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Pla2g6 deficiency resulted in axonal degeneration, dopaminergic and motor neuron cell loss, and increased beta-synuclein expression.
Two members of dynamical network biomarke, PLA2G6 and CYP2C44 were found to induce dysfunction of arachidonic acid metabolism and finally lead to impairments of liver detoxification and malignant transition to cancer.
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 activity for the recycling of alpha 6 integrin-GFP from the endosomal recycling complex to the plasma membrane.
iPLA2-gamma 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+) signalling is a trigger for autophagic dysfunction, progressive loss of dopaminergic (DA) neurons in substantia nigra pars 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.
diapocynin inhibited ROS production, abolished iPLA2 activity and reduced Ca2+ influx through stretch-activated and store-operated channels, two major pathways responsible for excessive Ca2+ entry in dystrophic muscle
Mice deficient in iPLA2Beta show evidence of neuroinflammation and motor dysfunction in later life.
membrane potential sensitive activity is the iPLA2gamma
In this study we demonstrate for the first time that corticostriatal LTP is dependant on iPLA2 signalling, which can be reversed with application of DHA.
Enteropathy may result from acute autoimmune hepatitis in a susceptible host such as iPLA2beta deficiency.
these data indicate that beta-cell apoptosis is, in part, attributable to the modulation of 5'SS selection in the Bcl-x pre-mRNA by bioactive lipids modulated by iPLA2beta.
The loss of PS2 could have a critical role in lung tumor development through the upregulation of iPLA2 activity by reducing gamma-secretase.
This study suggests that iPLA2beta-derived lipid signals modulate immune cell responses, raising the possibility that early inhibition of iPLA2beta may be beneficial in ameliorating autoimmune destruction of beta-cells and mitigating type 1 diabetes.
iPLA2beta confers significant protection of beta-cells against C16:0-induced injury
PLA2G6 mutations are associated with a continuous clinical spectrum from phospholipase A2-associated neurodegeneration to hereditary spastic paraplegia.
report a PLA2G6 compound complicated mutation in an atypical neuroaxonal dystrophy Chinese family, that is the p. A80T and p.D331Y mutation
PLA2G6-associated neurodegeneration was caused by paternal isodisomy of the chromosome 22 (carrying c.680C>T mutation) following in vitro fertilization
PLA2G6 mutation is associated with neurodegeneration presenting as a complicated form of hereditary spastic paraplegia.
A novel variant (NM_003560.2 c.1427 + 2 T > C) acting on a splice donor site and predicted to lead to skipping of exon 10 was found in PLA2G6 in two siblings diagnosed with infantile neuroaxonal dystrophy. This mutation seems to be pathogenic and was found in a homozygous state in the two patients and homozygous reference or heterozygous in five healthy family members.
This study showed that PANK2 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, iPLA2, and sPLA2 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 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 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).
PLA2G6 were identified in patients with a spectrum of neurodegenerative conditions, such as infantile neuroaxonal dystrophy, atypical late-onset neuroaxonal dystrophy and dystonia parkinsonism complex in Indian families
These results strongly suggest that PNPLA9, -6 and -4 play a key role in GPL turnover and homeostasis in human cells. A hypothetical model suggesting how these enzymes could recognize the relative concentration of the different GPLs is proposed
This study identifies a novel PLA2G6 mutation that is the possible genetic cause of FCMTE in this Chinese family.
Finding suggest the broadness of the clinical spectrum of group VI phospholipases A2 (PLA2G6)-related neurodegeneration.
A homozygous novel mutation at position c.2277-1G>C in PLA2G6 gene presumed to give rise to altered splicing, was detected, thus confirming the diagnosis of infantile Neuroaxonal Dystrophy (INAD).
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