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Cloning of human tumor necrosis factor (TNF) receptor cDNA and expression of recombinant soluble TNF-binding protein

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
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  1. Charing Cross Sunley Research Centre, Hammersmith, London (England)
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 {times} 10{sup {minus}9} M. This binding can be competitively inhibited with unlabeled TNF{alpha} or lymphotoxin (TNF{beta}).
OSTI ID:
5685259
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 87:19; ISSN PNASA; ISSN 0027-8424
Country of Publication:
United States
Language:
English