Ubiquitous Cell-Surface Glycoprotein on Tumor Cells is Proliferation-Associated Receptor for Transferrin

• Published in: Proceedings of the National Academy of Sciences - PNAS 1981-07, Vol.78 (7), p.4515-4519
• Main Authors: Sutherland, Robert, Delia, Domenico, Schneider, Claudio, Newman, Roland, Kemshead, John, Greaves, Melvyn
• Format: Article
• Language: English
• Subjects: Animals; Antibodies, Monoclonal - immunology; Antigens; Antigens, Neoplasm - immunology; Antigens, Surface - immunology; Cell Division; Cell lines; cell surface; glycoprotein composition; Glycoproteins - immunology; Humans; Leukemia; Lymphocytes; man; Membrane Proteins - immunology; Mice; Monoclonal antibodies; purification; Receptors; Receptors, Cell Surface - immunology; Receptors, Transferrin; T-Lymphocytes - immunology; transferrin; Transferrin - metabolism; Transferrin receptors; Transferrins; Tumor cell line; tumor cells; Tumors
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.78.7.4515

A murine monoclonal antibody (OKT9) raised against human leukemic cells binds to a wide variety of leukemia and tumor cell lines and to a minority of leukemia cells taken directly from patients. Fetal thymus and liver are strongly reactive as are some normal, immature hemopoietic cells and activated lymphocytes. Reactivity with OKT9 appears to correlate with proliferation status in both normal and malignant populations. Biochemical analysis indicates that this structure is a ≈ 180,000-dalton glycoprotein with two disulfide-bonded subunits of ≈ 90,000-daltons. Isolation of the transferrin receptor from a T-cell line (MOLT-4) indicates that it also has a dimeric ≈ 180,000-dalton structure. Radio-labeled transferrin bound to its receptors can be specifically precipitated by the monoclonal OKT9, although the latter does not bind transferrin itself, indicating that the antigenic structure defined by this antibody is likely to be the transferrin receptor.