Membrane lipid heterogeneity associated with acetylcholine receptor particle aggregates in Xenopus embryonic muscle cells.
Filipin, digitonin, and saponin react with membrane cholesterol to produce unique membrane alterations (sterol-specific complexes) that are easily discernible in freeze-fracture replicas. We have treated both noninnervated and innervated Xenopus embryonic muscle cells in culture with these agents. Freeze-fracture of these treated muscle cells showed that most areas of the muscle plasma membrane contain sterol-specific complexes (19- to 40-nm protuberances and dimples with filipin, a scalloped appearance with digitonin, or an irregular, rough appearance with saponin). However, these complexes were virtually absent from membrane areas of junctional and nonjunctional aggregates of acetylcholine receptor particles. This result suggests that the membrane matrix of these aggregates is low in cholesterol and that this membrane lipid heterogeneity may be linked to the mechanisms involved in their formation and stabilization on muscle cells in culture.
D000818:Animals; D002449:Cell Aggregation; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure; D002478:Cells, Cultured; D004072:Digitonin / Q000494:pharmacology; D004625:Embryo, Nonmammalian; D005260:Female; D005372:Filipin / Q000494:pharmacology; D005614:Freeze Fracturing; D008563:Membrane Lipids / Q000502:physiology*; D008854:Microscopy, Electron; D009132:Muscles / Q000294:innervation / Q000502:physiology* / Q000648:ultrastructure; D011950:Receptors, Cholinergic / Q000187:drug effects / Q000502:physiology*; D012503:Saponins / Q000494:pharmacology; D014981:Xenopus
D008563:Membrane Lipids; D011950:Receptors, Cholinergic; D012503:Saponins; D005372:Filipin; D004072:Digitonin