Choleragen-mediated release of trapped glucose from liposomes containing ganglioside GM1.
Open Access
- 1 October 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (10), 3480-3483
- https://doi.org/10.1073/pnas.73.10.3480
Abstract
125I-Labeled choleragen was bound to liposomes containing galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylceramide (GM1), but not in large amounts to ganglioside-free liposomes or to those containing N-acetylneuraminylgalactosylglucosylceramide (GM3), N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylceramide (GM2), or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylceramide (GD1a). Choleragen released trapped glucose only from GM1-liposomes. This choleragen-induced glucose release from GM1-liposomes was relatively rapid for the 1st few minutes, then continued more slowly. The amount of glucose released from liposomes in 30 min was dependent on the GM1 content and choleragen concentration. Prior incubation of GM1-liposomes with anti-GM1 [rabbit] antiserum prevented the choleragen-dependent release of trapped glucose. After incubation of GM1-liposomes with choleragen, addition of anticholeragen antibodies and complement led to more extensive glucose release. Under these latter conditions a much smaller glucose release was observed also from liposomes containing GM1 or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylceramide in the absence of choleragen. These releases were attributed to naturally-occurring antiganglioside antibodies in the antiserum and complement. Ganglioside-free liposomes did not release glucose in response to anticholeragen and complement. Choleragen in the absence of other proteins apparently binds specifically to liposomes containing GM1 and can induce permeability changes.This publication has 12 references indexed in Scilit:
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