Post-GPI attachment to proteins phospholipase 3 (PGAP3)

Post-GPI attachment to proteins phospholipase 3 (PGAP3) is an enzyme localized to the Golgi apparatus that participates in the maturation of glycosylphosphatidylinositol (GPI) anchors by removing unsaturated fatty acids from the sn-2 position, facilitating the association of GPI-anchored proteins with lipid rafts and correct protein sorting and trafficking[1][2]. Mutations in PGAP3 impair this process, causing a congenital disorder of glycosylation (PGAP3-CDG) with predominant neurological features (developmental delay, intellectual disability, seizures), distinct craniofacial anomalies, and biochemical evidence of elevated alkaline phosphatase[2]. The gene is ubiquitously expressed but has notable effects on brain and multisystem development when mutated, and affected individuals often require multidisciplinary management. While not currently a direct therapeutic target, its function is essential for neural development and GPI-anchor biology, and patients are managed symptomatically, with some pharmacological responsiveness to anti-epileptic drugs and possibly pyridoxine[2][1].

Other names

GPI-specific phospholipase A2-like PGAP3PERLD1CAB2COS16 homologgene coamplified with ERBB2 proteinPER1-like domain-containing protein 1post-GPI attachment to proteins factor 3hCOS16MGC9753PP1498AGLA546

For anti-epileptic drugs: Inhibition of neuronal excitability and seizure control via modulation of ion channels, neurotransmitter release, or enhancement of inhibitory neurotransmission For pyridoxine (B6): Supplementation may enhance GABA synthesis and help control seizures in case of impaired pyridoxal phosphate metabolism related to GPI-anchor defects[2]