Written | 2010-05 | Robert T Cormier |
Department of Biochemistry, Molecular Biology, University of Minnesota Medical School, Duluth, Minnesota, USA |
Identity |
Alias (NCBI) | MOM1 | PLA2 | PLA2B | PLA2L | PLA2S | PLAS1 | sPLA2 | sPLA2-IIA |
HGNC (Hugo) | PLA2G2A |
HGNC Previous name | PLA2B | PLA2L |
HGNC Previous name | "phospholipase A2, group IIA (platelets, synovial fluid)" |
LocusID (NCBI) | 5320 |
Atlas_Id | 41730 |
Location | 1p36.13 [Link to chromosome band 1p36] |
Location_base_pair | Starts at 19975431 and ends at 19979659 bp from pter ( according to GRCh38/hg38-Dec_2013) [Mapping PLA2G2A.png] |
Fusion genes (updated 2017) | Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands) |
GFRA1 (10q25.3) / PLA2G2A (1p36.13) | GNG7 (19p13.3) / PLA2G2A (1p36.13) | PLA2G2A (1p36.13) / AFDN (6q27) | |
PLA2G2A (1p36.13) / FBLN1 (22q13.31) | PLA2G2A (1p36.13) / ITGA6 (2q31.1) | PLA2G2A (1p36.13) / MBTPS1 (16q23.3) | |
PLA2G2A (1p36.13) / RPS24 (10q22.3) | PLA2G2A (1p36.13) / TAF15 (17q12) | TMCO4 (1p36.13) / PLA2G2A (1p36.13) | |
DNA/RNA |
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Figure 1. Structure of the PLA2G2A gene. | |
Description | Background: The phospholipase A2 (PLA2s) superfamily, consisting of at least 34 members subdivided into at least 15 groups, is a group of intracellular and secreted enzymes that hydrolyzes the sn-2 ester bond in glycerophospholipids found in lipoproteins and cellular membranes to liberate fatty acids and lysophospholipids that can act as intracellular second messengers or are further metabolized into mediators of a variety of cellular processes such as inflammation, proliferation, apoptosis and atherogenesis. PLA2s are a diverse family of enzymes in terms of sequence, localization, function, and divalent cation requirements. PLA2s are classified into several groups based on their size, structure, and need for divalent cations. Groups I, II, and III all contain secreted forms of PLA2, which are extracellular enzymes that have a low molecular mass of ~14 kD and require calcium ions for catalysis. PLA2G2A belongs to the subfamily of group II sPLA2s, comprising PLA2 group IIA, PLA2 group IIC, PLA2 group IID, PLA2 group IIE, PLA2 group IIF, and PLA2 group V. All of these enzymes are encoded by a cluster of highly homologous genes located within a ~250 kb genomic segment on human chromosome 1p35, and on its homologous region on mouse distal chromosome 4. PLA2G2A was first identified following the isolation and sequencing of proteins from the synovial fluid of human rheumatoid arthritis. A cDNA library prepared from peritoneal exudate cells identified a full-length PLA2G2A 0.8 kb transcript and cDNA of 435 nucleotides that encodes for a polypeptide of 144 amino acids with a molecular mass of 16 kD (~14 kD in the mature peptide). The protein was found to demonstrate features of the type II class of PLA2s, including conserved catalytic residues and a Ca2+-binding loop. Structure: The PLA2G2A gene is 4.98 kb in length, with 6 total exons and 4 protein coding exons. |
Transcription | 0.8 kb transcript of 435 nucleotides: atgaagaccctcctactgttggcagtgatcatgatctttggcctactgcaggcccatggg The PLA2G2A gene produces multiple transcripts arising from splice variants and alternative promoter usage. There are believed to be at least seven splice variants produced by usage of the predominant promoter. The gene contains 6 exons with 4 exons containing protein coding regions. Variants are produced that have different 5' UTRs. The longest and predominant transcript is NM_000300 with a processed length of 970 nt and a mRNA of 997 nt. This produces a mature mRNA (NP_000291.1) of 435 nt that encodes for a polypeptide of 144 amino acids. The different splice variants either encode for the same polypeptide or encode for no protein product. |
Protein |
Description | Structure: 144 amino acids: MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAAL SYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLE KRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDK AAATCFARNKTTYNKKYQYYSNKHCRGSTPRC The protein has a 20 amino acid signal sequence and a 124 amino acid mature peptide with a molecular mass of ~14 kD. PLA2G2A has protein domains typical of Type II PLA2s that include a highly conserved catalytic region (DXCCXXHD) and a Ca2+-binding loop (XCGXGG). PLA2G2A also shares with other PLA2s the characteristic seven cysteine disulfide bridges that are important for regulation and protein stability. |
Expression | PLA2G2A has been extensively studied in human tissues where its activity is associated with inflammation, host defense against bacteria, blood coagulation and atherosclerosis. PLA2G2A is expressed in prostate epithelial cells, coronary vascular smooth muscle cells, kidney uriniferous tubular epithelium, respiratory epithelial cells, pulmonary arterial smooth muscle cells, placenta, hepatocytes, stomach, small and large intestine, spleen, thymus, tonsil, parotid and lacrine glands, cartilage and bone marrow, seminal plasma, tears, platelets, neutrophils, eosinophils, mast cells, macrophages, and liver Kupfer cells. Many human cells can secrete PLA2G2A, including: mesangial cells, smooth muscle cells, endothelial cells, mast cells, neutrophils, macrophages, hepatic cells, platelets, Paneth cells, lacrimal cells, human tears, prostate cells, seminal plasma, chondrocytes, synoviocytes, and astrocytes. PLA2G2A is constitutively expressed in: spleen, thymus, tonsil, bone marrow, intestine (Paneth cells), liver (Kupfer cells), neutrophils, macrophages, mast cells, and Platelets. In these last 4 cell types PLA2G2A is stored in granules and secreted following cell activation. PLA2G2A is induced by inflammatory cytokines such as IL-6, TNF-alpha and IL-8 in smooth muscle cells and hepatocytes, which may be the main source of PLA2G2A in systemic inflammatory conditions. |
Function | Overview: PLA2G2A is involved in arachidonic acid metabolism, production of lysophospholipid-derived mediators, antimicrobial activity, anticoagulation, exocytosis of endocrine cells, release of pro-inflammatory mediators, cell proliferation, ischemic injury and allergic disease, lipid modifications, and cancer. These functions are mediated by both enzyme catalytic and no-catalytic activities of PLA2G2A. Phospholipase Catalytic activity. One important feature that discriminates PLA2G2A from other group II PLA2 family members is its highly cationic nature. PLA2G2A is highly basic with a pI of 9.4 and a net charge of +19; the positive charge is distributed over the surface of the protein and this permits the protein to bind anionic phospholipids, to bind tightly to anionic heparanoids such as heparin and heparan sulphate proteoglycans (HPSGs), and to form supra molecular aggregates, and in general PLA2G2A prefers substrates in aggregates (e.g., micelles). Thus, a large proportion of PLA2G2A protein will stick to cell surface molecules, as has been observed for recombinant PLA2 transfected into HEK293 cells. When bound to glycerophosphatidylinositol-anchored HSPGs such as glypicans, PLA2G2A is transferred to punctate compartments containing caveolin. Arachidonic acid metabolism. While PLA2G2A is clearly implicated in arachidonic acid release its relative importance in this activity in specific cells and tissues is still under investigation. cPLA2alpha/IVA-PLA2 is considered to be the primary enzyme responsible for arachidonic acid release in many cells. In some cells IVA and PLA2G2A cooperate in arachidonic acid release and PGE2 production (e.g., as shown in rat gastric cells). In other cells PLA2G2A activity is dependent on the activity of cPLA2s. The reason that PLA2G2A is believed to be less of a key factor in arachidonic acid release is that PLA2G2A prefers to act on anionic phospholipids such as phosphatidyl glycerol, phosphatidyl ethanolamine and phosphatidyl serine in marked preference to charge neutral phospatidylcholine (PA>PE PS>PC). But the outer leaflet of mammalian cells (and in general the extracellular environment) is normally zwitterionic (containing unperturbed phosphatidyl choline bilayers), making these cells refractory to hydrolysis; traumatized, necrotic and apoptotic cells are more susceptible to hydrolysis by PLA2G2A, one reason that PLA2G2A has been proposed to play a role in apoptotic processes. PLA2G2A added exogenously is poorly capable of releasing arachidonic acid because PLA2G2A binds poorly to zwitterioninc phospatidylcholine on the outer leaflets of resting cells. PLA2G2A may release arachidonic acid from the membrane microdomains where cell activation-induced membrane rearrangements including altered phospholipid symmetry, phospholipid oxidation, altered membrane fluidity, and possible sphingomyelin turnover. PLA2G2A is involved in Inflammation, an overview: PLA2G2A is induced during an inflammatory response by pro-inflammatory endotoxins and cytokines via both autocrine and paracrine processes and is involved in the acute phase of the immune responses. These stimuli can result from the action of microbial pathogens, chemical irritants, allergens and physical stress factors.PLA2G2A is an acute phase reactant and is found significantly increased in plasma in diseases that involve systemic inflammation such as sepsis, rheumatoid arthritis and cardiovascular diseases. For example, serum PLA2G2A concentrations can increase up to 1000 x fold in trauma and infection. Secreted PLA2G2A assists in the biosynthesis of lipid mediators in inflammatory cells such as mast cells, macrophages, neutrophils and eosinophils. Anti-inflammatory glucacorticoids are a potent suppressor of the induced expression of PLA2G2A. However, in certain contexts the actions of PLA2G2A may be anti-inflammatory. It plays a role in the removal of cell debris and micro particles resulting from tissue trauma and downstream lipid mediators such as prostaglandins may prevent chronic inflammation in tissues such as the gastrointestinal tract. PLA2G2A, a pro-inflammatory factor. Since the identification of PLA2G2A from synovial fluid of patients with rheumatoid arthritis, high levels of PLA2G2A have been detected in many inflammatory, autoimmune, and allergic disease like acute pancreatitis, septic shock, adult respiratory distress syndrome, Crohn's disease, ulcerative colitis, bronchial asthma, and allergic rhinitis. Serum levels of PLA2G2A can serve as an index of disease activity in rheumatoid arthritis. Moreover, expression of PLA2G2A by inflammatory cells is induced by pro-inflammatory stimuli like LPS, TNF-alpha, IL-1beta, IL-6, and IFN-gamma, and strongly repressed by anti-inflammatory glucocorticoids, indicating that expression of PLA2G2A is strongly associated with, and regulated by inflammatory responses. The enzymatic activity of PLA2 enzymes results in the generation of bioactive molecules such as lysophospholipids and free fatty acids, of which the release of arachidonic acid is of particular interest because it is the first and rate-limiting step in the generation of eicosanoids. Free arachidonic acid is metabolized by COXs and LOXs into various prostaglandins and leukotrienes, respectively, bioactive molecules that have a wide range of effects, including modulation of inflammatory responses. Although cPLA2 enzymes have been implicated in the release of arachidonic acid specifically for eicosanoid generation, there is functional coupling between sPLA2s and cPLA2. PLA2G2A and sPLA2-V have been demonstrated to enhance eicosanoid generation, e.g., by stimulating expression of inducible COX-2 in conjunction with other stimuli. COX-2 (also known as prostaglandin H synthase-2) converts arachidonic acid to PGH2, the immediate substrate for a variety of prostaglandin and thromboxane synthases. In the GI tract, COX-2 is best known for its promotion of inflammation, proliferation of cancer cells and resistance to apoptosis. Although the mechanisms through which sPLA2s stimulate COX-2 induction have not been completely resolved, sPLA2-mediated generation of lysophosphatidylcholine (lyso-PC) may play a role in this process. In addition, lyso-PC has been demonstrated to be a chemoattractant for monocytes, suggesting that sPLA2s mediate the influx of inflammatory cells during inflammation. In rodents, Pla2g2a and several other sPLA2s can also function as ligands for PLA2-binding proteins like the M-type PLA2 receptor PLA2R1. This receptor is expressed by various inflammatory cells like neutrophils and macrophages. Stimulation of the PLA2R1 by sPLA2s induces activation of signal transduction pathways involving p38 MAPK, ERK1/ERK2, phosphatidylinositol 3-kinase (PI3K) and Akt, and results in the induction of iNOS and the production of various cytokines that mediate inflammatory responses against bacterial infections. PLA2G2A, a potential anti-inflammatory factor. There is direct and indirect evidence that PLA2G2A may also act in an anti-inflammatory manner. Inbred strains of mice are naturally mutant or wildtype for the Pla2g2a allele. Several studies of gastric inflammation employing mice that expressed a wildtype allele of Pla2g2a, either as an endogenous copy or a transgene, clearly demonstrated that Pla2g2a+ mice were resistant to bacterially-induced gastric inflammation in comparison with C57BL/6 mice that expressed a mutant copy of Pla2g2a. In the DSS model of experimental IBD, C57BL/6 and Balb/c mice (Pla2g2a wildtype) were treated with DSS and it was observed that the C57BL/6 mice progressed to chronic inflammation while the Balb/c mice significantly upregulated production of PGE2, down-regulated expression of a great number of inflammatory cytokines and rapidly resolved the DSS-induced inflammation. This study indicated that PGE2 was protective against chronic inflammation, rather than a promoter of inflammation. Several other studies support this conclusion. DSS treatment of knockout mice that lack the EP4 PGE2 receptor caused a more severe colitis, greater mucosal damage, and enhanced proliferation of inflammatory CD4+ T cells when compared with EP4 wildtype mice. In rats, rectal injection of PGE2 following treatment with DSS caused the inhibition of tissue damage and the down-regulation of inflammatory cytokines. This finding was in agreement with the low levels of PGE2 observed upon enterocolitis relapse in the Lewis rat strain that is susceptible to relapse. PGE2 can also suppress Th1 cytokine production (IL-12, IFN-gamma) in intestinal macrophages, thereby helping to maintain resident macrophages in an anti-inflammatory mode. Indeed, COX-2 may have anti-inflammatory properties, and a number of studies suggest that inhibition of COX-2 and PGE2 can actually exacerbate IBD in mice. For example, in the IL-10 knockout model of colitis and inflammatory colon cancer, treatment of IL-10 knockout mice with the COX-2 selective inhibitors celecoxib and rofecoxib greatly increased the incidence of colitis. Thus, the specific context is a major determinant of whether a molecule acts in an inflammatory or anti-inflammatory fashion and this may be true for PGE2. PLA2G2A has potent bactericidal activity. The management of normal enteric and infectious bacterial flora by PLA2G2A in prevention of inflammatory disease in both mice and humans is well-documented. PLA2G2A is stored in secretory granules of platelets, neutrophils, mast cells, gastric cells, goblet cells and Paneth cells, and is also expressed by macrophages. These types of cells have a common function in the defense against microbacteria. PLA2G2A is particularly active against Gram+ bacterial cells where it demonstrates a preference for the inner cell membrane. The positively charged residues on the surface of the PLA2G2A protein allow it to penetrate through the negatively charged cell wall of Gram-positive bacteria, where its enzymatic activity is responsible for membrane phospholipid degradation and ultimately bacterial killing. Overexpression of human PLA2G2A in transgenic mice resulted in decreased mortality in experimental Staphylococcus aureus infection and improved clearance of bacteria from organs and body fluids, and provided protection against Bacillus anthracis infection. Hence, enzymatic activity of PLA2G2A forms a first line of defense against Gram-positive bacteria such as Bacillus, Listeria, Staphylococcus, Streptococcus, Enterococcus, and Clostridium. Catalytic-independent activity by PLA2G2A. Some biological effects of PLA2G2A are independent of its catalytic functions: catalytically inactive mutants can enhance COX-2 expression in connective tissue mast cells and catalytically inactive mutants can induce secretion of beta-glucuronidase, IL-6 and IL-8 from human eosinophils. Signaling mediated by binding to ανβ3 and α4β3 integrins stimulates proliferation of monocytes. PLA2G2A, arachidonic acid, and apoptosis. PLA2G2A has a preference for negatively charged lipid membranes containing anionic lipids like phosphatidylserine, due to its cationic nature. The outer leaflets of lipid bilayers in unperturbed cells have a neutral lipid composition enriched in phosphatidylcholines, sphingomyelin, and cholesterol, and form a poor substrate for PLA2G2A. However, cells that are undergoing apoptosis lose their membrane asymmetry, resulting in exposure of anionic lipids to the outer leaflet, thereby increasing the affinity for PLA2G2A binding. Moreover, perturbed cell membranes are also found in cancer cells. Apoptosis of transformed cancer cells is an important defense mechanism against neoplastic development, and PLA2 enzymes both promote and prevent apoptosis in different cell types under different pathological conditions. Addition of phospholipid scramblase, an enzyme that alters membrane symmetry, to HEK293 cells, caused an increase in PLA2G2A activity, resulting in an increase in arachidonic acid release and a slowing in cellular proliferation. Arachidonic acid produced by PLA2G2A enzymatic activity promotes apoptosis in colon cancer cells and in many other types of normal and cancer cells. Exogenous arachidonic acid is cytotoxic to HCT-116 colon cancer cells and causes an increase in the expression of pro-apoptotic genes such as caspase-3 and c-Jun and a decrease in the expression of genes that promote cancer cell survival. In another study, exogenous arachidonic acid caused a dramatic increase in rates of apoptosis in HCT-116 and SW480 colon cancer cells, a phenotype that was associated with the activation of neutral sphingomyelinase resulting in the greatly enhanced production of ceramide. Sphingomyelinases and their sphingolipid products confer resistance to colon cancer, including the suppression of tumorigenesis in ApcMin/+ mice. Sphingomyelin in the outer leaflet of healthy cells is not a substrate for PLA2G2A and inhibits its activity. It is possible that sphingomyelinase may stimulate PLA2G2A by the removal of inhibitory sphingomyelins. It has been reported that TNF-alpha induces sphingomyelinase hydrolysis, resulting in PLA2G2A activation and arachidonic acid release. Cytosolic PLA2's resistance to AOM-induced colon tumors was associated with a sharp increase in ceramide production in cPLA2 wildtype mice versus knockout mice. A similar mechanism may contribute to PLA2G2A's mode of action as has been shown with other sPLA2's. Interestingly, factors that promote release of arachidonic acid from cells, such as Vitamin D3 and other nuclear receptor agonists promote apoptosis despite the concurrent increase in lipoxygenases. PLA2G2A also induces apoptosis in a wide range of non-colonic cells including neurons, astrocytes, fibroblasts, murine macrophages and NK and cytotoxic T cells. Finally, while PGE2 is generally considered as a pro-cell-survival factor, it does induce apoptosis in certain cell types such as brain glial cells where PGE2 activates BAX. PLA2G2A receptors. In mice and rabbits PLA2G2A binds to a 180 kDa M-type high affinity receptor but no receptor has been identified in humans. Binding to this receptor in mice induces Pla2g2a internalization. Human PLA2G2A has been shown to bind to integrins (such as ανβ3 and α4β3), and to heparan sulfate proteoglycans such as glypican 1 and decorin. Inducers and downstream effectors of sPLA2-IIA. Factors that stimulate PLA2G2A include bacterial lipopolysaccarides (LPS), interleukin (IL)-1beta, IL-6, IL-8, tumor necrosis factor (TNF)-alpha, interferon (IFN)-gamma, phorbol esters, and cyclic AMP (cAMP) elevating agents. The PLA2G2A promoter has TATA and CAAT boxes and binding sites for AP-1, C/EBPs, CREB, NF-kappaB, STAT, PPAR-gamma, LXR/RXR heterodimers and NFATs. In some contexts PLA2G2A activation is dependent upon prior activation by cPLA2 and 12-LOX/15-LOX. Factors that inhibit PLA2G2A include TGF-beta, IL-10, epidermal growth factor (EGF), basic fibroblast growth factor (bFGF), platelet derived growth factor (PDGF) and insulin growth factor (IGF). Some of the molecules and pathways that act downstream of PLA2G2A include ERK1/2, inducible nitric oxide synthase (iNOS) in RAW264.7 macrophages, EGF, based on its ability to increase activation of EGF receptor (EGFR) in A431 cells, MUC16 in human conjunctive epithelium, and in human microvascular cells PLA2G2A induces NF-kappaB, intercellular adhesion molecule (ICAM)-1, IL-8, epithelial derived neutrophil activating peptide (ENA)-78/CXCL5 and growth regulated protein Gro-alpha/CXCL1. |
Homology | PLA2G2A is conserved in mice, rats, chimpanzees, cows and chickens. |
Mutations |
Somatic | 1 mutation listed: a small deletion in codon 47 of NM_000300.2 (HGMD). |
Implicated in |
Note | |
Entity | Gastric cancer |
Note | PLA2G2A expression is positively associated with resistance to human gastric cancer progression. PLA2G2A is a direct target of Wnt/beta catenin signaling in human gastric cancer; its expression is silenced by hypermethylation of promoter elements that contain beta catenin target sites; expression of PLA2G2A suppressed gastric cancer migration and invasion in cell culture and this phenotype was mediated by the inhibition of S100A4 and NEDD9; hemizygous gene deletions were found in at least two human gastric cancer cell lines. |
Entity | Colorectal cancer |
Note | The role of PLA2G2a in human colorectal cancer is unclear. In one study, expression of PLA2G2A was found to decline with cancer progression. Other studies have found that PLA2G2A is upregulated in human colon adenomas; that expression of PLA2G2A is associated with shorter disease free survival; that PLA2G2A is upregulated in MSI+ colorectal cancers but down-regulated in APC-dependent colorectal cancers; and another study found that PLA2G2A is highly expressed in normal colon mucosa but its expression did not vary in adenocarcinomas. With the exception of a single European family, there are no reports of mutations in PLA2G2A that are implicated in differential risk for familial colorectal cancer. However, PLA2G2A lies in a region of chromosome one that is frequently subject to LOH in a variety of human epithelial cancers, including colorectal cancers. Mouse strains that are naturally mutant for a truncation mutation that eliminates the Pla2g2a catalytic region in the protein (e.g., C57BL/6) are susceptible to intestinal tumorigenesis, compared with strains that express a wildtype Pla2g2a allele. Introduction of a wildtype Pla2g2a transgene into the susceptible C57BL/6 strain caused a significant reduction in tumor multiplicity, tumor size and progression in several mouse models of intestinal cancer, including ApcMin/+ mice, Muc2 knockout mice and mice treated with azoxymethane. |
Entity | Pancreatic cancer |
Note | Upregulation of PLA2G2A is associated with better prognosis. |
Entity | Prostate cancer |
Note | There is one report showing that expression of PLA2G2A is downregulated in metastatic human prostate cancer. However, many more groups have reported that expression of PLA2G2A is upregulated at all stages of prostate cancer with one report indicating that its upregulation may be androgen inducible. |
Entity | Ovarian cancer |
Note | PLA2G2A is decreased in ovarian cancer following chemotherapy. |
Entity | Breast cancer |
Note | Aberrant expression of PLA2G2A has been reported in breast cancer. |
Entity | Familial adenomatous polyposis (FAP) |
Note | PLA2G2A is reported to be a modifier for fundic gland polyposis in FAP patients. |
Entity | Gastric gland metaplasia |
Note | Increased levels of PLA2G2A are associated with gastric gland metaplasia. |
Entity | Inflammation |
Note | Upregulation of PLA2G2A is associated with a variety of inflammatory conditions. For example, large amounts of PLA2G2A is detected in exudating fluids and plasma of patients with various systemic and local inflammatory diseases such as Crohn's disease, ulcerative colitis, sepsis, psoriasis, arthritis, respiratory distress syndrome, and asthma. While the predominance of evidence links PLA2G2A to the promotion of inflammation, there is also some evidence that PLA2G2A, in some specific contexts, may exert anti-inflammatory actions, such as by its management of flora, its involvement in removal of cell debris and micro particles resulting from tissue trauma, and by production of anti-inflammatory lipid mediators, including a variety of eicosanoids. |
Entity | Atherosclerosis |
Note | PLA2G2A expression is increased in atherosclerotic lesions and its expression is associated with a decrease in levels of high density lipoprotein and in one report expression of PLA2G2A in macrophages is proposed to be the source of the upregulation. PLA2G2A can also modify LDL leading to more pronounced lipid accumulation in the vessel wall. |
Entity | Acute myocardial infarction |
Note | Increased levels of PLA2G2A are reported following these events. |
Entity | Renal infarction |
Note | Increased levels of PLA2G2A are reported in infracted kidneys, in the uriniferoustubular epithelium. |
Entity | Viral hepatitis |
Note | Levels of PLA2G2A are increased in hepatocytes with fatty degeneration associated with viral hepatitis C. |
Entity | Ischemia |
Note | PLA2G2A-induced changes in phospholipid integrity and toxic actions of free fatty acids and lysophospolipids may be critical for altered plasma membrane and mitochondrial permeability properties associated with ischemia and perfusion. |
Entity | Coronary heart disease |
Note | An increase in circulating PLA2G2A is associated with unstable angina and is considered a risk factor for cardiovascular disease; PLA2G2A is increased in infarcted tissues and severely damaged cardiomyocytes. |
Entity | Lung disorders |
Note | Expression of PLA2G2A is increased in patients with cystic fibrosis; PLA2G2A is expressed by alveolar macrophages. |
Entity | Brain disorders |
Note | Dysregulation of PLA2G2A is associated with Alzheimer disease, stroke, oxidative pathways in astrocytes and cortical neurons, apoptosis in neurons. |
Entity | Other disorders |
Note | Aberrant expression of PLA2G2A has been reported in glaucoma, pancreatitis, schizophrenia, affective disorder, diabetes. |
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Citation |
This paper should be referenced as such : |
Cormier, RT |
PLA2G2A (phospholipase A2, group IIA (platelets, synovial fluid)) |
Atlas Genet Cytogenet Oncol Haematol. 2011;15(2):198-207. |
Free journal version : [ pdf ] [ DOI ] |
Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 6 ] |
TMCO4/PLA2G2A (1p36)
t(1;2)(p36;q31) PLA2G2A/ITGA6 t(1;16)(p36;q23) PLA2G2A/MBTPS1 t(1;17)(p36;q12) PLA2G2A/TAF15 t(1;19)(p36;p13) GNG7/PLA2G2A t(1;22)(p36;q13) PLA2G2A/FBLN1 |
External links |
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