Two human TNF receptors have similar extracellular, but distinct intracellular, domain sequences

Cytokine. 1990 Jul;2(4):231-7. doi: 10.1016/1043-4666(90)90022-l.


Tumor necrosis factor (TNF) is a cytokine with a wide range of biological activities in inflammatory and immunologic responses. These activities are mediated by specific cell surface receptors of 55 kDa and 75 kDa apparent molecular masses. A 75-kDa TNF receptor cDNA was isolated using partial amino acid sequence information and the polymerase chain reaction (PCR). When expressed in COS-1 cells, the cDNA transfers specific TNF-binding properties comparable to those of the native receptor. The predicted extracellular region contains four domains with characteristic cysteine residues highly similar to those of the 55-kDa TNF receptor, the nerve growth factor (NGF) receptor, and the CDw40 and OX40 antigens. The consensus sequence of the TNF receptor extracellular domains also has similarity to the cysteine-rich sequence motif LIM. In marked contrast to the extracellular regions, the intracellular domains of the two TNF receptors are entirely unrelated, suggesting different modes of signaling and function.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Cell Line
  • Chlorocebus aethiops
  • DNA / genetics
  • Extracellular Space
  • Gene Expression
  • Humans
  • In Vitro Techniques
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • RNA, Messenger / genetics
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / classification
  • Receptors, Cell Surface / metabolism
  • Receptors, Nerve Growth Factor
  • Receptors, Tumor Necrosis Factor
  • Signal Transduction
  • Tumor Necrosis Factor-alpha / metabolism*


  • Membrane Proteins
  • RNA, Messenger
  • Receptors, Cell Surface
  • Receptors, Nerve Growth Factor
  • Receptors, Tumor Necrosis Factor
  • Tumor Necrosis Factor-alpha
  • DNA