TY - JOUR
T1 - Membrane lipid heterogeneity associated with acetylcholine receptor particle aggregates in Xenopus embryonic muscle cells
AU - Bridgman, P. C.
AU - Nakajima, Y.
PY - 1981
Y1 - 1981
N2 - Filipin, digitonin, and saponin react with membrane cholesterol to produce unique membrane alterations (sterolspecific 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.
AB - Filipin, digitonin, and saponin react with membrane cholesterol to produce unique membrane alterations (sterolspecific 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.
UR - http://www.scopus.com/inward/record.url?scp=0019460078&partnerID=8YFLogxK
U2 - 10.1073/pnas.78.2.1278
DO - 10.1073/pnas.78.2.1278
M3 - Article
C2 - 6940140
AN - SCOPUS:0019460078
SN - 0027-8424
VL - 78
SP - 1278
EP - 1282
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 2 II
ER -