nach oben

Inflammation

Erschienen in:

01.06.2015

Inhibitory Effect of FXa on Secretory Group IIA Phospholipase A₂

verfasst von: Sae-Kwang Ku, Jong-Sup Bae

Erschienen in: Inflammation | Ausgabe 3/2015

Einloggen, um Zugang zu erhalten

Abstract

It is well known that the expression level of secretory group IIA phospholipase A₂ (sPLA₂-IIA) is elevated in inflammatory diseases and lipopolysaccharide (LPS) upregulates the expression of sPLA₂-IIA in human umbilical vein endothelial cells (HUVECs). Activated factor X (FXa) is an important enzyme in the coagulation cascade responsible for thrombin generation, and it influences cell signaling in various cell types by activating protease-activated receptors (PARs). Here, FX or FXa was examined for its effects on the expression and activity of sPLA₂-IIA in HUVECs and mouse. Prior treatment of cells or mouse with FXa inhibited LPS-induced expression and activity of sPLA₂-IIA via interacting with FXa receptor (effective cell protease receptor-1, EPR-1). And FXa suppressed the activation of cytosolic phospholipase A2 (cPLA2) and extracellular signal-regulated kinase (ERK) 1/2 by LPS. Therefore, these results suggest that FXa may inhibit LPS-mediated expression of sPLA₂-IIA by suppression of cPLA2 and ERK 1/2.

Furie, B., and B.C. Furie. 1988. The molecular basis of blood coagulation. Cell 53: 505–518.CrossRefPubMed

Edgington, T.S., N. Mackman, K. Brand, and W. Ruf. 1991. The structural biology of expression and function of tissue factor. Thrombosis and Haemostasis 66: 67–79.PubMed

Ahamed, J., M. Belting, and W. Ruf. 2005. Regulation of tissue factor-induced signaling by endogenous and recombinant tissue factor pathway inhibitor 1. Blood 105: 2384–2391.CrossRefPubMed

Davie, E.W., K. Fujikawa, and W. Kisiel. 1991. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 30: 10363–10370.CrossRefPubMed

Steinberg, S.F. 2005. The cardiovascular actions of protease-activated receptors. Molecular Pharmacology 67: 2–11.CrossRefPubMed

Ossovskaya, V.S., and N.W. Bunnett. 2004. Protease-activated receptors: contribution to physiology and disease. Physiological Reviews 84: 579–621.CrossRefPubMed

Six, D.A., and E.A. Dennis. 2000. The expanding superfamily of phospholipase A(2) enzymes: classification and characterization. Biochimica et Biophysica Acta 1488: 1–19.CrossRefPubMed

Kudo, I., and M. Murakami. 2002. Phospholipase A2 enzymes. Prostaglandins & Other Lipid Mediators 68–69: 3–58.CrossRef

Hara, S., I. Kudo, H.W. Chang, K. Matsuta, T. Miyamoto, and K. Inoue. 1989. Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. Journal of Biochemistry 105: 395–399.PubMed

10.

Seilhamer, J.J., W. Pruzanski, P. Vadas, et al. 1989. Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. Journal of Biological Chemistry 264: 5335–5338.PubMed

11.

Menschikowski, M., A. Hagelgans, and G. Siegert. 2006. Secretory phospholipase A2 of group IIA: is it an offensive or a defensive player during atherosclerosis and other inflammatory diseases? Prostaglandins & Other Lipid Mediators 79: 1–33.CrossRef

12.

Pruzanski, W., and P. Vadas. 1991. Phospholipase A2–a mediator between proximal and distal effectors of inflammation. Immunology Today 12: 143–146.PubMed

13.

Waydhas, C., D. Nast-Kolb, K.H. Duswald, P. Lehnert, and L. Schweiberer. 1989. Prognostic value of serum phospholipase A in the multitraumatized patient. Klinische Wochenschrift 67: 203–206.CrossRefPubMed

14.

Nakano, T., O. Ohara, H. Teraoka, and H. Arita. 1990. Glucocorticoids suppress group II phospholipase A2 production by blocking mRNA synthesis and post-transcriptional expression. Journal of Biological Chemistry 265: 12745–12748.PubMed

15.

Oka, S., and H. Arita. 1991. Inflammatory factors stimulate expression of group II phospholipase A2 in rat cultured astrocytes. Two distinct pathways of the gene expression. Journal of Biological Chemistry 266: 9956–9960.PubMed

16.

Crowl, R.M., T.J. Stoller, R.R. Conroy, and C.R. Stoner. 1991. Induction of phospholipase A2 gene expression in human hepatoma cells by mediators of the acute phase response. Journal of Biological Chemistry 266: 2647–2651.PubMed

17.

Bae, J.S., W. Lee, J.O. Nam, J.E. Kim, S.W. Kim, and I.S. Kim. 2014. Transforming growth factor beta-induced protein promotes severe vascular inflammatory responses. American Journal of Respiratory and Critical Care Medicine 189: 779–786.CrossRefPubMed

18.

Wang, H., H. Liao, M. Ochani, et al. 2004. Cholinergic agonists inhibit HMGB1 release and improve survival in experimental sepsis. Nature Medicine 10: 1216–1221.CrossRefPubMed

19.

Rittirsch, D., M.S. Huber-Lang, M.A. Flierl, and P.A. Ward. 2009. Immunodesign of experimental sepsis by cecal ligation and puncture. Nature Protocols 4: 31–36.CrossRefPubMedCentralPubMed

20.

Menschikowski, M., A. Hagelgans, B. Heyne, et al. 2005. Statins potentiate the IFN-gamma-induced upregulation of group IIA phospholipase A2 in human aortic smooth muscle cells and HepG2 hepatoma cells. Biochimica et Biophysica Acta 1733: 157–171.CrossRefPubMed

21.

Bae, J.S., and A.R. Rezaie. 2010. Thrombin and activated protein C inhibit the expression of secretory group IIA phospholipase A(2) in the TNF-alpha-activated endothelial cells by EPCR and PAR-1 dependent mechanisms. Thrombosis Research 125: e9–e15.CrossRefPubMedCentralPubMed

22.

Shimoyama, Y., R. Sakamoto, T. Akaboshi, M. Tanaka, and K. Ohtsuki. 2001. Characterization of secretory type IIA phospholipase A2 (sPLA2-IIA) as a glycyrrhizin (GL)-binding protein and the GL-induced inhibition of the CK-II-mediated stimulation of sPLA2-IIA activity in vitro. Biological and Pharmaceutical Bulletin 24: 1004–1008.CrossRefPubMed

23.

Alaoui-El-Azher, M., Y. Wu, N. Havet, A. Israel, A. Lilienbaum, and L. Touqui. 2002. Arachidonic acid differentially affects basal and lipopolysaccharide-induced sPLA(2)-IIA expression in alveolar macrophages through NF-kappaB and PPAR-gamma-dependent pathways. Molecular Pharmacology 61: 786–794.CrossRefPubMed

24.

Kuwata, H., C. Fujimoto, E. Yoda, et al. 2007. A novel role of group VIB calcium-independent phospholipase A2 (iPLA2gamma) in the inducible expression of group IIA secretory PLA2 in rat fibroblastic cells. Journal of Biological Chemistry 282: 20124–20132.CrossRefPubMed

25.

Flynn, J.T., and H. Hoff 3rd. 1995. Lipopolysaccharide induces time-dependent increases in prostaglandin H synthase-2 and cytosolic phospholipase A2 mRNA in cultured human microvessel-derived endothelial cells. Shock 4: 433–440.PubMed

26.

Goldblum, S.E., T.W. Brann, X. Ding, J. Pugin, and P.S. Tobias. 1994. Lipopolysaccharide (LPS)-binding protein and soluble CD14 function as accessory molecules for LPS-induced changes in endothelial barrier function, in vitro. Journal of Clinical Investigation 93: 692–702.CrossRefPubMedCentralPubMed

27.

Russell, J.A. 2006. Management of sepsis. New England Journal of Medicine 355: 1699–1713.CrossRefPubMed

28.

Baluk, P., L.C. Yao, J. Feng, et al. 2009. TNF-alpha drives remodeling of blood vessels and lymphatics in sustained airway inflammation in mice. Journal of Clinical Investigation 119: 2954–2964.PubMedCentralPubMed

29.

Mehta, D., and A.B... Malik. 2006. Signaling mechanisms regulating endothelial permeability. Physiological Reviews 86: 279–367.

30.

Buras, J.A., B. Holzmann, and M. Sitkovsky. 2005. Animal models of sepsis: setting the stage. Nature Reviews Drug Discovery 4: 854–865.CrossRefPubMed

31.

Harris, S.G., J. Padilla, L. Koumas, D. Ray, and R.P. Phipps. 2002. Prostaglandins as modulators of immunity. Trends in Immunology 23: 144–150.CrossRefPubMed

32.

Natarajan, G., M. Glibetic, V. Raykova, J.P. Ofenstein, R.L. Thomas, and J.V. Aranda. 2007. Nitric oxide and prostaglandin response to group B streptococcal infection in the lung. Annals of Clinical and Laboratory Science 37: 170–176.PubMed

33.

Agard, M., S. Asakrah, and L.A. Morici. 2013. PGE(2) suppression of innate immunity during mucosal bacterial infection. Front Cell Infect Microbiol 3: 45.CrossRefPubMedCentralPubMed

34.

Leslie, C.C. 1997. Properties and regulation of cytosolic phospholipase A2. Journal of Biological Chemistry 272: 16709–16712.CrossRefPubMed

35.

Clark, J.D., A.R. Schievella, E.A. Nalefski, and L.L. Lin. 1995. Cytosolic phospholipase A2. Journal of Lipid Mediators and Cell Signalling 12: 83–117.CrossRefPubMed

36.

Sano, H., X. Zhu, A. Sano, et al. 2001. Extracellular signal-regulated kinase 1/2-mediated phosphorylation of cytosolic phospholipase A2 is essential for human eosinophil adhesion to fibronectin. Journal of Immunology 166: 3515–3521.CrossRef

37.

Bosetti, F., and G.R. Weerasinghe. 2003. The expression of brain cyclooxygenase-2 is down-regulated in the cytosolic phospholipase A2 knockout mouse. Journal of Neurochemistry 87: 1471–1477.CrossRefPubMed

38.

Johann, S., E. Kampmann, B. Denecke, et al. 2008. Expression of enzymes involved in the prostanoid metabolism by cortical astrocytes after LPS-induced inflammation. Journal of Molecular Neuroscience 34: 177–185.CrossRefPubMed

39.

Balsinde, J., M.A. Balboa, P.A. Insel, and E.A. Dennis. 1999. Regulation and inhibition of phospholipase A2. Annual Review of Pharmacology and Toxicology 39: 175–189.CrossRefPubMed

40.

Bradley, J.D., A.A. Dmitrienko, A.J. Kivitz, et al. 2005. A randomized, double-blinded, placebo-controlled clinical trial of LY333013, a selective inhibitor of group II secretory phospholipase A2, in the treatment of rheumatoid arthritis. Journal of Rheumatology 32: 417–423.PubMed

41.

Tanaka, K., T. Kato, K. Matsumoto, and T. Yoshida. 1993. Antiinflammatory action of thielocin A1 beta, a group II phospholipase A2 specific inhibitor, in rat carrageenan-induced pleurisy. Inflammation 17: 107–119.CrossRefPubMed

42.

Vadas, P., W. Pruzanski, J. Kim, and V. Fornasier. 1989. The proinflammatory effect of intra-articular injection of soluble human and venom phospholipase A2. American Journal of Pathology 134: 807–811.PubMedCentralPubMed

43.

Zeiher, B.G., J. Steingrub, P.F. Laterre, A. Dmitrienko, Y. Fukiishi, and E. Abraham. 2005. LY315920NA/S-5920, a selective inhibitor of group IIA secretory phospholipase A2, fails to improve clinical outcome for patients with severe sepsis. Critical Care Medicine 33: 1741–1748.CrossRefPubMed

44.

Grass, D.S., R.H. Felkner, M.Y. Chiang, et al. 1996. Expression of human group II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate. Journal of Clinical Investigation 97: 2233–2241.CrossRefPubMedCentralPubMed

45.

Beck, G., B.A. Yard, J. Schulte, et al. 2003. Secreted phospholipases A2 induce the expression of chemokines in microvascular endothelium. Biochemical and Biophysical Research Communications 300: 731–737.CrossRefPubMed

Titel: Inhibitory Effect of FXa on Secretory Group IIA Phospholipase A2
verfasst von: Sae-Kwang Ku
Jong-Sup Bae
Publikationsdatum: 01.06.2015
Verlag: Springer US
Erschienen in: Inflammation / Ausgabe 3/2015
Print ISSN: 0360-3997
Elektronische ISSN: 1573-2576
DOI: https://doi.org/10.1007/s10753-014-0062-4

Leitlinien kompakt für die Innere Medizin

Mit medbee Pocketcards sicher entscheiden.

^{Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag}

Kostenlos registrieren

Neu im Fachgebiet Innere Medizin

23.04.2024 | Ablationstherapie | Nachrichten

Update Innere Medizin

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.

Newsletter bestellen

Live-Webinar: Aktuelle Leitlinien bei Herz-Kreislauf-Erkrankungen

Springer Medizin

Inhibitory Effect of FXa on Secretory Group IIA Phospholipase A₂

Abstract

Leitlinien kompakt für die Innere Medizin

Neu im Fachgebiet Innere Medizin

Wie erfolgreich ist eine Re-Ablation nach Rezidiv?

Europäische Ernährungsgewohnheiten: Das sind die häufigsten Fehler

Hinter dieser Appendizitis steckte ein Erreger

Demenzkranke durch Antipsychotika vielfach gefährdet

Update Innere Medizin

Live-Webinar: Aktuelle Leitlinien bei Herz-Kreislauf-Erkrankungen

Springer Medizin

Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 3/2015

NOD1 and NOD2 Interact with the Phagosome Cargo in Mast Cells: A Detailed Morphological Evidence

Erratum to: Potential Effects of Calcium Binding Protein S100A12 on Severity Evaluation and Curative Effect of Severe Acute Pancreatitis

Preventive Effects of Protocatechuic Acid on LPS-Induced Inflammatory Response in Human Gingival Fibroblasts via Activating PPAR-γ

Overexpression and Potential Regulatory Role of IL-17F in Pathogenesis of Chronic Periodontitis

Inhibitory Effects of JEUD-38, a New Sesquiterpene Lactone from Inula japonica Thunb, on LPS-Induced iNOS Expression in RAW264.7 Cells

Artesunate Ameliorates Functional Limitations in Freund’s Complete Adjuvant-Induced Monoarthritis in Rat by Maintaining Oxidative Homeostasis and Inhibiting COX-2 Expression

Leitlinien kompakt für die Innere Medizin

Neu im Fachgebiet Innere Medizin

Wie erfolgreich ist eine Re-Ablation nach Rezidiv?

Europäische Ernährungsgewohnheiten: Das sind die häufigsten Fehler

Hinter dieser Appendizitis steckte ein Erreger

Demenzkranke durch Antipsychotika vielfach gefährdet

Update Innere Medizin