscans were obtained in 17 patients following a single injection of 131I-labelled PNA. Only in 1 patient was this technique able to reveal a known metastasis at analogue imaging. In the remaining patients, no visible uptake of 131I-PNA could be demonstrated at sites of known metastases. PNA is rapidly excreted through the kidneys and localises in the renal tubules. As a tumour-imaging agent, 131I-PNA appears to be without value, but its renalexcretory characteristics make it a potentially useful agent for the in vivo assessment of renal-tubular disorders.
Similar content being viewed by others
References
Boland CR, Montgomery CK, Kim YS (1982a) Alterations in human colonic mucin occurring with cellular differentiation and malignant transformation. Proc Natl Acad Sci USA 79:2051–2055
Boland CR, Montgomery CK, Kim YS (1982b) A cancer associated mucin alteration in benign colonic polyps. Gastroenterology 82:664–672
Boniface GR, Suresh MR, Willans DJ, Tam YK, Shysh A, Noujaim AA (1984) 131I-Labeled peanut lectin for the quantitative determination of renal tubular function. J Label Cpds Radiopharm 12:1129 (abstract)
Codington JF, Linsley KB, Jeanlot RW (1975) Immunochemical and chemical investigations of the structure of glycoprotein fragments obtained from epiglycanin, a glycoprotein at the surface of the TA3-Ha cancer cell. Carbohydr Res 40:171–182
Cooper HS (1982) Peanut lectin-binding sites in large bowel carcinoma. Lab Invest 47:383–390
De Vita VT Jr., Young RC, Cannellos GP (1975) Combination versus single-agent chemotherapy: review of the basis of selection of drug treatment of cancer. Cancer 35:98–110
Fraker PJ, Speck JC (1978) Protein and cell membrane iodinations with a sparingly soluble chloramide 1, 3, 4, 6-tetrachloro-3a, 6a diphrenylglycouril. Biochem Biophys Res Commun 80:849–857
Goldstein IJ, Hayes CE (1978) The lectins: Carbohydrate binding proteins of plants and animals. Adv Carbohydr Chem Biochem 35:127–340
Holt S, Longenecker BM, Terner UK, Noujaim AA, Styles CB (1983) Radioimmunodetection and treatment of human colon cancer in male mice using a monoclonal antibody. J Nucl Med 24:110 (abstract)
Holt S, Wilkinson A, Suresh MR, Mate G, Reid WB, Longenecker BM, McPherson TA, Noujaim AA (1985) Radiolabelled peanut lectin for the scintigraphic detection of cancer. Cancer Lett 25:55–60
Howard DR, Batsakis JG (1980) Cytostructural localization of a tumor-associated antigen. Science 210:210–203
Howard DR, Taylor CR (1980) An anti-tumor antibody in normal human serum. Reaction of anti-T with breast carcinoma cells. Oncology 37:142–148
Howard DR, Ferguson P, Batsakis JG (1981) Carcinoma associated cytostructural antigenic alterations: Detection by lectin binding. Cancer 47:2872–2877
Huggins JW, Trenbeath TP, Sherblom AP, Howard SC, Carraway KL (1980) Glycoprotein differences in solid and ascites froms of the 13762 rat mammary adenocarcinoma. Cancer Res 40:1873–1878
Klein PJ, Newman RA, Muller P, Uhlenbruck G, Citoler P, Schaefer HE, Lennartz KJ, Fischer R (1979) The presence and significance of the Thomsen-Friedenreich antigen in mammary gland. II. Its topochemistry in normal, hyperplastic and carcinoma tissue of the breast. J Cancer Res Clin Oncol 93:205–214
Klein PJ, Osmers R, Vierbuchen M, Ortmann M, Kania J, Uhlenbrunk G (1981) The importance of lectin binding sites and carcinoembryonic antigen with regard to normal, hyperplastic, adenomatous and carcinomatous colonic mucosa. Recent Results Cancer Res 79:1–9
Lis H, Sharon N (1981) Lectins in higher plants. In: Marcus A (ed) The biochemistry of plants: A comprehensive treatise, vol 6. Academic Press, New York, pp 371–447
London J, Berrih S, Bach J-F (1978) Peanut agglutinin. I. A new tool for studying T lymphocyte subpopulations. J Immunol 121:438–443
Lotan R, Skutelsky E, Danon D, Sharon R (1975) The purification, composition and specificity of the anti-T lectin from peanut (Arachis hypogaea). J Biol Chem 250:8518–8523
Louis CJ, Wyllie RG, Chou ST, Sztynda T (1981) Lectin-binding affinities of human epidermal tumors and related conditions: Am J Clin Pathol 75:642–647
Louis CJ, Sztynda T, Cheung ZM, Wyllie RG (1983) Lectin-binding affinities of human breast tumors. Cancer 52:1244–1250
Newman RA, Klein PJ, Uhlenbruck G, Citoler P, Karduck D (1979a) The presence and significance of the Thomsen-Friedenreich antigen in breast cancer. J Cancer Res Clin Oncol 93:181–188
Newman RA, Klein PJ, Rudland PS (1979b) Binding of peanut lectin to breast epithelium, human carcinomas and a cultured rat mammary stem cell: Use of the lectin as a marker of mammary differentiation. JNCI 63:1339–1346
Paulie S, Hansson Y, Lundbald M-L, Perlman P (1983) Lectins as probes for identification of tumor associated antigens on urothelial and colonic carcinoma cell lines. Int J Cancer 31:297–303
Ree HJ, Raine L, Crowley JP (1983) Lectin binding patterns in diffuse large cell lymphoma. Cancer 52:2089–2099
Sfakianakis GN, De Land FH (1982) Radioimmuno-diagnosis and radioimmunotherapy. J Nucl Med 23:840–850
Shysh A, Eu SM, Noujaim AA, Suresh MR, Longenecker BM (1985) In vivo localization of radioiodinated peanut lectin in a murine TA3/Ha mammary carcinoma model. Eur J Nucl Med 10:68–74
Springer GF, Desai PR (1977) Cross-reacting carcinoma associated antigens with blood group and precursor specificities. Transplant Proc 9:1105–1110
Springer GF, Desai PR (1982) Extent of desialation of blood group MM, NN And MN antigen required for reactivity with human anti-T antibody and Arachis hypogaea lectin. J Biol Chem 257:2744–2746
Springer GF, Tegtmeyer H (1980) On the origin of the anti-Thomsen-Friedenreich (T) antibodies. Naturwissenschaften 67:317–318
Springer GF, Desai PR, Banatwala I (1975) Blood group MN antigens and precursors in normal and malignant human breast gladular tissue. JNCI 54:335–339
Springer GF, Desai PR, Scanlon EF (1976) Blood group precursors as human breast carcinoma associated antigen and naturally occurring human cytotoxis against them. Cancer 37:169–176
Springer GF, Murthy MS, Desai PR, Scanlon EF (1980) Breast cancer patients' cell-mediated immune response to Thomsen-Friedenreich (T) antigen. Cancer 45:2949–2954
Springer GF, Murthy MS, Desai PR, Fry WA, Tegtmeyer H, Scanlon EF (1982) Patients' immune response to breast and lung carcinoma associated Thomsen-Friedenreich (T) specificity. Klin Wochenschr 60:121–131
Suresh MR, Wilkinson AA, Holt S, Shysh A, Matte G, Longenecker BM, Noujaim AA (1983) The disposition of peanut lectin in humans. In: Hoffman G (ed) Proceedings of the 3rd International Symposium on Radiopharmacology, Freiburg, p 75 (abstract)
Uhlenbruck G (1981) The Thomsen-Friedenreich (TF) receptor: an old history with new mystery. Immunol Commun 10:251–264
Zabel PL, Noujaim AA, Shysh A, Bray J (1982) Radioiodinated peanut lectin: A potential radiopharmaceutical for detection of tumours expressing the T antigen. In: Raynaud C (ed) Proceedings of the 3rd World Congress of Nuclear Medicine and Biology, vol 4. Pergamon, New York, pp 3670–3673
Zabel PL, Noujaim AA, Shysh A, Bray J (1983) Radioiodinated peanut lectin: A potential radiopharmaceutical for immunodetection of carcinoma expressing the T antigen. Eur J Nucl Med 8:250–254
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Abdi, E.A., Kamitomo, V.J., McPherson, T.A. et al. Radioiodinated peanut lectin: Clinical use as a tumour-imaging agent and potential use in assessing renal-tubular function. Eur J Nucl Med 11, 350–354 (1986). https://doi.org/10.1007/BF00253300
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF00253300