The phospholipase A2 superfamily and its group numbering system

Schaloske, Ralph; Dennis, Edward A.

doi:10.1016/j.bbalip.2006.07.011

Cited by 832 publications

(857 citation statements)

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“…Neuronal cells express at least 2 types of phospholipases A 2 : (1) the calcium-independent membrane-associated enzyme (iPLA 2 ) that is thought to be involved in the metabolism of docosahexaenoic acid, the major n-3 long-chain polyunsaturated fatty acid in the brain; and (2) the calciumdependent cytosolic enzyme (cPLA 2 ) that displays a strong selectivity for the AA-containing phospholipids (for review, see Sun et al, 2010). This latter 85-kDa enzyme, which is also referred to as GIVA-PLA 2 (Schaloske and Dennis, 2006), is activated and translocated to membranes after calcium influx and phosphorylation by mitogen-activated protein (MAP) kinases or other kinases (Clark et al, 1995). Activation of MAP kinases and perturbation of calcium homeostasis are well known to be involved in the deleterious effects of A␤ oligomers (Small, 2009;Wang et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Critical role of cPLA2 in Aβ oligomer-induced neurodegeneration and memory deficit

Desbène

Malaplate-Armand

Youssef

et al. 2012

Neurobiology of Aging

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Soluble beta-amyloid (A␤) oligomers are considered to putatively play a critical role in the early synapse loss and cognitive impairment observed in Alzheimer's disease. We previously demonstrated that A␤ oligomers activate cytosolic phospholipase A 2 (cPLA 2 ), which specifically releases arachidonic acid from membrane phospholipids. We here observed that cPLA 2 gene inactivation prevented the alterations of cognitive abilities and the reduction of hippocampal synaptic markers levels noticed upon a single intracerebroventricular injection of A␤ oligomers in wild type mice. We further demonstrated that the A␤ oligomer-induced sphingomyelinase activation was suppressed and that phosphorylation of Akt/protein kinase B (PKB) was preserved in neuronal cells isolated from cPLA 2 Ϫ/Ϫ mice. Interestingly, expression of the A␤ precursor protein (APP) was reduced in hippocampus homogenates and neuronal cells from cPLA 2 Ϫ/Ϫ mice, but the relationship with the resistance of these mice to the A␤ oligomer toxicity requires further investigation. These results therefore show that cPLA 2 plays a key role in the A␤ oligomer-associated neurodegeneration, and as such represents a potential therapeutic target for the treatment of Alzheimer's disease.

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Section: Introductionmentioning

confidence: 99%

Critical role of cPLA2 in Aβ oligomer-induced neurodegeneration and memory deficit

Desbène

Malaplate-Armand

Youssef

et al. 2012

Neurobiology of Aging

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“…L'appartenance des iPLA 2 β et γ à la superfamille des phospholipases A 2 (PLA 2 ) définie par E.A. Dennis a conduit à l'assimilation abusive de l'ensemble des PNPLA dans cette classification [8]. Cependant, alors que les iPLA 2 présentent une activité PLA 2 indiscutable, il n'en est pas de même pour tous les membres de la famille patatine [9].…”

Section: Les Protéines à Domaine Pnpla Chez Les Mammifèresunclassified

Les protéines à domaine patatine

Baulande¹,

Langlois²

2010

Med Sci (Paris)

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Identification des enzymes à domaine patatineLes lipides ont des rôles essentiels et multiples dans les cellules, que ce soit dans le maintien des structures intracellulaires et le transport vésiculaire, la régulation de l'équilibre énergétique et la génération de seconds messagers participant à des mécanismes de signalisation cellulaire. Ces dernières années, la découverte de l'ATGL (adipose triglyceride lipase) et de l'adiponutrine, deux protéines adipocytaires, a permis d'identifier une nouvelle famille d'enzymes intervenant dans le méta-bolisme lipidique et ayant un domaine enzymatique commun appelé patatine ou PNPLA. La mise en évidence de ces nouvelles enzymes dotées d'activités lipase/ transacylase met en lumière de nouveaux mécanismes de la régulation du métabolisme lipidique d'importance fondamentale chez les organismes supérieurs.> Les avancées prodigieuses dans le séquençage des génomes ont permis de mettre en évidence nombre de nouveaux gènes jusqu'alors inconnus, ouvrant ainsi un vaste chantier d'investigations relatives à la caractérisation de leurs fonctions biologiques. L'ère de la génomique fonctionnelle succède donc à celle du séquençage des géno-mes avec comme enjeu majeur de permettre une meilleure compréhension de la physiologie cellulaire. Ces dernières années, plusieurs protéines partageant un même domaine protéique appelé patatine, ou domaine PNPLA (patatin-like phospholipase domain), ont été découvertes.

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“…Novel sPLA 2 were identified in the 90 th by screening nucleic acid data bases. Up to now, eleven sPLA 2 s have been cloned: IB, IIA, IIC, IID, IIE, IIF, III, V, X, and XIIA PLA 2 s together with the XIIB PLA 2 -like protein devoid of catalytic activity [1,15,16]. They express different catalytic and binding properties to natural phospholipids [17,18].…”

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of a secreted group IIA chicken intestinal phospholipase A2

et al. 2011

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BackgroundSecretory phospholipase A2 group IIA (IIA PLA2) is a protein shown to be highly expressed in the intestine of mammals. However, no study was reported in birds.ResultsChicken intestinal group IIA phospholipase A2 (ChPLA2-IIA) was obtained after an acidic treatment (pH.3.0), precipitation by ammonium sulphate, followed by sequential column chromatographies on Sephadex G-50 and mono-S ion exchanger. The enzyme was found to be a monomeric protein with a molecular mass of around 14 kDa. The purified enzyme showed a substrate preference for phosphatidylethanolamine and phosphatidylglycerol, and didn't hydrolyse phosphatidylcholine. Under optimal assay conditions, in the presence of 10 mM NaTDC and 10 mM CaCl2, a specific activity of 160 U.mg-1 for purified ChPLA2-IIA was measured using egg yolk as substrate. The fifteen NH2-terminal amino acid residues of ChPLA2-IIA were sequenced and showed a close homology with known intestinal secreted phospholipases A2. The gene encoding the mature ChPLA2-IIA was cloned and sequenced. To further investigate structure-activity relationship, a 3D model of ChPLA2-IIA was built using the human intestinal phospholipase A2 structure as template.ConclusionChPLA2-IIA was purified to homogeneity using only two chromatographic colomns. Sequence analysis of the cloned cDNA indicates that the enzyme is highly basic with a pI of 9.0 and has a high degree of homology with mammalian intestinal PLA2-IIA.

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The phospholipase A2 superfamily and its group numbering system

Cited by 832 publications

References 189 publications

Critical role of cPLA2 in Aβ oligomer-induced neurodegeneration and memory deficit

Critical role of cPLA2 in Aβ oligomer-induced neurodegeneration and memory deficit

Les protéines à domaine patatine

Purification and biochemical characterization of a secreted group IIA chicken intestinal phospholipase A2

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