Strong immunoreactivity of β-amyloid precursor protein, including the β-amyloid protein sequence, at human neuromuscular junctions
1992; Elsevier BV; Volume: 143; Issue: 1-2 Linguagem: Inglês
10.1016/0304-3940(92)90241-x
ISSN1872-7972
AutoresValerie Askanas, W. King Engel, Renate B. Alvarez,
Tópico(s)Cellular transport and secretion
ResumoAt the postsynaptic domain of the human neuromuscular junction (NMJ), we have demonstrated strong concentrations of the N-terminus 45–62, C-terminus 676–695 and β-amyloid protein sequences of β-amyloid precursor protein (βAPP). We used well-characterized monoclonal and polyclonal antibodies for co-localization with three other postsynaptic proteins, applying double and triple fluorescence labeling. Strong immunoreactivity of all three βAPP sequences was found at all NMJs identified by bound α-bungarotoxin (αBT), where they co-localized with αBT and with immunoreactive desmin and dystrophin, which are postsynaptic proteins of human NMJs. This appears to be the first demonstration of βAPP sequences concentrated postsynaptically at human NMJs. βAPP may have a role in normal junctional biology and possibly in some diseases affecting NMJs.
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