Prion protein is strongly immunolocalized at the postsynaptic domain of human normal neuromuscular junctions

Neurosci Lett. 1993 Sep 3;159(1-2):111-4. doi: 10.1016/0304-3940(93)90811-x.

Abstract

Using three well-characterized polyclonal and monoclonal antibodies against prion protein (PrP), we demonstrated a strong concentration of PrP at human neuromuscular junctions (NMJs). Applying double and triple fluorescence-labeling, we found that PrP immunoreactivity exactly co-localized with alpha-bungarotoxin (alpha-BT) identified acetylcholine receptors, as well as with the high junctional concentrations of beta-amyloid precursor protein, beta-amyloid protein, desmin, ubiquitin and dystrophin. Therefore, PrP was considered to be located on the postsynaptic muscle membrane. At all NMJs identified by bound alpha-BT, strong PrP immunoreactivity was obtained with all PrP antibodies. This appears to be the first demonstration of PrP concentrated at human NMJs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / immunology
  • Bungarotoxins / pharmacology
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism
  • Histocytochemistry
  • Humans
  • Muscles / metabolism
  • Muscles / pathology
  • Neuromuscular Junction / metabolism*
  • Prions / immunology
  • Prions / metabolism*
  • Receptors, Cholinergic / drug effects
  • Synapses / metabolism*

Substances

  • Antibodies, Monoclonal
  • Bungarotoxins
  • Prions
  • Receptors, Cholinergic