Biological activities of human tumor necrosis factor-alpha and its novel mutants

Biochem Mol Biol Int. 1996 May;38(6):1183-9.

Abstract

Biological activities of human tumor necrosis factor-alpha (hTNF-alpha) and its mutants were compared. In cytotoxicity assay with L929 cells, one mutant, designated as TNF-B, showed 4.5-fold higher activity than TNF examined. In receptor binding assay, TNF-B had almost the same affinity for TNF receptors on L929 cells as hTNF-alpha. We also found that TNF-B retained the cytotoxicity of hTNF-alpha for HEp-2 cells. TNF-B also had two-fold higher affinity than hTNF-alpha for receptors on HEp-2 cells (only carrying hTNF-R55) and lower affinity for receptors on U937 cells (expressing mainly hTNF-R75). These results suggested that TNF-B might still interact with the human TNF-R55 receptor, but it might largely lose its ability to bind to human TNF-R75. Changes of biological activity of TNFs might be due to an altered affinity to the different types of TNF receptor on the target cells.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • DNA, Neoplasm / biosynthesis
  • Drug Screening Assays, Antitumor
  • Fibroblasts / drug effects
  • Humans
  • Laryngeal Neoplasms / drug therapy
  • Leukemia, Monocytic, Acute / drug therapy
  • Leukemia, Monocytic, Acute / metabolism
  • Mice
  • Molecular Sequence Data
  • Mutation*
  • Neoplasm Proteins / biosynthesis
  • Radioligand Assay
  • Receptors, Tumor Necrosis Factor / metabolism
  • Sequence Homology, Amino Acid
  • Tumor Cells, Cultured
  • Tumor Necrosis Factor-alpha / genetics
  • Tumor Necrosis Factor-alpha / metabolism
  • Tumor Necrosis Factor-alpha / pharmacology*

Substances

  • DNA, Neoplasm
  • Neoplasm Proteins
  • Receptors, Tumor Necrosis Factor
  • Tumor Necrosis Factor-alpha