Analysis of the carbohydrate and lipid components of glycosylphosphatidylinositol structures

Achim Treumann, M. Lucia Güther, Pascal Schneider, Michael A. J. Ferguson

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

    12 Citations (Scopus)

    Abstract

    Glycosylphosphatidylinositols (GPIs) are a family of structures that contain the structural motif: Mana1-4GlcNH2a1-6myo-Inositol-1-PO4-lipid. This common substructure suggests that this family of molecules are biosynthetically related and differentiates them from other glycosylated phosphoinositides, such as the glycosylated phosphatidylinositols of mycobacteria and the glycosylated inositol phosphoceramides of yeasts and plants. The GPI family can be conveniently divided into two groups based on structural homology and function. The first group (1–28) are the membrane protein anchors (Fig. 1) that are found covalently linked to the C-termini of a wide variety of externally disposed plasma membrane proteins throughout the eukaryotes These GPI anchors afford a stable attachment of proteins to the membrane and can be viewed as an alternative mechanism of membrane attachment to a single-pass hydrophobic transmembrane peptide domain. For recent reviews of GPI anchor structure, biosynthesis, and function see refs. 29–31. The second group of GPI structures have only been found in protozoan organisms. These molecules exist as free glycophospholipids, such as the glycoinositol phospholipids (GIPLs) of the Leishmania, Trypanosoma cruzi, Leptomonas, Herpetomonas, and Phytomonas (29,32–34), or attached to phosphorylated repeating units as in the lipophosphoglycans (LPGs) of the Leishmania (29,35). In this chapter protocols specifically designed to analyse the protein-linked GPI anchors, although they are also applicable to the GIPLs and, to some extent, the LPGs will be described.
    Original languageEnglish
    Title of host publicationGlycoanalysis protocols
    EditorsElizabeth F. Hounsell
    Place of PublicationTotowa
    PublisherHumana Press
    Pages213-235
    Number of pages23
    ISBN (Electronic)9781592595624
    ISBN (Print)9780896033559
    DOIs
    Publication statusPublished - 1998

    Publication series

    NameMethods in Molecular Biology
    PublisherHumana Press
    Volume76
    ISSN (Print)1064-3745

    Fingerprint

    Glycosylphosphatidylinositols
    Carbohydrates
    Lipids
    Inositol
    Phospholipids
    Membrane Proteins
    Membranes
    Molecules
    Biosynthesis
    Cell membranes
    Phosphatidylinositols
    Anchors
    Yeast
    Proteins
    Peptides

    Cite this

    Treumann, A., Güther, M. L., Schneider, P., & Ferguson, M. A. J. (1998). Analysis of the carbohydrate and lipid components of glycosylphosphatidylinositol structures. In E. F. Hounsell (Ed.), Glycoanalysis protocols (pp. 213-235). (Methods in Molecular Biology; Vol. 76). Totowa: Humana Press. https://doi.org/10.1385/0-89603-355-4:213
    Treumann, Achim ; Güther, M. Lucia ; Schneider, Pascal ; Ferguson, Michael A. J. / Analysis of the carbohydrate and lipid components of glycosylphosphatidylinositol structures. Glycoanalysis protocols . editor / Elizabeth F. Hounsell. Totowa : Humana Press, 1998. pp. 213-235 (Methods in Molecular Biology).
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    abstract = "Glycosylphosphatidylinositols (GPIs) are a family of structures that contain the structural motif: Mana1-4GlcNH2a1-6myo-Inositol-1-PO4-lipid. This common substructure suggests that this family of molecules are biosynthetically related and differentiates them from other glycosylated phosphoinositides, such as the glycosylated phosphatidylinositols of mycobacteria and the glycosylated inositol phosphoceramides of yeasts and plants. The GPI family can be conveniently divided into two groups based on structural homology and function. The first group (1–28) are the membrane protein anchors (Fig. 1) that are found covalently linked to the C-termini of a wide variety of externally disposed plasma membrane proteins throughout the eukaryotes These GPI anchors afford a stable attachment of proteins to the membrane and can be viewed as an alternative mechanism of membrane attachment to a single-pass hydrophobic transmembrane peptide domain. For recent reviews of GPI anchor structure, biosynthesis, and function see refs. 29–31. The second group of GPI structures have only been found in protozoan organisms. These molecules exist as free glycophospholipids, such as the glycoinositol phospholipids (GIPLs) of the Leishmania, Trypanosoma cruzi, Leptomonas, Herpetomonas, and Phytomonas (29,32–34), or attached to phosphorylated repeating units as in the lipophosphoglycans (LPGs) of the Leishmania (29,35). In this chapter protocols specifically designed to analyse the protein-linked GPI anchors, although they are also applicable to the GIPLs and, to some extent, the LPGs will be described.",
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    Treumann, A, Güther, ML, Schneider, P & Ferguson, MAJ 1998, Analysis of the carbohydrate and lipid components of glycosylphosphatidylinositol structures. in EF Hounsell (ed.), Glycoanalysis protocols . Methods in Molecular Biology, vol. 76, Humana Press, Totowa, pp. 213-235. https://doi.org/10.1385/0-89603-355-4:213

    Analysis of the carbohydrate and lipid components of glycosylphosphatidylinositol structures. / Treumann, Achim; Güther, M. Lucia; Schneider, Pascal; Ferguson, Michael A. J.

    Glycoanalysis protocols . ed. / Elizabeth F. Hounsell. Totowa : Humana Press, 1998. p. 213-235 (Methods in Molecular Biology; Vol. 76).

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

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    N2 - Glycosylphosphatidylinositols (GPIs) are a family of structures that contain the structural motif: Mana1-4GlcNH2a1-6myo-Inositol-1-PO4-lipid. This common substructure suggests that this family of molecules are biosynthetically related and differentiates them from other glycosylated phosphoinositides, such as the glycosylated phosphatidylinositols of mycobacteria and the glycosylated inositol phosphoceramides of yeasts and plants. The GPI family can be conveniently divided into two groups based on structural homology and function. The first group (1–28) are the membrane protein anchors (Fig. 1) that are found covalently linked to the C-termini of a wide variety of externally disposed plasma membrane proteins throughout the eukaryotes These GPI anchors afford a stable attachment of proteins to the membrane and can be viewed as an alternative mechanism of membrane attachment to a single-pass hydrophobic transmembrane peptide domain. For recent reviews of GPI anchor structure, biosynthesis, and function see refs. 29–31. The second group of GPI structures have only been found in protozoan organisms. These molecules exist as free glycophospholipids, such as the glycoinositol phospholipids (GIPLs) of the Leishmania, Trypanosoma cruzi, Leptomonas, Herpetomonas, and Phytomonas (29,32–34), or attached to phosphorylated repeating units as in the lipophosphoglycans (LPGs) of the Leishmania (29,35). In this chapter protocols specifically designed to analyse the protein-linked GPI anchors, although they are also applicable to the GIPLs and, to some extent, the LPGs will be described.

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    Treumann A, Güther ML, Schneider P, Ferguson MAJ. Analysis of the carbohydrate and lipid components of glycosylphosphatidylinositol structures. In Hounsell EF, editor, Glycoanalysis protocols . Totowa: Humana Press. 1998. p. 213-235. (Methods in Molecular Biology). https://doi.org/10.1385/0-89603-355-4:213