Macphee CH

References (13)

Title : Atherosclerotic plaque inflammation varies between vascular sites and correlates with response to inhibition of lipoprotein-associated phospholipase A2 - Fenning_2015_J.Am.Heart.Assoc_4_
Author(s) : Fenning RS , Burgert ME , Hamamdzic D , Peyster EG , Mohler ER , Kangovi S , Jucker BM , Lenhard SC , Macphee CH , Wilensky RL
Ref : J Am Heart Assoc , 4 : , 2015
Abstract : BACKGROUND: Despite systemic exposure to risk factors, the circulatory system develops varying patterns of atherosclerosis for unclear reasons. In a porcine model, we investigated the relationship between site-specific lesion development and inflammatory pathways involved in the coronary arteries (CORs) and distal abdominal aortas (AAs). METHODS AND RESULTS: Diabetes mellitus (DM) and hypercholesterolemia (HC) were induced in 37 pigs with 3 healthy controls. Site-specific plaque development was studied by comparing plaque severity, macrophage infiltration, and inflammatory gene expression between CORs and AAs of 17 DM/HC pigs. To assess the role of lipoprotein-associated phospholipase A2 (Lp-PLA2) in plaque development, 20 DM/HC pigs were treated with the Lp-PLA2 inhibitor darapladib and compared with the 17 DM/HC untreated pigs. DM/HC caused site-specific differences in plaque severity. In the AAs, normalized plaque area was 4.4-fold higher (P<0.001) and there were more fibroatheromas (9 of the 17 animals had a fibroatheroma in the AA and not the COR, P=0.004), while normalized macrophage staining area was 1.5-fold higher (P=0.011) compared with CORs. DM/HC caused differential expression of 8 of 87 atherosclerotic genes studied, including 3 important in inflammation with higher expression in the CORs. Darapladib-induced attenuation of normalized plaque area was site-specific, as CORs responded 2.9-fold more than AAs (P=0.045). CONCLUSIONS: While plaque severity was worse in the AAs, inflammatory genes and inflammatory pathways that use Lp-PLA2 were more important in the CORs. Our results suggest fundamental differences in inflammation between vascular sites, an important finding for the development of novel anti-inflammatory therapeutics.
ESTHER : Fenning_2015_J.Am.Heart.Assoc_4_
PubMedSearch : Fenning_2015_J.Am.Heart.Assoc_4_
PubMedID: 25672369

Title : Platelet aggregation unchanged by lipoprotein-associated phospholipase A inhibition: results from an in vitro study and two randomized phase I trials - Shaddinger_2014_PLoS.One_9_e83094
Author(s) : Shaddinger BC , Xu Y , Roger JH , Macphee CH , Handel M , Baidoo CA , Magee M , Lepore JJ , Sprecher DL
Ref : PLoS ONE , 9 :e83094 , 2014
Abstract : BACKGROUND: We explored the theorized upregulation of platelet-activating factor (PAF)- mediated biologic responses following lipoprotein-associated phospholipase A2 (Lp-PLA2) inhibition using human platelet aggregation studies in an in vitro experiment and in 2 clinical trials. METHODS AND RESULTS: Full platelet aggregation concentration response curves were generated in vitro to several platelet agonists in human plasma samples pretreated with rilapladib (selective Lp-PLA2 inhibitor) or vehicle. This was followed by a randomized, double-blind crossover study in healthy adult men (n=26) employing a single-agonist dose assay of platelet aggregation, after treatment of subjects with 250 mg oral rilapladib or placebo once daily for 14 days. This study was followed by a second randomized, double-blind parallel-group trial in healthy adult men (n=58) also treated with 250 mg oral rilapladib or placebo once daily for 14 days using a full range of 10 collagen concentrations (0-10 microg/ml) for characterizing EC50 values for platelet aggregation for each subject. Both clinical studies were conducted at the GlaxoSmithKline Medicines Research Unit in the Prince of Wales Hospital, Sydney, Australia. EC50 values derived from multiple agonist concentrations were compared and no pro-aggregant signals were observed during exposure to rilapladib in any of these platelet studies, despite Lp-PLA2 inhibition exceeding 90%. An increase in collagen-mediated aggregation was observed 3 weeks post drug termination in the crossover study (15.4% vs baseline; 95% confidence interval [CI], 3.9-27.0), which was not observed during the treatment phase and was not observed in the parallel-group study employing a more robust EC50 examination. CONCLUSIONS: Lp-PLA2 inhibition does not enhance platelet aggregation. TRIAL REGISTRATION: 1) Study 1: NCT01745458 2) Study 2: NCT00387257.
ESTHER : Shaddinger_2014_PLoS.One_9_e83094
PubMedSearch : Shaddinger_2014_PLoS.One_9_e83094
PubMedID: 24475026

Title : Effect of darapladib treatment on endarterectomy carotid plaque lipoprotein-associated phospholipase A2 activity: a randomized, controlled trial - Johnson_2014_PLoS.One_9_e89034
Author(s) : Johnson JL , Shi Y , Snipes R , Janmohamed S , Rolfe TE , Davis B , Postle A , Macphee CH
Ref : PLoS ONE , 9 :e89034 , 2014
Abstract : BACKGROUND: The aim of this study was to assess the effects of darapladib, a selective oral investigational lipoprotein-associated phospholipase A2 inhibitor, on both plasma and plaque lipoprotein-associated phospholipase A2 activity. METHODS: Patients undergoing elective carotid endarterectomy were randomized to darapladib 40 mg (n = 34), 80 mg (n = 34), or placebo (n = 34) for 14 days, followed by carotid endarterectomy 24 hours after the last dose of study medication. RESULTS: Darapladib 40 mg and 80 mg reduced plasma lipoprotein-associated phospholipase A2 activity by 52% and 81%, respectively, versus placebo (both P<0.001). Significant reductions in plaque lipoprotein-associated phospholipase A2 activity were also observed compared with placebo (P<0.0001), which equated to a 52% and 80% decrease compared with placebo. No significant differences were observed between groups in plaque lysophosphatidylcholine content or other biomarkers, although a dose-dependent decrease in plaque matrix metalloproteinase-9 mRNA expression was observed with darapladib 80 mg (P = 0.053 vs placebo). In a post-hoc analysis, plaque caspase-3 (P<0.001) and caspase-8 (P<0.05) activity were found to be significantly lower in the darapladib 80-mg group versus placebo. No major safety concerns were identified in the study. CONCLUSIONS: Short-term treatment (14 +/- 4 days) with darapladib produced a robust, dose-dependent reduction in plasma lipoprotein-associated phospholipase A2 activity. More importantly, darapladib demonstrated placebo-corrected reductions in carotid plaque lipoprotein-associated phospholipase A2 activity of similar magnitude. Darapladib was generally well tolerated and no safety concerns were identified. Additional studies of longer duration are needed to explore whether these pharmacodynamic effects are associated with improved clinical outcomes, as might be hypothesized.
ESTHER : Johnson_2014_PLoS.One_9_e89034
PubMedSearch : Johnson_2014_PLoS.One_9_e89034
PubMedID: 24586490

Title : Lipoprotein-associated phospholipase A(2) and atherosclerosis - Wilensky_2009_Curr.Opin.Lipidol_20_415
Author(s) : Wilensky RL , Macphee CH
Ref : Curr Opin Lipidol , 20 :415 , 2009
Abstract : PURPOSE OF REVIEW: There is substantial data from over 50 000 patients that increased lipoprotein-associated phospholipase A2 (Lp-PLA2) mass or activity is associated with an increased risk of cardiac death, myocardial infarction, acute coronary syndromes and ischemic stroke. However, only recently have data emerged demonstrating a role of Lp-PLA2 in development of advanced coronary artery disease. Indeed, Lp-PLA2 may be an important link between lipid homeostasis and the vascular inflammatory response. RECENT FINDINGS: Lp-PLA2, also known as platelet-activating factor acetylhydrolase, rapidly cleaves oxidized phosphatidylcholine molecules produced during the oxidation of LDL and atherogenic lipoprotein Lp(a), generating the soluble proinflammatory and proapoptotic lipid mediators, lyso-phosphatidylcholine and oxidized nonesterified fatty acids. These proinflammatory lipids play an important role in the development of atherosclerotic necrotic cores, the substrate for acute unstable coronary disease by recruiting and activating leukocytes/macrophages, inducing apoptosis and impairing the subsequent removal of dead cells. Selective inhibition of Lp-PLA2 reduces development of necrotic cores and may result in stabilization of atherosclerotic plaques. SUMMARY: Recent data have shown that immune pathways play a major role in the development and progression of high-risk atherosclerosis, which leads to ischemic sudden death, myocardial infarction, acute coronary syndromes and ischemic strokes. Persistent and sustained macrophage apoptosis appears to play a major role in the resulting local inflammatory response in part by effects elicited by Lp-PLA2. Selective inhibition of Lp-PLA2 has been postulated to reduce necrotic core progression and the clinical sequelae of advanced, unstable atherosclerosis.
ESTHER : Wilensky_2009_Curr.Opin.Lipidol_20_415
PubMedSearch : Wilensky_2009_Curr.Opin.Lipidol_20_415
PubMedID: 19667981

Title : Inhibition of lipoprotein-associated phospholipase A2 reduces complex coronary atherosclerotic plaque development - Wilensky_2008_Nat.Med_14_1059
Author(s) : Wilensky RL , Shi Y , Mohler ER, 3rd , Hamamdzic D , Burgert ME , Li J , Postle A , Fenning RS , Bollinger JG , Hoffman BE , Pelchovitz DJ , Yang J , Mirabile RC , Webb CL , Zhang L , Zhang P , Gelb MH , Walker MC , Zalewski A , Macphee CH
Ref : Nat Med , 14 :1059 , 2008
Abstract : Increased lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) activity is associated with increased risk of cardiac events, but it is not known whether Lp-PLA(2) is a causative agent. Here we show that selective inhibition of Lp-PLA(2) with darapladib reduced development of advanced coronary atherosclerosis in diabetic and hypercholesterolemic swine. Darapladib markedly inhibited plasma and lesion Lp-PLA(2) activity and reduced lesion lysophosphatidylcholine content. Analysis of coronary gene expression showed that darapladib exerted a general anti-inflammatory action, substantially reducing the expression of 24 genes associated with macrophage and T lymphocyte functioning. Darapladib treatment resulted in a considerable decrease in plaque area and, notably, a markedly reduced necrotic core area and reduced medial destruction, resulting in fewer lesions with an unstable phenotype. These data show that selective inhibition of Lp-PLA(2) inhibits progression to advanced coronary atherosclerotic lesions and confirms a crucial role of vascular inflammation independent from hypercholesterolemia in the development of lesions implicated in the pathogenesis of myocardial infarction and stroke.
ESTHER : Wilensky_2008_Nat.Med_14_1059
PubMedSearch : Wilensky_2008_Nat.Med_14_1059
PubMedID: 18806801
Gene_locus related to this paper: human-PLA2G7

Title : The identification of clinical candidate SB-480848: a potent inhibitor of lipoprotein-associated phospholipase A2 - Blackie_2003_Bioorg.Med.Chem.Lett_13_1067
Author(s) : Blackie JA , Bloomer JC , Brown MJ , Cheng HY , Hammond B , Hickey DM , Ife RJ , Leach CA , Lewis VA , Macphee CH , Milliner KJ , Moores KE , Pinto IL , Smith SA , Stansfield IG , Stanway SJ , Taylor MA , Theobald CJ
Ref : Bioorganic & Medicinal Chemistry Lett , 13 :1067 , 2003
Abstract : Modification of the pyrimidone 5-substituent in clinical candidate SB-435495 has given a series of inhibitors of recombinant lipoprotein-associated phospholipase A(2) with sub-nanomolar potency. Cyclopentyl fused derivative 21, SB-480848, showed an enhanced in vitro and in vivo profile versus SB-435495 and has been selected for progression to man.
ESTHER : Blackie_2003_Bioorg.Med.Chem.Lett_13_1067
PubMedSearch : Blackie_2003_Bioorg.Med.Chem.Lett_13_1067
PubMedID: 12643913

Title : The identification of a potent, water soluble inhibitor of lipoprotein-associated phospholipase A2 - Boyd_2001_Bioorg.Med.Chem.Lett_11_701
Author(s) : Boyd HF , Hammond B , Hickey DM , Ife RJ , Leach CA , Lewis VA , Macphee CH , Milliner KJ , Pinto IL , Smith SA , Stansfield IG , Theobald CJ , Whittaker CM
Ref : Bioorganic & Medicinal Chemistry Lett , 11 :701 , 2001
Abstract : Modification of the pyrimidone 5-substituent in a series of 1-((amidolinked)-alkyl)-pyrimidones, lipophilic inhibitors of lipoprotein-associated phospholipase A2, has given inhibitors of nanomolar potency and improved physicochemical properties. Compound 23 was identified as a potent, highly water soluble. CNS penetrant inhibitor suitable for intravenous administration.
ESTHER : Boyd_2001_Bioorg.Med.Chem.Lett_11_701
PubMedSearch : Boyd_2001_Bioorg.Med.Chem.Lett_11_701
PubMedID: 11266173

Title : Lipoprotein-associated phospholipase A2 as an independent predictor of coronary heart disease. West of Scotland Coronary Prevention Study Group - Packard_2000_N.Engl.J.Med_343_1148
Author(s) : Packard CJ , O'Reilly DS , Caslake MJ , McMahon AD , Ford I , Cooney J , Macphee CH , Suckling KE , Krishna M , Wilkinson FE , Rumley A , Lowe GD
Ref : N Engl J Med , 343 :1148 , 2000
Abstract : BACKGROUND: Chronic inflammation is believed to increase the risk of coronary events by making atherosclerotic plaques in coronary vessels prone to rupture. We examined blood constituents potentially affected by inflammation as predictors of risk in men with hypercholesterolemia who were enrolled in the West of Scotland Coronary Prevention Study, a trial that evaluated the value of pravastatin in the prevention of coronary events.
METHODS: A total of 580 men who had had a coronary event (nonfatal myocardial infarction, death from coronary heart disease, or a revascularization procedure) were each matched for age and smoking status with 2 control subjects (total, 1160) from the same cohort who had not had a coronary event. Lipoprotein-associated phospholipase A2, C-reactive protein, and fibrinogen levels, and the white-cell count were measured at base line, along with other traditional risk factors. The association of these variables with the risk of coronary events was tested in regression models and by dividing the range of values according to quintiles.
RESULTS: Levels of C-reactive protein, the white-cell count, and fibrinogen levels were strong predictors of the risk of coronary events; the risk in the highest quintile of the study cohort for each variable was approximately twice that in the lowest quintile. However, the association of these variables with risk was markedly attenuated when age, systolic blood pressure, and lipoprotein levels were included in multivariate models. Levels of lipoprotein-associated phospholipase A2 (platelet-activating factor acetylhydrolase), the expression of which is regulated by mediators of inflammation, had a strong, positive association with risk that was not confounded by other factors. It was associated with almost a doubling of the risk in the highest quintile as compared with the lowest quintile.
CONCLUSIONS: Inflammatory markers are predictors of the risk of coronary events, but their predictive ability is attenuated by associations with other coronary risk factors. Elevated levels of lipoprotein-associated phospholipase A2 appear to be a strong risk factor for coronary heart disease, a finding that has implications for atherogenesis and the assessment of risk.
ESTHER : Packard_2000_N.Engl.J.Med_343_1148
PubMedSearch : Packard_2000_N.Engl.J.Med_343_1148
PubMedID: 11036120
Gene_locus related to this paper: human-PLA2G7

Title : 2-(Alkylthio)pyrimidin-4-ones as novel, reversible inhibitors of lipoprotein-associated phospholipase A2 - Boyd_2000_Bioorg.Med.Chem.Lett_10_395
Author(s) : Boyd HF , Flynn ST , Hickey DM , Ife RJ , Jones M , Leach CA , Macphee CH , Milliner KJ , Rawlings DA , Slingsby BP , Smith SA , Stansfield IG , Tew DG , Theobald CJ
Ref : Bioorganic & Medicinal Chemistry Lett , 10 :395 , 2000
Abstract : Starting from two weakly active hits from high throughput screening, a novel series of 2-(alkylthio)-pyrimidin-4-ones with high potency and selectivity for lipoprotein-associated phospholipase A2 has been designed. In contrast to previously known inhibitors, these have been shown to act by a non-covalent and substrate competitive mechanism.
ESTHER : Boyd_2000_Bioorg.Med.Chem.Lett_10_395
PubMedSearch : Boyd_2000_Bioorg.Med.Chem.Lett_10_395
PubMedID: 10714508

Title : Lipoprotein-associated phospholipase A2, platelet-activating factor acetylhydrolase, generates two bioactive products during the oxidation of low-density lipoprotein: use of a novel inhibitor - MacPhee_1999_Biochem.J_338 ( Pt 2)_479
Author(s) : Macphee CH , Moores KE , Boyd HF , Dhanak D , Ife RJ , Leach CA , Leake DS , Milliner KJ , Patterson RA , Suckling KE , Tew DG , Hickey DM
Ref : Biochemical Journal , 338 ( Pt 2) :479 , 1999
Abstract : A novel and potent azetidinone inhibitor of the lipoprotein-associated phospholipase A2 (Lp-PLA2), i.e. platelet-activating factor acetylhydrolase, is described for the first time. This inhibitor, SB-222657 (Ki=40+/-3 nM, kobs/[I]=6. 6x10(5) M-1.s-1), is inactive against paraoxonase, is a poor inhibitor of lecithin:cholesterol acyltransferase and has been used to investigate the role of Lp-PLA2 in the oxidative modification of lipoproteins. Although pretreatment with SB-222657 did not affect the kinetics of low-density lipoprotein (LDL) oxidation by Cu2+ or an azo free-radical generator as determined by assay of lipid hydroperoxides (LOOHs), conjugated dienes and thiobarbituric acid-reacting substances, in both cases it inhibited the elevation in lysophosphatidylcholine content. Moreover, the significantly increased monocyte chemoattractant activity found in a non-esterified fatty acid fraction from LDL oxidized by Cu2+ was also prevented by pretreatment with SB-222657, with an IC50 value of 5.0+/-0.4 nM. The less potent diastereoisomer of SB-222657, SB-223777 (Ki=6.3+/-0.5 microM, kobs/[I]=1.6x10(4) M-1.s-1), was found to be significantly less active in both assays. Thus, in addition to generating lysophosphatidylcholine, a known biologically active lipid, these results demonstrate that Lp-PLA2 is capable of generating oxidized non-esterified fatty acid moieties that are also bioactive. These findings are consistent with our proposal that Lp-PLA2 has a predominantly pro-inflammatory role in atherogenesis. Finally, similar studies have demonstrated that a different situation exists during the oxidation of high-density lipoprotein, with enzyme(s) other than Lp-PLA2 apparently being responsible for generating lysophosphatidylcholine.
ESTHER : MacPhee_1999_Biochem.J_338 ( Pt 2)_479
PubMedSearch : MacPhee_1999_Biochem.J_338 ( Pt 2)_479
PubMedID: 10024526

Title : Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor - Rice_1998_Biochem.J_330 ( Pt 3)_1309
Author(s) : Rice SQ , Southan C , Boyd HF , Terrett JA , Macphee CH , Moores K , Gloger IS , Tew DG
Ref : Biochemical Journal , 330 ( Pt 3) :1309 , 1998
Abstract : Using expressed sequence tag (EST) homology screening, a new human serine dependent phospholipase A2 (HSD-PLA2) was identified that has 40% amino acid identity with human low density lipoprotein-associated phospholipase A2 (LDL-PLA2). HSD-PLA2 has very recently been purified and cloned from brain tissue but named PAF-AH II. However, because the homology with LDL-PLA2 suggested a broader substrate specificity than simply platelet activating factor (PAF), we have further characterized this enzyme using baculovirus-expressed protein. The recombinant enzyme, which was purified 21-fold to homogeneity, had a molecular mass of 44kDa and possessed a specific activity of 35 micromol min-1 mg-1 when assayed against PAF. Activity could also be measured using 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate (DNGP) as substrate. Like LDL-PLA2, HSD-PLA2 was able to hydrolyse oxidatively modified phosphatidylcholines when supplemented to human LDL prior to copper-stimulated oxidation. A GXSXG motif evident from sequence information and inhibition of its activity by 3,4, dichloroisocoumarin, diisopropyl fluorophosphate (DFP) and diethyl p-nitrophenyl phosphate (DENP) confirm that the enzyme is serine dependent. Moreover, sequence comparison indicates the HSD-PLA2 probable active site triad positions are shared with LDL-PLA2 and a C. elegans homologue, suggesting that these sequences comprise members of a new enzyme family. Although clearly structurally related with similar substrate specificities further work reported here shows HSD-PLA2 and LDL-PLA2 to be different with respect to chromosomal localization and tissue distribution.
ESTHER : Rice_1998_Biochem.J_330 ( Pt 3)_1309
PubMedSearch : Rice_1998_Biochem.J_330 ( Pt 3)_1309
PubMedID: 9494101
Gene_locus related to this paper: human-PAFAH2

Title : Systematic screening of the LDL-PLA2 gene for polymorphic variants and case-control analysis in schizophrenia - Bell_1997_Biochem.Biophys.Res.Commun_241_630
Author(s) : Bell R , Collier DA , Rice SQ , Roberts GW , Macphee CH , Kerwin RW , Price J , Gloger IS
Ref : Biochemical & Biophysical Research Communications , 241 :630 , 1997
Abstract : Systematic scans of the genome using microsatellite markers have identified chromosome 6p21.1 as a putative locus for schizophrenia in multiply affected families. There is also evidence from a series of studies for a role of abnormal phospholipid metabolism in schizophrenia. In light of these findings, and the role of platelet activating factor in neurotransmission and neurodevelopment, we have examined the LDL-PLA2 (plasma PAF acetylhydrolase, PAF-AH) gene, a serine dependent phospholipase that has been mapped by hybrid mapping to chromosome 6p21.1, as a positional candidate gene for schizophrenia. The gene was systematically screened using SSCP/HD analysis for polymorphisms associated with the disease. Four polymorphic variants were found within the gene and studied in a group of 200 schizophrenic patients and 100 controls. The variant in exon 7 (Iso195Thr) was found to be weakly associated with schizophrenia (p = 0.04) and the variant in exon 11 (Val379Ala) almost reached significance (p = 0.057). After correcting for multiple testing no significant associations were detected. Haplotype analysis combining pairs of polymorphisms also provided no evidence for association of this gene with schizophrenia in our sample of patients.
ESTHER : Bell_1997_Biochem.Biophys.Res.Commun_241_630
PubMedSearch : Bell_1997_Biochem.Biophys.Res.Commun_241_630
PubMedID: 9434759
Gene_locus related to this paper: human-PLA2G7

Title : Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins - Tew_1996_Arterioscler.Thromb.Vasc.Biol_16_591
Author(s) : Tew DG , Southan C , Rice SQ , Lawrence MP , Li H , Boyd HF , Moores K , Gloger IS , Macphee CH
Ref : Arterioscler Thromb Vasc Biol , 16 :591 , 1996
Abstract : A novel LDL-associated phospholipase A2 (LDL-PLA2) has been purified to homogeneity from human LDL obtained from plasma apheresis. This enzyme has activity toward both oxidized phosphatidylcholine and platelet activating factor (PAF). A simple purification procedure involving detergent solubilization and affinity and ion exchange chromatography has been devised. Vmax and Km for the purified enzyme are 170 and 12 micromol/L, respectively. Extensive peptide sequence from LDL-PLA2 facilitated identification of an expressed sequence tag partial cDNA. This has led to cloning and expression of active protein in baculovirus. A lipase motif is also evident from sequence information, indicating that the enzyme is serine dependent. Inhibition by diethyl p-nitrophenyl phosphate and 3,4-dichloroisocoumarin and insensitivity to EDTA, Ca2+, and sulfhydryl reagents confirm that the enzyme is indeed a serine-dependent hydrolase. The protein is extensively glycosylated, and the glycosylation site has been identified. Antibodies to this LDL-PLA2 have been raised and used to show that this enzyme is responsible for >95% of the phospholipase activity associated with LDL. Inhibition of LDL-PLA2 before oxidation of LDL reduces both lysophosphatidylcholine content and monocyte chemoattractant ability of the resulting oxidized LDL. Lysophosphatidylcholine production and monocyte chemoattractant ability can be restored by addition of physiological quantities of pure LDL-PLA2.
ESTHER : Tew_1996_Arterioscler.Thromb.Vasc.Biol_16_591
PubMedSearch : Tew_1996_Arterioscler.Thromb.Vasc.Biol_16_591
PubMedID: 8624782
Gene_locus related to this paper: human-PLA2G7