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The cDNA for one of the receptors for human tumor necrosis factor (TNF) has been isolated. This cDNA encodes a protein of 455 amino acids that is divided into an extracellular domain of 171 residues and a cytoplasmic domain of 221 residues. The extracellular domain has been engineered for expression in mammalian cells, and this recombinant derivative binds TNF alpha with high affinity and inhibits its cytotoxic activity in vitro. The TNF receptor exhibits similarity with a family of cell surface proteins that includes the nerve growth factor receptor, the human B-cell surface antigen CD40, and the rat T-cell surface antigen OX40. The TNF receptor contains four cysteine-rich subdomains in the extracellular portion. Mammalian cells transfected with the entire TNF receptor cDNA bind radiolabeled TNF alpha with an affinity of 2.5 x 10(-9) M. This binding can be competitively inhibited with unlabeled TNF alpha or lymphotoxin (TNF beta).

Original publication

DOI

10.1073/pnas.87.19.7380

Type

Journal article

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Date

10/1990

Volume

87

Pages

7380 - 7384

Addresses

Charing Cross Sunley Research Centre, Hammersmith, London, England.

Keywords

Cell Line, Animals, Humans, Tumor Necrosis Factor-alpha, Peptide Fragments, Receptors, Cell Surface, Receptors, Tumor Necrosis Factor, Recombinant Proteins, DNA, Oligonucleotide Probes, Restriction Mapping, Cloning, Molecular, Transfection, Gene Expression, Amino Acid Sequence, Base Sequence, Sequence Homology, Nucleic Acid, Kinetics, Molecular Sequence Data