Emergence of a metalloproteinase/phospholipase A₂ axis of systemic inflammation

References

• Gross J, Nagai Y. Specific degradation of the collagen molecule by tadpole collagenolytic enzyme. Proc Natl Acad Sci U S A. 1965;54(4):1197–1204.
   Web of Science ®Google Scholar
• Schulz R. Intracellular targets of matrix metalloproteinase-2 in cardiac disease: rationale and therapeutic approaches. Annu Rev Pharmacol Toxicol. 2007;47:211–242.
   PubMed Web of Science ®Google Scholar
• Berry E, Bosonea AM, Wang X, Fernandez-Patron C. Insights into the activity, differential expression, mutual regulation, and functions of matrix metalloproteinases and a disintegrin and metalloproteinases in hypertension and cardiac disease. J Vasc Res. 2013;50(1):52–68.
   Web of Science ®Google Scholar
• Derynck R, Zhang YE. Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature. 2003;425(6958):577–584.
   PubMed Web of Science ®Google Scholar
• Imai K, Hiramatsu A, Fukushima D, Pierschbacher MD, Okada Y. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem J. 1997;322(Pt 3):809–814.
   PubMedGoogle Scholar
• Prudova A, auf dem Keller U, Butler GS, Overall CM. Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics. Mol Cell Proteomics. 2010;9(5):894–911.
   PubMed Web of Science ®Google Scholar
• Rodriguez D, Morrison CJ, Overall CM. Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics. Biochim Biophys Acta. 2010;1803(1):39–54.
   PubMed Web of Science ®Google Scholar
• McQuibban GA, Gong JH, Tam EM, McCulloch CA, Clark-Lewis I, Overall CM. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science. 2000;289(5482):1202–1206.
   PubMed Web of Science ®Google Scholar
• McQuibban GA, Gong JH, Wong JP, Wallace JL, Clark-Lewis I, Overall CM. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood. 2002;100(4):1160–1167.
   PubMed Web of Science ®Google Scholar
• Morrison CJ, Butler GS, Rodriguez D, Overall CM. Matrix metalloproteinase proteomics: substrates, targets, and therapy. Curr Opin Cell Biol. 2009;21(5):645–653.
   PubMed Web of Science ®Google Scholar
• Fernandez-Patron C, Radomski MW, Davidge ST. Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor. Circ Res. 1999;85(10):906–911.
   PubMed Web of Science ®Google Scholar
• Fernandez-Patron C, Stewart KG, Zhang Y, Koivunen E, Radomski MW, Davidge ST. Vascular matrix metalloproteinase-2-dependent cleavage of calcitonin gene-related peptide promotes vasoconstriction. Circ Res. 2000;87(8):670–676.
   PubMed Web of Science ®Google Scholar
• Martínez A, Oh HR, Unsworth EJ, et al. Matrix metalloproteinase-2 cleavage of adrenomedullin produces a vasoconstrictor out of a vasodilator. Biochem J. 2004;383(Pt 3):413–418.
   Google Scholar
• Jeyabalan A, Novak J, Danielson LA, Kerchner LJ, Opett SL, Conrad KP. Essential role for vascular gelatinase activity in relaxin-induced renal vasodilation, hyperfiltration, and reduced myogenic reactivity of small arteries. Circ Res. 2003;93(12):1249–1257.
   PubMed Web of Science ®Google Scholar
• Hao L, Du M, Lopez-Campistrous A, Fernandez-Patron C. Agonist- induced activation of matrix metalloproteinase-7 promotes vasoconstriction through the epidermal growth factor-receptor pathway. Circ Res. 2004;94(1):68–76.
   Web of Science ®Google Scholar
• Friese RS, Rao F, Khandrika S, et al. Matrix metalloproteinases: discrete elevations in essential hypertension and hypertensive end-stage renal disease. Clin Exp Hypertens. 2009;31(7):521–533.
   PubMed Web of Science ®Google Scholar
• Rodrigues SF, Tran ED, Fortes ZB, Schmid-Schonbein GW. Matrix metalloproteinases cleave the beta2-adrenergic receptor in spontaneously hypertensive rats. Am J Physiol Heart Circ Physiol. 2010;299(1):H25–H35.
   Web of Science ®Google Scholar
• DeLano FA, Schmid-Schönbein GW. Proteinase activity and receptor cleavage: mechanism for insulin resistance in the spontaneously hypertensive rat. Hypertension. 2008;52(2):415–423.
   Web of Science ®Google Scholar
• Castro MM, Rizzi E, Figueiredo-Lopes L, et al. Metalloproteinase inhibition ameliorates hypertension and prevents vascular dysfunction and remodeling in renovascular hypertensive rats. Atherosclerosis. 2008;198(2):320–331.
   Web of Science ®Google Scholar
• Merchant SJ, Narumiya H, Zhang Y, Guilbert LJ, Davidge ST. The effects of preeclampsia and oxygen environment on endothelial release of matrix metalloproteinase-2. Hypertens Pregnancy. 2004;23(1):47–60.
   PubMed Web of Science ®Google Scholar
• Lekontseva ON, Rueda-Clausen CF, Morton JS, Davidge ST. Ovariectomy in aged versus young rats augments matrix metalloproteinase-mediated vasoconstriction in mesenteric arteries. Menopause. 2010;17(3):516–523.
   Web of Science ®Google Scholar
• Lekontseva O, Jiang Y, Davidge ST. Estrogen replacement increases matrix metalloproteinase contribution to vasoconstriction in a rat model of menopause. J Hypertens. 2009;27(8):1602–1608.
   PubMed Web of Science ®Google Scholar
• Conrad KP, Davison JM. The renal circulation in normal pregnancy and preeclampsia: is there a place for relaxin? Am J Physiol Renal Physiol. 2014;306(10):F1121–F1135.
   PubMed Web of Science ®Google Scholar
• Jeyabalan A, Novak J, Doty KD, et al. Vascular matrix metalloproteinase-9 mediates the inhibition of myogenic reactivity in small arteries isolated from rats after short-term administration of relaxin. Endocrinology. 2007;148(1):189–197.
   PubMed Web of Science ®Google Scholar
• Narumiya H, Zhang Y, Fernandez-Patron C, Guilbert LJ, Davidge ST. Matrix metalloproteinase-2 is elevated in the plasma of women with preeclampsia. Hypertens Pregnancy. 2001;20(2):185–194.
   PubMed Web of Science ®Google Scholar
• Myers JE, Merchant SJ, Macleod M, Mires GJ, Baker PN, Davidge ST. MMP-2 levels are elevated in the plasma of women who subsequently develop preeclampsia. Hypertens Pregnancy. 2005;24(2):103–115.
   PubMed Web of Science ®Google Scholar
• Brennan LJ, Morton JS, Davidge ST. Vascular dysfunction in preeclampsia. Microcirculation. 2014;21(1):4–14.
   PubMed Web of Science ®Google Scholar
• Wang X, Berry E, Hernandez-Anzaldo S, Takawale A, Kassiri Z, Fernandez-Patron C. Matrix metalloproteinase-2 mediates a mechanism of metabolic cardioprotection consisting of negative regulation of the sterol regulatory element-binding protein-2/3-hydroxy-3-methylglutaryl-CoA reductase pathway in the heart. Hypertension. 2015;65(4):882–888.
   Web of Science ®Google Scholar
• Van Hul M, Lijnen HR. A functional role of gelatinase A in the development of nutritionally induced obesity in mice. J Thromb Haemost. 2008;6(7):1198–1206.
   PubMed Web of Science ®Google Scholar
• Lijnen HR, Demeulemeester D, Van Hoef B, Collen D, Maquoi E. Deficiency of tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) impairs nutritionally induced obesity in mice. Thromb Haemost. 2003;89(2):249–255.
   PubMed Web of Science ®Google Scholar
• Lee SW, Song KE, Shin DS, et al. Alterations in peripheral blood levels of TIMP-1, MMP-2, and MMP-9 in patients with type-2 diabetes. Diabetes Res Clin Pract. 2005;69(2):175–179.
   Web of Science ®Google Scholar
• Jaworski DM, Sideleva O, Stradecki HM, et al. Sexually dimorphic diet-induced insulin resistance in obese tissue inhibitor of metalloproteinase-2 (TIMP-2)-deficient mice. Endocrinology. 2011;152(4):1300–1313.
   Web of Science ®Google Scholar
• Van Hul M, Piccard H, Lijnen HR. Gelatinase B (MMP-9) deficiency does not affect murine adipose tissue development. Thromb Haemost. 2010;104(1):165–171.
   Web of Science ®Google Scholar
• Van Hul M, Lijnen HR. Effect of weight loss on gelatinase levels in obese mice. Clin Exp Pharmacol Physiol. 2011;38(9):647–649.
   Web of Science ®Google Scholar
• Van Hul M, Bauters D, Lijnen RH. Differential effects of a gelatinase inhibitor on adipocyte differentiation and adipose tissue development. Clin Exp Pharmacol Physiol. 2013;40(10):689–697.
   Web of Science ®Google Scholar
• Van Hul M, Bauters D, Himmelreich U, et al. Effect of gelatinase inhibition on adipogenesis and adipose tissue development. Clin Exp Pharmacol Physiol. 2012;39(1):49–56.
   Web of Science ®Google Scholar
• Lijnen HR, Silence J, Lemmens G, Frederix L, Collen D. Regulation of gelatinase activity in mice with targeted inactivation of components of the plasminogen/plasmin system. Thromb Haemost. 1998;79(6):1171–1176.
   Web of Science ®Google Scholar
• Bauters D, Van Hul M, Lijnen HR. Gelatinase B (MMP-9) gene silencing does not affect murine preadipocyte differentiation. Adipocyte. 2014;3(1):50–53.
   PubMedGoogle Scholar
• Park JY, Park JH, Jang W, et al. Apolipoprotein A-IV is a novel substrate for matrix metalloproteinases. J Biochem. 2011;151(3):291–298.
   Web of Science ®Google Scholar
• Park JH, Park SM, Park SH, Cho KH, Lee ST. Cleavage and functional loss of human apolipoprotein E by digestion of matrix metalloproteinase-14. Proteomics. 2008;8(14):2926–2935.
   Web of Science ®Google Scholar
• Park JH, Park SM, Park KH, Cho KH, Lee ST. Analysis of apolipoprotein A-I as a substrate for matrix metalloproteinase-14. Biochem Biophys Res Commun. 2011;409(1):58–63.
   Web of Science ®Google Scholar
• Marcel YL, Kiss RS. Structure-function relationships of apolipoprotein A-I: a flexible protein with dynamic lipid associations. Curr Opin Lipidol. 2003;14(2):151–157.
   Web of Science ®Google Scholar
• Mahley RW, Innerarity TL, Rall SC Jr, Weisgraber KH. Plasma lipoproteins: apolipoprotein structure and function. J Lipid Res. 1984;25(12):1277–1294.
   PubMed Web of Science ®Google Scholar
• Kim SY, Park SM, Lee ST. Apolipoprotein C-II is a novel substrate for matrix metalloproteinases. Biochem Biophys Res Commun. 2006;339(1):47–54.
   PubMed Web of Science ®Google Scholar
• Beisiegel U, Weber W, Ihrke G, Herz J, Stanley KK. The LDL-receptor-related protein, LRP, is an apolipoprotein E-binding protein. Nature. 1989;341(6238):162–164.
   PubMed Web of Science ®Google Scholar
• Aoki T, Sato D, Li Y, Takino T, Miyamori H, Sato H. Cleavage of apolipoprotein E by membrane-type matrix metalloproteinase-1 abrogates suppression of cell proliferation. J Biochem. 2005;137(1):95–99.
   Web of Science ®Google Scholar
• Wang X, Berry E, Hernandez-Anzaldo S, et al. MMP-2 inhibits PCSK9-induced degradation of the LDL receptor in Hepa1-c1c7 cells. FEBS Lett. 2015;589(4):490–496.
   Web of Science ®Google Scholar
• Horton JD, Cohen JC, Hobbs HH. PCSK9: a convertase that coordinates LDL catabolism. J Lipid Res. 2009;50 Suppl:S172–S177.
   Google Scholar
• Benjannet S, Rhainds D, Essalmani R, et al. NARC-1/PCSK9 and its natural mutants: zymogen cleavage and effects on the low density lipoprotein (LDL) receptor and LDL cholesterol. J Biol Chem. 2004;279(47):48865–48875.
   PubMed Web of Science ®Google Scholar
• Abifadel M, Varret M, Rabès JP, et al. Mutations in PCSK9 cause autosomal dominant hypercholesterolemia. Nat Genet. 2003;34(2):154–156.
   PubMed Web of Science ®Google Scholar
• Doucet A, Overall CM. Protease proteomics: revealing protease in vivo functions using systems biology approaches. Mol Aspects Med. 2008;29(5):339–358.
   PubMed Web of Science ®Google Scholar
• O’Reilly MS, Wiederschain D, Stetler-Stevenson WG, Folkman J, Moses MA. Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance. J Biol Chem. 1999;274(41):29568–29571.
   PubMed Web of Science ®Google Scholar
• Martignetti JA, Aqeel AA, Sewairi WA, et al. Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome. Nat Genet. 2001;28(3):261–265.
   PubMed Web of Science ®Google Scholar
• Mosig RA, Dowling O, DiFeo A, et al. Loss of MMP-2 disrupts skeletal and craniofacial development and results in decreased bone mineralization, joint erosion and defects in osteoblast and osteoclast growth. Hum Mol Genet. 2007;16(9):1113–1123.
   PubMed Web of Science ®Google Scholar
• Tuysuz B, Mosig R, Altun G, Sancak S, Glucksman MJ, Martignetti JA. A novel matrix metalloproteinase 2 (MMP2) terminal hemopexin domain mutation in a family with multicentric osteolysis with nodulosis and arthritis with cardiac defects. Eur J Hum Genet. 2009;17(5):565–572.
   Web of Science ®Google Scholar
• Greenlee KJ, Werb Z, Kheradmand F. Matrix metalloproteinases in lung: multiple, multifarious, and multifaceted. Physiol Rev. 2007;87(1):69–98.
   PubMed Web of Science ®Google Scholar
• Corry DB, Rishi K, Kanellis J, et al. Decreased allergic lung inflammatory cell egression and increased susceptibility to asphyxiation in MMP2-deficiency. Nat Immunol. 2002;3(4):347–353.
   Web of Science ®Google Scholar
• Corry DB, Kiss A, Song LZ, et al. Overlapping and independent contributions of MMP2 and MMP9 to lung allergic inflammatory cell egression through decreased CC chemokines. FASEB J. 2004;18(9):995–997.
   PubMed Web of Science ®Google Scholar
• Mosig RA, Martignetti JA. Loss of MMP-2 in murine osteoblasts upregulates osteopontin and bone sialoprotein expression in a circuit regulating bone homeostasis. Dis Model Mech. 2013;6(2):397–403.
   Web of Science ®Google Scholar
• Berry E, Hernandez-Anzaldo S, Ghomashchi F, et al. Matrix metalloproteinase-2 negatively regulates cardiac secreted phospholipase A2 to modulate inflammation and fever. J Am Heart Assoc. 2015;4(4):e001868.
   Web of Science ®Google Scholar
• Lambeau G, Gelb MH. Biochemistry and physiology of mammalian secreted phospholipases A2. Annu Rev Biochem. 2008;77:495–520.
   PubMed Web of Science ®Google Scholar
• Ou J, Tu H, Shan B, et al. Unsaturated fatty acids inhibit transcription of the sterol regulatory element-binding protein-1c (SREBP-1c) gene by antagonizing ligand-dependent activation of the LXR. Proc Natl Acad Sci U S A. 2001;98(11):6027–6032.
   PubMed Web of Science ®Google Scholar
• Hartl D, Krauss-Etschmann S, Koller B, et al. Infiltrated neutrophils acquire novel chemokine receptor expression and chemokine responsiveness in chronic inflammatory lung diseases. J Immunol. 2008;181(11):8053–8067.
   Web of Science ®Google Scholar
• Monden Y, Kubota T, Inoue T, et al. Tumor necrosis factor-alpha is toxic via receptor 1 and protective via receptor 2 in a murine model of myocardial infarction. Am J Physiol Heart Circ Physiol. 2007;293(1):H743–H753.
   Web of Science ®Google Scholar
• Matsumura S, Iwanaga S, Mochizuki S, Okamoto H, Ogawa S, Okada Y. Targeted deletion or pharmacological inhibition of MMP-2 prevents cardiac rupture after myocardial infarction in mice. J Clin Invest. 2005;115(3):599–609.
   Web of Science ®Google Scholar
• Hayashidani S, Tsutsui H, Ikeuchi M, et al. Targeted deletion of MMP-2 attenuates early LV rupture and late remodeling after experimental myocardial infarction. Am J Physiol Heart Circ Physiol. 2003;285(3):H1229–H1235.
   PubMed Web of Science ®Google Scholar
• Lijnen HR, Collen D. Matrix metalloproteinase system deficiencies and matrix degradation. Thromb Haemost. 1999;82(2):837–845.
   Web of Science ®Google Scholar
• Pinto YM, Heymans S. Letter by Pinto and Heymans regarding article, “Ablation of matrix metalloproteinase-9 increases severity of viral myocarditis in mice”. Circulation. 2008;118(20):e697.
   Web of Science ®Google Scholar
• Cheung C, Marchant D, Walker EK, et al. Ablation of matrix metalloproteinase-9 increases severity of viral myocarditis in mice. Circulation. 2008;117(12):1574–1582.
   PubMed Web of Science ®Google Scholar
• Westermann D, Savvatis K, Lindner D, et al. Reduced degradation of the chemokine MCP-3 by matrix metalloproteinase-2 exacerbates myocardial inflammation in experimental viral cardiomyopathy. Circulation. 2011;124(19):2082–2093.
   PubMed Web of Science ®Google Scholar
• Dennis EA, Cao J, Hsu YH, Magrioti V, Kokotos G. Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention. Chem Rev. 2011;111(10):6130–6185.
   PubMed Web of Science ®Google Scholar
• Murakami M, Sato H, Miki Y, Yamamoto K, Taketomi Y. A new era of secreted phospholipase A2. J Lipid Res. 2015;56(7):1248–1261.
   Web of Science ®Google Scholar
• Seftor RE, Seftor EA, De Larco JE, et al. Chemically modified tetracyclines inhibit human melanoma cell invasion and metastasis. Clin Exp Metastasis. 1998;16(3):217–225.
   Web of Science ®Google Scholar
• Greenwald RA, Moak SA, Ramamurthy NS, Golub LM. Tetracyclines suppress matrix metalloproteinase activity in adjuvant arthritis and in combination with flurbiprofen, ameliorate bone damage. J Rheumatol. 1992;19(6):927–938.
   PubMed Web of Science ®Google Scholar
• Golub LM, McNamara TF, D’Angelo G, Greenwald RA, Ramamurthy NS. A non-antibacterial chemically-modified tetracycline inhibits mammalian collagenase activity. J Dent Res. 1987;66(8):1310–1314.
   PubMed Web of Science ®Google Scholar
• Golub LM, Wolff M, Lee HM, et al. Further evidence that tetracyclines inhibit collagenase activity in human crevicular fluid and from other mammalian sources. J Periodontal Res. 1985;20(1):12–23.
   PubMed Web of Science ®Google Scholar
• Gu Y, Lee HM, Sorsa T, et al. Non-antibacterial tetracyclines modulate mediators of periodontitis and atherosclerotic cardiovascular disease: a mechanistic link between local and systemic inflammation. Pharmacol Res. 2011;64(6):573–579.
   PubMed Web of Science ®Google Scholar
• Han KH, Hong KH, Park JH, et al. C-reactive protein promotes monocyte chemoattractant protein-1 – mediated chemotaxis through upregulating CC chemokine receptor 2 expression in human monocytes. Circulation. 2004;109(21):2566–2571.
   Web of Science ®Google Scholar
• Carnevale KA, Cathcart MK. Calcium-independent phospholipase A(2) is required for human monocyte chemotaxis to monocyte chemoattractant protein 1. J Immunol. 2001;167(6):3414–3421.
   Web of Science ®Google Scholar
• Mishra RS, Carnevale KA, Cathcart MK. iPLA2beta: front and center in human monocyte chemotaxis to MCP-1. J Exp Med. 2008;205(2):347–359.
   Web of Science ®Google Scholar
• Ii H, Hontani N, Toshida I, Oka M, Sato T, Akiba S. Group IVA phospholipase A2-associated production of MMP-9 in macrophages and formation of atherosclerotic lesions. Biol Pharm Bull. 2008;31(3):363–368.
   Web of Science ®Google Scholar
• Gorovetz M, Schwob O, Krimsky M, Yedgar S, Reich R. MMP production in human fibrosarcoma cells and their invasiveness are regulated by group IB secretory phospholipase A2 receptor-mediated activation of cytosolic phospholipase A2. Front Biosci. 2008;13:1917–1925.
   PubMed Web of Science ®Google Scholar
• Choi YA, Kim DK, Bang OS, Kang SS, Jin EJ. Secretory phospholipase A2 promotes MMP-9-mediated cell death by degrading type I collagen via the ERK pathway at an early stage of chondrogenesis. Biol Cell. 2010;102(2):107–119.
   Web of Science ®Google Scholar
• Choi YA, Lim HK, Kim JR, et al. Group IB secretory phospholipase A2 promotes matrix metalloproteinase-2-mediated cell migration via the phosphatidylinositol 3-kinase and Akt pathway. J Biol Chem. 2004;279(35):36579–36585.
   Web of Science ®Google Scholar
• Ping D, Jones PL, Boss JM. TNF regulates the in vivo occupancy of both distal and proximal regulatory regions of the MCP-1/JE gene. Immunity. 1996;4(5):455–469.
   PubMed Web of Science ®Google Scholar
• Andoh A, Takaya H, Saotome T, et al. Cytokine regulation of chemokine (IL-8, MCP-1, and RANTES) gene expression in human pancreatic periacinar myofibroblasts. Gastroenterology. 2000;119(1):211–219.
   PubMed Web of Science ®Google Scholar
• Braunwald E, Harrison DC, Chidsey CA. The heart as an endocrine organ. Am J Med. 1964;36:1–4.
   PubMed Web of Science ®Google Scholar
• Ogawa T, de Bold AJ. The heart as an endocrine organ. Endocr Connect. 2014;3(2):R31–R44.
   Web of Science ®Google Scholar
• Chakraborti S, Chowdhury A, Alam MN, et al. Vascular aneurysms: a perspective. Indian J Biochem Biophys. 2014;51(6):449–456.
   Web of Science ®Google Scholar
• Jackson CL, Raines EW, Ross R, Reidy MA. Role of endogenous platelet-derived growth factor in arterial smooth muscle cell migration after balloon catheter injury. Arterioscler Thromb. 1993;13(8):1218–1226.
   Google Scholar
• Zeng S, Zhou X, Tu Y, et al. Long-term MMP inhibition by doxycycline exerts divergent effect on ventricular extracellular matrix deposition and systolic performance in stroke-prone spontaneously hypertensive rats. Clin Exp Hypertens. 2011;33(5):316–324.
   PubMed Web of Science ®Google Scholar
• Hori Y, Kunihiro S, Sato S, et al. Doxycycline attenuates isoproterenol-induced myocardial fibrosis and matrix metalloproteinase activity in rats. Biol Pharm Bull. 2009;32(10):1678–1682.
   Web of Science ®Google Scholar
• Vinet L, Rouet-Benzineb P, Marniquet X, et al. Chronic doxycycline exposure accelerates left ventricular hypertrophy and progression to heart failure in mice after thoracic aorta constriction. Am J Physiol Heart Circ Physiol. 2008;295(1):H352–H360.
   Web of Science ®Google Scholar
• Yen H, Zhang Y, Penfold S, Rollins BJ. MCP-1-mediated chemotaxis requires activation of non-overlapping signal transduction pathways. J Leukoc Biol. 1997;61(4):529–532.
   Web of Science ®Google Scholar
• Sonoki K, Iwase M, Ohdo S, Ieiri I, Takata Y, Kitazono T. Statin inhibits the expression of secretory phospholipase A2 and subsequent monocyte chemoattractant protein-1 in human endothelial cells. J Cardiovasc Pharmacol. 2014;64(6):489–496.
   Web of Science ®Google Scholar
• Hu MM, Zhang J, Wang WY, et al. The inhibition of lipoprotein-associated phospholipase A2 exerts beneficial effects against atherosclerosis in LDLR-deficient mice. Acta Pharmacol Sin. 2011;32(10):1253–1258.
   Web of Science ®Google Scholar
• Gonçalves I, Edsfeldt A, Ko NY, et al. Evidence supporting a key role of Lp-PLA2-generated lysophosphatidylcholine in human atherosclerotic plaque inflammation. Arterioscler Thromb Vasc Biol. 2012;32(6):1505–1512.
   Web of Science ®Google Scholar
• Dean RA, Cox JH, Bellac CL, Doucet A, Starr AE, Overall CM. Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx. Blood. 2008;112(8):3455–3464.
   PubMed Web of Science ®Google Scholar
• Sommerfelt RM, Feuerherm AJ, Skuland T, Johansen B. Cytosolic phospholipase A2 modulates TLR2 signaling in synoviocytes. PLoS One. 2015;10(4):e0119088.
   Web of Science ®Google Scholar
• Kazantseva MG, Hung NA, Highton J, Hessian PA. MMP expression in rheumatoid inflammation: the rs11568818 polymorphism is associated with MMP-7 expression at an extra-articular site. Genes Immun. 2013;14(3):162–169.
   Web of Science ®Google Scholar
• McGarry T, Veale DJ, Gao W, Orr C, Fearon U, Connolly M. Toll-like receptor 2 (TLR2) induces migration and invasive mechanisms in rheumatoid arthritis. Arthritis Res Ther. 2015;17(1):153.
   Google Scholar
• Silosi I, Cojocaru M, Foia L, et al. Significance of circulating and crevicular matrix metalloproteinase-9 in rheumatoid arthritis-chronic periodontitis association. J Immunol Res. 2015;2015:218060.
   Web of Science ®Google Scholar