Premium
Interleukin‐1β dissociates β‐amyloid precursor protein and β‐amyloid peptide secretion
Author(s) -
Vasilakos J.P.,
Carroll R.T.,
Emmerling M.R.,
Doyle P.D.,
Davis R.E.,
Kim K.S.,
Shivers B.D.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01142-7
Subject(s) - secretion , amyloid precursor protein , p3 peptide , amyloid (mycology) , epitope , peptide , chemistry , alzheimer's disease , microbiology and biotechnology , biology , medicine , biochemistry , immunology , antibody , disease , inorganic chemistry
A heightened production of interleukin 1β(IL‐1β) has been reported in microglial‐associated amyloid deposits in Alzheimer's disease (AD) brains. These plaques are composed predominantly of β/A4 peptide derived from β‐amyloid precursor protein (βAPP). We demonstrate that short‐term (1 h) IL‐1β‐treatment increases βAPP s secretion and concomitantly decreases cell‐associated βAPP in human H4 neuroglioma cells. Long‐term (5 h) IL‐1β treatment did not alter secreted or cell‐associated βAPP content. In contrast, the secretion of β/A4‐containing epitope was not affected by short‐term IL‐1β stimulation; however, long‐term IL‐1β treatment decreased the amount of β/A4‐containing epitope secreted from the cells. These results show that IL‐1β modifies the processing and secretion of βAPP to exacerbate perhaps the neuropathology of AD.