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Disturbances in mitochondrial potential and changes in calcium signaling are dependent on iPLA2 activity in an animal model of infantile neuroaxonal dystrophy.
The antinociceptive effect of maprotiline was abrogated by iPLA2 antisense oligonucleotide injection to the prefrontal cortex, indicating a role of this enzyme in antinociception. In contrast, injection of iPLA2 antisense oligonucleotide to the somatosensory cortex did not reduce the antinociceptive effect of maprotiline.
The absence of iPLA2beta promotes macrophage M2 polarization.
Time lapse microscopy and integrin endocytosis assay revealed the essential role of calcium-independent phospholipase A2 (show LYPLA1 Proteins) activity for the recycling of alpha 6 integrin-GFP from the endosomal recycling complex to the plasma membrane.
iPLA2-gamma (show PNPLA8 Proteins) has a protective functional role in the normal glomerulus and in glomerulonephritis.
Results suggest that the degeneration of dopaminergic neurons occurs mainly in the distal region of axons in iPLA2beta-KO mice.
This study showed that the absence of iPLA2beta activity does not influence myocardial inflammation, but iPLA2beta is essential for T. cruzi clearance.
Results support the deleterious role of iPLA2beta in severe obesity associated NAFLD.
Genetic or molecular impairment of PLA2g6-dependent Ca(2 (show CA2 Proteins)+) signalling is a trigger for autophagic dysfunction, progressive loss of dopaminergic (DA) neurons in substantia nigra pars (show EPRS Proteins) compacta and age-dependent L-DOPA-sensitive motor dysfunction.
An inactivation of iPLA2beta exacerbated pathogenesis of experimental colitis by promoting intestinal epithelial cell apoptosis, inhibiting crypt cell regeneration, and causing damage to mucus barrier allowing an activation of innate immune response.
This study showed that PANK2 (show PANK2 Proteins) genes account for disease of patients diagnosed with an Neurodegeneration with brain iron accumulation disorder.
A lipidomics-based LC/MS assay was used to define the specificity of cPLA2 (show PLA2G4A Proteins), iPLA2, and sPLA2 (show PLA2G2A Proteins) toward a variety of phospholipids. A unique hydrophobic binding site for the cleaved fatty acid dominates each enzyme's specificity rather than its catalytic residues and polar headgroup binding site.
This exome sequencing in a family and identified compound-heterozygous PLA2G6 mutations in 2 affected sisters.
PLA2G6 gene mutations in 3 families, are reported.
The catalytic domains of iPLA2beta form a tight dimer and surrounded by ankyrin repeat domains that adopt an outwardly flared orientation, poised to interact with membrane proteins.
performed a longitudinal brain volumetry study in a couple of bicorial twins with PLA2G6-positive infantile neuronal axonal dystrophy
We found no significant influence of the PLA2G6 and PLA2G4C (show PLA2G4C Proteins) polymorphisms on mean age at first hospital admission (P > 0.05) and that the investigated polymorphisms significantly influenced the clinical psychopathology only in male patients. The PLA2G4C (show PLA2G4C Proteins) polymorphism accounted for approximately 12% of negative symptom severity.
Study performed direct sequencing and investigated copy number variations (CNVs) of this gene in 109 Japanese patients with parkinsonism. Results suggest that CNV in PLA2G6 is rare in parkinsonism, at least in the Japanese population, in contrast to the reports of its frequency in neurodegeneration associated with brain iron accumulation.
the association of PLA2G6 with the pathogenesis of idiopathic PD, in addition to PARK14.
A novel missense mutation in PLA2G6 gene (c.3G > T:p.M1I) in one and half-year-old boy with muscle weakness and neurodevelopmental regression (speech, motor and cognition).
The protein encoded by this gene is an A2 phospholipase, a class of enzyme that catalyzes the release of fatty acids from phospholipids. The encoded protein may play a role in phospholipid remodelling, arachidonic acid release, leukotriene and prostaglandin synthesis, fas-mediated apoptosis, and transmembrane ion flux in glucose-stimulated B-cells. Several transcript variants encoding multiple isoforms have been described, but the full-length nature of only three of them have been determined to date.
85 kDa calcium-independent phospholipase A2
, patatin-like phospholipase domain containing 9
, phospholipase A2, group 6 (cytosolic, calcium-independent)
, phospholipase A2, group VI (cytosolic, calcium-independent)
, 85 kDa calcium-independent phospholipase A2-like
, 85/88 kDa calcium-independent phospholipase A2
, GVI PLA2
, group VI phospholipase A2
, intracellular membrane-associated calcium-independent phospholipase A2 beta
, patatin-like phospholipase domain-containing protein 9
, calcium-independent phospholipase A2
, cytosolic, calcium-independent phospholipase A2
, neurodegeneration with brain iron accumulation 2