MAIL, a novel nuclear I kappa B protein that potentiates LPS-induced IL-6 production

FEBS Lett. 2000 Nov 17;485(1):53-6. doi: 10.1016/s0014-5793(00)02185-2.


We have identified and characterized a novel member of the ankyrin-repeat family named 'molecule possessing ankyrin-repeats induced by lipopolysaccharide' (MAIL). The C-terminal portion of MAIL shared high sequence homology with the I kappa B family. Intraperitoneal injection of lipopolysaccharide (LPS) into mice rapidly (<0.5 h) induced MAIL mRNA in various tissues, particularly in the spleen, lymph node, and lung. Ectopically expressed MAIL was localized in the nucleus, and remarkably potentiated the LPS-induced mRNA expression and secretion of interleukin (IL)-6 in Swiss 3T3 cells. These findings indicate that MAIL is one of the nuclear I kappa B proteins and an activator of IL-6 production.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Cell Nucleus / chemistry
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Drug Synergism
  • Gene Expression
  • Green Fluorescent Proteins
  • Interleukin-6 / biosynthesis*
  • Lipopolysaccharides / pharmacology*
  • Luminescent Proteins / genetics
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / pharmacology*
  • Organ Specificity
  • RNA, Messenger / analysis
  • Recombinant Fusion Proteins
  • Sequence Homology
  • Transfection


  • Adaptor Proteins, Signal Transducing
  • DNA, Complementary
  • Interleukin-6
  • Lipopolysaccharides
  • Luminescent Proteins
  • Nfkbiz protein, mouse
  • Nuclear Proteins
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins