Glycosylphosphatidylinositol (GPI)-hydrolysing enzymes have been described in many mammalian tissues and body fluids; however, their site(s) of action and in vivo functions have remained unclear. In order to identify a possible intracellular site of GPI hydrolysis, we studied the subcellular distribution of GPI-hydrolysing activity in rat liver. We found that purified fractions from rat liver hydrolysed the GPI moieties of two GPI-anchored proteins with the specificity of a phospholipase D. This GPI-specific phospholipase D (GPI-PLD) activity was found to be highly enriched in a lysosomal fraction and showed a similar intracellular distribution to that of typical lysosomal enzymes. Our results indicate that lysosomes may represent a possible intracellular site of GPI-PLD action.
Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver
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Thomas HARI, Hans KUNZE, Ernst BOHN, Urs BRODBECK, Peter BÜTIKOFER; Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver. Biochem J 15 November 1996; 320 (1): 315–319. doi: https://doi.org/10.1042/bj3200315
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