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      Glycosyl-Phosphatidylinositol (GPI)-Anchored Renal Dipeptidase Is Released by a Phospholipase C in vivo

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          The release mechanism of the glycosyl-phosphatidylinositol (GPI)-anchored renal dipeptidase (EC in vivo has been investigated. Triton X-114 phase separation indicated that the dipeptidase is exclusively present as a hydrophilic form in urine from porcine, rat, rabbit and human. Western blot analysis of human and porcine purified dipeptidase and the urine concentrates with anti-(cross-reacting determinant) serum demonstrated the presence of inositol 1,2-cyclic monophosphate indicating that the renal dipeptidase had been released from the membrane by the action of a phospholipase C. This is the first direct evidence for cleavage of a human GPI-anchored protein by a responsible phospholipase C in vivo.

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          Most cited references 5

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          Signal transduction via glycosyl phosphatidylinositol-anchored proteins in T cells is inhibited by lowering cellular cholesterol.

          Glycosylphosphatidylinositol (GPI)-anchored proteins can deliver costimulatory signals to lymphocytes, but the exact pathway of signal transduction involved is not yet characterized. GPI-anchored proteins are fixed to the cell surface solely by a phospholipid moiety and are clustered in distinct membrane domains that are formed by an unique lipid composition requiring cholesterol. To elucidate the role of membrane lipids for signal transduction via GPI-anchored proteins, we studied the influence of reduced cellular cholesterol content on calcium signaling via GPI-anchored CD59 and CD48 in Jurkat T cells. Lowering cholesterol by different inhibitors of cellular cholesterol synthesis suppressed calcium response via GPI-anchored proteins by about 50%, whereas stimulation via CD3 was only minimally affected (<10%). The decrease in overall calcium response via GPI-anchored proteins was reflected by inhibition of calcium release from intracellular stores. Cell surface expression of GPI-anchored proteins was not changed quantitatively by lowering cellular cholesterol, and neither was the pattern of immunofluorescence in microscopic examination. In addition, the distribution of GPI-anchored proteins in detergent-insoluble complexes remained unaltered. These results suggest that cellular cholesterol is an important prerequisite for signal transduction via GPI-anchored proteins beyond formation of membrane domains.
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            Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (Review)

             Nigel Hooper (2009)
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              T cell signalling through CD73.

              CD73 (ecto-5'-nucleotidase), a glycosyl phosphatidylinositol (GPI) anchored purine salvage enzyme expressed on the surface of human T and B lymphocytes, catalyzes the conversion of purine and pyrimidine ribo- and deoxyribonucleoside monophosphates to the corresponding nucleosides. The cellular distribution, cDNA sequence, and structure of CD73 are reviewed. CD73 serves as a costimulatory molecule in activating T cells. A Jurkat.T cell line transfected with the CD73 cDNA revealed that neither enzymatic activity nor the GPI anchor is necessary for T cell activation in vitro via CD73, while expression of p56kk, CD45 and the T cell receptor are required. Models for the transmission of signals via CD73 and other GPI-anchored proteins are discussed. CD73 generated adenosine functions in cell signalling in many physiologic systems, including intestinal epithelium, ischemic myocardium, and cholinergic synapses. The hypothesis that CD73 produces adenosine that is important for T cell development is presented.

                Author and article information

                Kidney Blood Press Res
                Kidney and Blood Pressure Research
                S. Karger AG
                06 February 2002
                : 25
                : 1
                : 7-12
                aCollege of Pharmacy, bHormone Research Center, Chonnam National University, Kwangju, cCollege of Medicine, Chonbuk National University, Chonju, Korea, and dProteolysis Research Group, School of Biochemistry and Molecular Biology, University of Leeds, UK
                49429 Kidney Blood Press Res 2002;25:7–12
                © 2002 S. Karger AG, Basel

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                Figures: 2, References: 36, Pages: 6
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