Immunocytochemical localization of ubiquitin at human neuromuscular junctions.
Using several specific monoclonal and polyclonal antibodies, we found that ubiquitin is highly concentrated in the post-synaptic domain of human neuromuscular junctions. The distribution and pattern of ubiquitin immunoreactivity is identical to the localization of bound alpha-bungarotoxin, suggesting that ubiquitin may be involved in post-translational modification or turnover of the acetylcholine receptor or other junctional proteins of the muscle fibre.
Serdaroglu
P
P
USC Neuromuscular Center, University of Southern California School of Medicine, Los Angeles 90017.
Askanas
V
V
Engel
W K
WK
D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D002038:Bungarotoxins; D003893:Desmin; D016650:Fluorescein-5-isothiocyanate; D006801:Humans; D007150:Immunohistochemistry; D009132:Muscles / Q000648:ultrastructure; D009469:Neuromuscular Junction / Q000378:metabolism* / Q000648:ultrastructure; D011950:Receptors, Cholinergic / Q000276:immunology / Q000378:metabolism; D014452:Ubiquitins / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D002038:Bungarotoxins; D003893:Desmin; D011950:Receptors, Cholinergic; D014452:Ubiquitins; D016650:Fluorescein-5-isothiocyanate