Phosphatidylinositol-glycan-specific phospholipase D is anenzyme that in humans is encoded by theGPLD1gene.[5][6]
Many proteins are tethered to the extracellular face of eukaryotic plasma membranes by aglycosylphosphatidylinositol (GPI) anchor. The GPI-anchor is a glycolipid found on many blood cells. The protein encoded by the GPLD1 gene is a GPI degrading enzyme thathydrolyzes the inositol phosphate linkage in proteins anchored byphosphatidylinositol glycans, thereby releasing the attached protein from theplasma membrane.[6]
Plasma concentrations of Gpld1 in mice were found to increase after exercise and to correlate with improvedcognitive function, and concentrations of GPLD1 in blood were increased in active elderly humans.[7][8]
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
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Slomiany A, Nishikawa H, Slomiany BL (March 2002). "Screening and modulation of extracellular signals by mucous barrier. Serum glycosylphosphatidylinositol phospholipase D (GPI-PLD) releases protective mucous barrier from oral mucosa".Journal of Physiology and Pharmacology.53 (1):21–38.PMID11939716.
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Deeg MA, Bowen RF (2002). "Phosphorylation decreases trypsin activation and apolipoprotein al binding to glycosylphosphatidylinositol-specific phospholipase D".Biochemistry and Cell Biology.80 (2):253–60.doi:10.1139/o02-004.PMID11989719.
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Magnusson P, Sharp CA, Farley JR (November 2002). "Different distributions of human bone alkaline phosphatase isoforms in serum and bone tissue extracts".Clinica Chimica Acta; International Journal of Clinical Chemistry.325 (1–2):59–70.doi:10.1016/S0009-8981(02)00248-6.PMID12367767.
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