Interleukin-1 beta dissociates beta-amyloid precursor protein and beta-amyloid peptide secretion

FEBS Lett. 1994 Nov 14;354(3):289-92. doi: 10.1016/0014-5793(94)01142-7.

Abstract

A heightened production of interleukin 1 beta (IL-1 beta) has been reported in microglial-associated amyloid deposits in Alzheimer's disease (AD) brains. These plaques are composed predominantly of beta/A4 peptide derived from beta-amyloid precursor protein (beta APP). We demonstrate that short-term (1 h) IL-1 beta-treatment increases beta APPs secretion and concomitantly decreases cell-associated beta APP in human H4 neuroglioma cells. Long-term (5 h) IL-1 beta treatment did not alter secreted or cell-associated beta APP content. In contrast, the secretion of beta/A4-containing epitope was not affected by short-term IL-1 beta stimulation; however, long-term IL-1 beta treatment decreased the amount of beta/A4-containing epitope secreted from the cells. These results show that IL-1 beta modifies the processing and secretion of beta APP to exacerbate perhaps the neuropathology of AD.

MeSH terms

  • Amyloid beta-Peptides / metabolism*
  • Amyloid beta-Protein Precursor / metabolism*
  • Blotting, Western
  • Culture Media, Conditioned
  • Enzyme-Linked Immunosorbent Assay
  • Glioma
  • Humans
  • Interleukin-1 / administration & dosage
  • Interleukin-1 / pharmacology*
  • Time Factors
  • Tumor Cells, Cultured

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Culture Media, Conditioned
  • Interleukin-1