Abstract
The name glycosyl-phosphatidylinositol (GPI) is a trivial name for a family of structures that contains the structural motif: Manα1-4GlcNH2α-6myo-Inositol. This common substructure suggests that this family of molecules is biosynthetically related and differentiates it from other glycosylated phosphoinositides, such as the glycosylated phosphatidylinositols of mycobacteria and inositol phosphoceramides of yeasts and plants. The GPI family (for recent comprehensive reviews, see 1–3) can be conveniently divided into two groups based on structural homology and function. The first group is composed of the membrane protein anchors (Fig. 1), which 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. The second group has been found so far only in the parasitic kinetoplastid protozoans Leishmania major, L. donovani L. mexicana, and the South American tiypanosome Trypanosoma cruzi. These molecules exist as free glycophospholipids, such as the “glycosyl inositol phospholipids” (GIPLs) of the Leishmania (4,5), or attached to phosphorylated repeating units known as the lipophosphoglycans (LPGs) of the Leishmania (6,7).
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© 1993 Humana Press Inc., Totowa, NJ
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Güther, M.L., Ferguson, M.A.J. (1993). The Microanalysis of Glycosyl-Phosphatidylinositol Glycans. In: Hounsell, E.F. (eds) Glycoprotein Analysis in Biomedicine. Methods in Molecular Biology, vol 14. Humana Press. https://doi.org/10.1385/0-89603-226-4:99
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DOI: https://doi.org/10.1385/0-89603-226-4:99
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