Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin.

R. Sutherland, D. Delia, C. Schneider, R. Newman, J. Kemshead, M. Greaves

Research output: Contribution to journalArticle

Abstract

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 approximately equal to 180,000-dalton glycoprotein with two disulfide-bonded subunits of approximately equal to 90,000-daltons. Isolation of the transferrin receptor from a T-cell line (MOLT-4) indicates that it also has a dimeric approximately equal to 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.

Original languageEnglish
Pages (from-to)4515-4519
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number7
Publication statusPublished - Jul 1981

ASJC Scopus subject areas

  • General
  • Genetics

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