Cloning and expression of cDNAs for two distinct murine tumor necrosis factor receptors demonstrate one receptor is species specific.

We describe the cloning and expression of the murine homologs of the 55-kDa and 75-kDa human Tumor necrosis factor

M. Lewis

2006

Scholarcy highlights

  • Complementary DNA clones encoding two distinct tumor necrosis factor receptors were isolated from a mouse macrophage cDNA library
  • A murine macrophage cDNA library was screened at low stringency with a DNA fragment corresponding to the coding region of the human 55-kDa Tumor necrosis factor receptor
  • The structure of the protein suggested by hydrophobicity data predicts a typical receptor molecule, consisting of an extracellular domain of 183 amino acids) and a cytoplasmic domain of 219 amino acids, bisected by a transmembrane region of 23 amino acids
  • As previously observed for hTNF-R1, the presumed extracellular domain of murine tumor necrosis factor receptor type 1 contains 24 cysteine residues, which can be divided into four related subdomains
  • The extracellular domain contains three potential sites for N-linked glycosylation, two of which are conserved in hTNF-R1
  • The predicted N-terminal residue for murine tumor necrosis factor receptor type 2 is the valine at position + 1 that corresponds to the predicted
  • The low affinity of human tumor necrosis factor a for murine tumor necrosis factor receptor type 2 may have important clinical implications because potential therapeutic benefits or toxic activities signaled by the type-2 receptor might be missed in mouse experiments done with hTNF-a

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