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A lipid in the plasma membrane of cells that anchors proteins on the cell's surface. Some of the proteins held on the cell surface protect cells against attack by serum complement. Mutations that decrease or eliminate GPI are responsible for the destruction of blood cells by the complement system, which characterizes the disease called paroxysmal nocturnal hemoglobinuria.
Medical Dictionary, © 2009 Farlex and Partners
References in periodicals archive ?
Ferguson, "The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research," Journal of Cell Science, vol.
Kinoshita, "PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2," Biochemical and Biophysical Research Communications, vol.
Luzzatto, "Two distinct patterns of glycosylphosphatidylinositol (GPI) linked protein deficiency in the red cells of patients with paroxysmal nocturnal haemoglobinuria," The British Journal of Haematology, vol.
It has been shown that plasmodial toxin glycosylphosphatidylinositol (GPI) augments apoptosis rates in cardiomyocyte culture.
Prostate stem cell antigen is a cell surface antigen belonging to the Thy-1/Ly-6 family of glycosylphosphatidylinositol (GPI) anchored proteins [1].
CNTN-1 is a glycosylphosphatidylinositol (GPI)-anchored 135-kDa cell surface protein that belongs to a family of immunoglobulin (lg) domain-containing cell adhesion molecules (CAMs) that also includes N-CAM, L1, and Nr-CAM [29, 30].
Glycosylphosphatidylinositol (GPI)-anchor biosynthesis was associated with all doses of benzene exposure in the present study.
Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin.
Signal transduction in host cells by a glycosylphosphatidylinositol toxin of malaria parasites.
It is a glycosylphosphatidylinositol (GPI)-anchored neuronal membrane protein that functions as a neuronal cell adhesion molecule implicated in axogenesis and myelination (20).
gC1qR does not have any conventional transmembrane domain in its sequence nor a glycosylphosphatidylinositol (GPI) anchor, suggesting that any role of this molecule in intracellular signaling should need an association with transmembrane proteins such as [[beta].sub.1]-integrins [12, 14].

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