Presenilin-1 and the amyloid precursor protein are transported bidirectionally in the sciatic nerve of adult rat

Neurochem Int. 2002 Dec;41(6):429-35. doi: 10.1016/s0197-0186(02)00014-1.


The amyloid precursor protein (APP) and presenilin-1 (PS-1) are not only of importance for the normal functioning of the various neurons, but also play central roles in the pathogenesis of Alzheimer's disease (AD). Through the use of immunohistochemical and Western blot techniques, the bidirectional axonal transport of these proteins has been demonstrated in the sciatic nerve of adult rat. Double-ligation of the sciatic nerve for 6, 12 or 24h was observed to cause a progressive accumulation of the 45kDa presenilin-1 holoprotein and APPs with molecular masses of 116 and 94kDa on both sites of the ligature. It is concluded that the functions of presenilin-1 and APPs are not restricted to the neuronal perikarya: they may carry information in both directions, from the cell body to the axon terminals and vice versa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Protein Precursor / metabolism*
  • Animals
  • Biological Transport
  • Blotting, Western
  • Immunohistochemistry
  • Ligation
  • Male
  • Membrane Proteins / metabolism*
  • Presenilin-1
  • Rats
  • Rats, Sprague-Dawley
  • Reference Values
  • Sciatic Nerve / metabolism*
  • Tissue Distribution


  • Amyloid beta-Protein Precursor
  • Membrane Proteins
  • Presenilin-1