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PMID: 2170974 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 19 ·1990-10-00 ·Pages 7380-4

Gray PW, Barrett K, Chantry D, Turner M, Feldmann M

Abstract

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).

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cell Line Cloning, Molecular/methods DNA/genetics,isolation & purification Gene Expression Humans Kinetics Molecular Sequence Data Oligonucleotide Probes Peptide Fragments/isolation & purification Receptors, Cell Surface/genetics Receptors, Tumor Necrosis Factor Recombinant Proteins/biosynthesis,metabolism Restriction Mapping Sequence Homology, Nucleic Acid Transfection Tumor Necrosis Factor-alpha/biosynthesis,metabolism
Chemicals
Oligonucleotide Probes Peptide Fragments Receptors, Cell Surface Receptors, Tumor Necrosis Factor Recombinant Proteins Tumor Necrosis Factor-alpha DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Gray P W
Charing Cross Sunley Research Centre, Hammersmith, London, England.
Barrett K
Chantry D
Turner M
Feldmann M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.87.19.7380
Published
1990-10-00
Pages
7380-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC54750
Subset
IM
Databases
GENBANK
M37764
External Links
PubMed source DOI: 10.1073/pnas.87.19.7380 PMC Full Text View journal details
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