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Choleragen-Mediated Release of Trapped Glucose from Liposomes Containing Ganglioside G M1

125 I-Labeled choleragen was bound to liposomes containing galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylce ramide (G M1 ), but not in large amounts to ganglioside-free liposomes nor to those containing N-acetylneuraminylgalactosylglucosylceramide (G M3 ), N - acetylgalact... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America 1 October 1976, Vol.73(10), pp.3480-3483
Main Author: Moss, Joel
Other Authors: Fishman, Peter H. , Richards, Roberta L. , Alving, Carl R. , Vaughan, Martha , Brady, Roscoe O.
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 00278424
Link: https://www.jstor.org/stable/66623
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recordid: jstor_archive_2366623
title: Choleragen-Mediated Release of Trapped Glucose from Liposomes Containing Ganglioside G M1
format: Article
creator:
  • Moss, Joel
  • Fishman, Peter H.
  • Richards, Roberta L.
  • Alving, Carl R.
  • Vaughan, Martha
  • Brady, Roscoe O.
subjects:
  • Applied sciences -- Materials science -- Materials -- Polyclonal antibodies
  • Health sciences -- Medical sciences -- Immunology -- Polyclonal antibodies
  • Biological sciences -- Biochemistry -- Biomolecules -- Polyclonal antibodies
  • Biological sciences -- Biology -- Cytology -- Polyclonal antibodies
  • Health sciences -- Medical sciences -- Immunology -- Polyclonal antibodies
  • Biological sciences -- Biochemistry -- Biomolecules -- Polyclonal antibodies
  • Biological sciences -- Biochemistry -- Chemical mixtures -- Polyclonal antibodies
  • Physical sciences -- Chemistry -- Thermodynamics -- Polyclonal antibodies
  • Physical sciences -- Physics -- Immunology -- Polyclonal antibodies
  • Health sciences -- Medical sciences -- Immunology -- Polyclonal antibodies
ispartof: Proceedings of the National Academy of Sciences of the United States of America, 1 October 1976, Vol.73(10), pp.3480-3483
description: 125 I-Labeled choleragen was bound to liposomes containing galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylce ramide (G M1 ), but not in large amounts to ganglioside-free liposomes nor to those containing N-acetylneuraminylgalactosylglucosylceramide (G M3 ), N - acetylgalactosaminyl - (N - acetylneuraminyl) - galactosylglucosylceramide (G M2 ), or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N- acetylneuraminyl)-galactosylglucosylceramide (G D 1a ). Choleragen released trapped glucose only from G M1 -liposomes. This choleragen-induced glucose release from G M1 -liposomes was relatively rapid for the first few minutes, then continued more slowly. The amount of glucose released from liposomes in 30 min was dependent on both the G M1 content and choleragen concentration. Prior incubation of G M1 -liposomes with anti-G M1 antiserum prevented the choleragen-dependent release of trapped glucose. After incubation of G M1 -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 G M1 or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-ga lactosylglucosylceramide 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. It appears that choleragen in the absence of other proteins binds specifically to liposomes containing G M1 and can induce permeability changes.
language: eng
source:
identifier: ISSN: 00278424
fulltext: fulltext
issn:
  • 0027-8424
  • 00278424
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titleCholeragen-Mediated Release of Trapped Glucose from Liposomes Containing Ganglioside G M1
creatorMoss, Joel ; Fishman, Peter H. ; Richards, Roberta L. ; Alving, Carl R. ; Vaughan, Martha ; Brady, Roscoe O.
ispartofProceedings of the National Academy of Sciences of the United States of America, 1 October 1976, Vol.73(10), pp.3480-3483
identifierISSN: 00278424
subjectApplied sciences -- Materials science -- Materials -- Polyclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Polyclonal antibodies ; Biological sciences -- Biochemistry -- Biomolecules -- Polyclonal antibodies ; Biological sciences -- Biology -- Cytology -- Polyclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Polyclonal antibodies ; Biological sciences -- Biochemistry -- Biomolecules -- Polyclonal antibodies ; Biological sciences -- Biochemistry -- Chemical mixtures -- Polyclonal antibodies ; Physical sciences -- Chemistry -- Thermodynamics -- Polyclonal antibodies ; Physical sciences -- Physics -- Immunology -- Polyclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Polyclonal antibodies
description125 I-Labeled choleragen was bound to liposomes containing galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylce ramide (G M1 ), but not in large amounts to ganglioside-free liposomes nor to those containing N-acetylneuraminylgalactosylglucosylceramide (G M3 ), N - acetylgalactosaminyl - (N - acetylneuraminyl) - galactosylglucosylceramide (G M2 ), or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N- acetylneuraminyl)-galactosylglucosylceramide (G D 1a ). Choleragen released trapped glucose only from G M1 -liposomes. This choleragen-induced glucose release from G M1 -liposomes was relatively rapid for the first few minutes, then continued more slowly. The amount of glucose released from liposomes in 30 min was dependent on both the G M1 content and choleragen concentration. Prior incubation of G M1 -liposomes with anti-G M1 antiserum prevented the choleragen-dependent release of trapped glucose. After incubation of G M1 -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 G M1 or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-ga lactosylglucosylceramide 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. It appears that choleragen in the absence of other proteins binds specifically to liposomes containing G M1 and can induce permeability changes.
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titleCholeragen-Mediated Release of Trapped Glucose from Liposomes Containing Ganglioside G M1
description125 I-Labeled choleragen was bound to liposomes containing galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylce ramide (G M1 ), but not in large amounts to ganglioside-free liposomes nor to those containing N-acetylneuraminylgalactosylglucosylceramide (G M3 ), N - acetylgalactosaminyl - (N - acetylneuraminyl) - galactosylglucosylceramide (G M2 ), or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N- acetylneuraminyl)-galactosylglucosylceramide (G D 1a ). Choleragen released trapped glucose only from G M1 -liposomes. This choleragen-induced glucose release from G M1 -liposomes was relatively rapid for the first few minutes, then continued more slowly. The amount of glucose released from liposomes in 30 min was dependent on both the G M1 content and choleragen concentration. Prior incubation of G M1 -liposomes with anti-G M1 antiserum prevented the choleragen-dependent release of trapped glucose. After incubation of G M1 -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 G M1 or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-ga lactosylglucosylceramide 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. It appears that choleragen in the absence of other proteins binds specifically to liposomes containing G M1 and can induce permeability changes.
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titleCholeragen-Mediated Release of Trapped Glucose from Liposomes Containing Ganglioside G M1
authorMoss, Joel ; Fishman, Peter H. ; Richards, Roberta L. ; Alving, Carl R. ; Vaughan, Martha ; Brady, Roscoe O.
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abstract125 I-Labeled choleragen was bound to liposomes containing galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-galactosylglucosylce ramide (G M1 ), but not in large amounts to ganglioside-free liposomes nor to those containing N-acetylneuraminylgalactosylglucosylceramide (G M3 ), N - acetylgalactosaminyl - (N - acetylneuraminyl) - galactosylglucosylceramide (G M2 ), or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N- acetylneuraminyl)-galactosylglucosylceramide (G D 1a ). Choleragen released trapped glucose only from G M1 -liposomes. This choleragen-induced glucose release from G M1 -liposomes was relatively rapid for the first few minutes, then continued more slowly. The amount of glucose released from liposomes in 30 min was dependent on both the G M1 content and choleragen concentration. Prior incubation of G M1 -liposomes with anti-G M1 antiserum prevented the choleragen-dependent release of trapped glucose. After incubation of G M1 -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 G M1 or N-acetylneuraminylgalactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)-ga lactosylglucosylceramide 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. It appears that choleragen in the absence of other proteins binds specifically to liposomes containing G M1 and can induce permeability changes.
pubNational Academy of Sciences of the United States of America
doi10.1073/pnas.73.10.3480
eissn10916490
date1976-10-01