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Volumn 6, Issue 1, 2013, Pages

Neutrophil roles in left ventricular remodeling following myocardial infarction

Author keywords

Degranulation; Inflammation; Innate immunity; Matrix metalloproteinases; Myocardial infarction; PMNs

Indexed keywords

ALPHA DEFENSIN; AZUROCIDIN; CATHELICIDIN; CATHEPSIN G; GELATINASE B; LACTOFERRIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 25; MYELOPEROXIDASE; NEUTROPHIL COLLAGENASE; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; REACTIVE OXYGEN METABOLITE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 84878353026     PISSN: None     EISSN: 17551536     Source Type: Journal    
DOI: 10.1186/1755-1536-6-11     Document Type: Review
Times cited : (148)

References (107)
  • 1
    • 84862307996 scopus 로고    scopus 로고
    • Regulation of neutrophil trafficking from the bone marrow
    • 10.1007/s00018-011-0870-8, 22045556
    • Day RB, Link DC. Regulation of neutrophil trafficking from the bone marrow. Cell Mol Life Sci 2012, 69:1415-1423. 10.1007/s00018-011-0870-8, 22045556.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1415-1423
    • Day, R.B.1    Link, D.C.2
  • 2
    • 84864945934 scopus 로고    scopus 로고
    • Relation of neutrophil/lymphocyte ratio to coronary flow to in-hospital major adverse cardiac events in patients with ST-elevated myocardial infarction undergoing primary coronary intervention
    • 10.1016/j.amjcard.2012.04.041, 22608360
    • Akpek M, Kaya MG, Lam YY, Sahin O, Elcik D, Celik T, Ergin A, Gibson CM. Relation of neutrophil/lymphocyte ratio to coronary flow to in-hospital major adverse cardiac events in patients with ST-elevated myocardial infarction undergoing primary coronary intervention. Am J Cardiol 2012, 110:621-627. 10.1016/j.amjcard.2012.04.041, 22608360.
    • (2012) Am J Cardiol , vol.110 , pp. 621-627
    • Akpek, M.1    Kaya, M.G.2    Lam, Y.Y.3    Sahin, O.4    Elcik, D.5    Celik, T.6    Ergin, A.7    Gibson, C.M.8
  • 4
    • 58749115760 scopus 로고    scopus 로고
    • Association of leukocyte and neutrophil counts with infarct size, left ventricular function and outcomes after percutaneous coronary intervention for ST-elevation myocardial infarction
    • 10.1016/j.amjcard.2008.09.085, 19166685
    • Chia S, Nagurney JT, Brown DF, Raffel OC, Bamberg F, Senatore F, Wackers FJ, Jang IK. Association of leukocyte and neutrophil counts with infarct size, left ventricular function and outcomes after percutaneous coronary intervention for ST-elevation myocardial infarction. Am J Cardiol 2009, 103:333-337. 10.1016/j.amjcard.2008.09.085, 19166685.
    • (2009) Am J Cardiol , vol.103 , pp. 333-337
    • Chia, S.1    Nagurney, J.T.2    Brown, D.F.3    Raffel, O.C.4    Bamberg, F.5    Senatore, F.6    Wackers, F.J.7    Jang, I.K.8
  • 5
    • 0022519328 scopus 로고
    • Reduction of myocardial infarct size by neutrophil depletion: effect of duration of occlusion
    • 10.1016/0002-8703(86)90461-8, 3766367
    • Jolly SR, Kane WJ, Hook BG, Abrams GD, Kunkel SL, Lucchesi BR. Reduction of myocardial infarct size by neutrophil depletion: effect of duration of occlusion. Am Heart J 1986, 112:682-690. 10.1016/0002-8703(86)90461-8, 3766367.
    • (1986) Am Heart J , vol.112 , pp. 682-690
    • Jolly, S.R.1    Kane, W.J.2    Hook, B.G.3    Abrams, G.D.4    Kunkel, S.L.5    Lucchesi, B.R.6
  • 6
    • 0020583038 scopus 로고
    • Reduction of the extent of ischemic myocardial injury by neutrophil depletion in the dog
    • 10.1161/01.CIR.67.5.1016, 6831665
    • Romson JL, Hook BG, Kunkel SL, Abrams GD, Schork MA, Lucchesi BR. Reduction of the extent of ischemic myocardial injury by neutrophil depletion in the dog. Circulation 1983, 67:1016-1023. 10.1161/01.CIR.67.5.1016, 6831665.
    • (1983) Circulation , vol.67 , pp. 1016-1023
    • Romson, J.L.1    Hook, B.G.2    Kunkel, S.L.3    Abrams, G.D.4    Schork, M.A.5    Lucchesi, B.R.6
  • 7
    • 0020612909 scopus 로고
    • Dose-dependent effects of short-term methylprednisolone on myocardial infarct extent, scar formation, and ventricular function
    • 10.1161/01.CIR.68.2.446, 6861321
    • Hammerman H, Kloner RA, Hale S, Schoen FJ, Braunwald E. Dose-dependent effects of short-term methylprednisolone on myocardial infarct extent, scar formation, and ventricular function. Circulation 1983, 68:446-452. 10.1161/01.CIR.68.2.446, 6861321.
    • (1983) Circulation , vol.68 , pp. 446-452
    • Hammerman, H.1    Kloner, R.A.2    Hale, S.3    Schoen, F.J.4    Braunwald, E.5
  • 8
    • 16844363111 scopus 로고    scopus 로고
    • Neutrophils and keratinocytes in innate immunity-cooperative actions to provide antimicrobial defense at the right time and place
    • Borregaard N, Theilgaard-Monch K, Cowland JB, Stahle M, Sorensen OE. Neutrophils and keratinocytes in innate immunity-cooperative actions to provide antimicrobial defense at the right time and place. J Leukoc Biol 2005, 77:439-443.
    • (2005) J Leukoc Biol , vol.77 , pp. 439-443
    • Borregaard, N.1    Theilgaard-Monch, K.2    Cowland, J.B.3    Stahle, M.4    Sorensen, O.E.5
  • 9
    • 84858661677 scopus 로고    scopus 로고
    • Regulation of neutrophil function by adenosine
    • 10.1161/ATVBAHA.111.226845, 3353547, 22423037
    • Barletta KE, Ley K, Mehrad B. Regulation of neutrophil function by adenosine. Arterioscler Thromb Vasc Biol 2012, 32:856-864. 10.1161/ATVBAHA.111.226845, 3353547, 22423037.
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , pp. 856-864
    • Barletta, K.E.1    Ley, K.2    Mehrad, B.3
  • 10
    • 84859387081 scopus 로고    scopus 로고
    • Neutrophil function: from mechanisms to disease
    • 10.1146/annurev-immunol-020711-074942, 22224774
    • Amulic B, Cazalet C, Hayes GL, Metzler KD, Zychlinsky A. Neutrophil function: from mechanisms to disease. Annu Rev Immunol 2012, 30:459-489. 10.1146/annurev-immunol-020711-074942, 22224774.
    • (2012) Annu Rev Immunol , vol.30 , pp. 459-489
    • Amulic, B.1    Cazalet, C.2    Hayes, G.L.3    Metzler, K.D.4    Zychlinsky, A.5
  • 12
    • 80054899779 scopus 로고    scopus 로고
    • Phenotypic and functional plasticity of cells of innate immunity: macrophages, mast cells and neutrophils
    • 10.1038/ni.2109, 3412172, 22012443
    • Galli SJ, Borregaard N, Wynn TA. Phenotypic and functional plasticity of cells of innate immunity: macrophages, mast cells and neutrophils. Nat Immunol 2011, 12:1035-1044. 10.1038/ni.2109, 3412172, 22012443.
    • (2011) Nat Immunol , vol.12 , pp. 1035-1044
    • Galli, S.J.1    Borregaard, N.2    Wynn, T.A.3
  • 14
    • 0026795415 scopus 로고
    • Modulation of granulocyte survival and programmed cell death by cytokines and bacterial products
    • Colotta F, Re F, Polentarutti N, Sozzani S, Mantovani A. Modulation of granulocyte survival and programmed cell death by cytokines and bacterial products. Blood 1992, 80:2012-2020.
    • (1992) Blood , vol.80 , pp. 2012-2020
    • Colotta, F.1    Re, F.2    Polentarutti, N.3    Sozzani, S.4    Mantovani, A.5
  • 15
    • 78649375771 scopus 로고    scopus 로고
    • Neutrophils, from marrow to microbes
    • 10.1016/j.immuni.2010.11.011, 21094463
    • Borregaard N. Neutrophils, from marrow to microbes. Immunity 2010, 33:657-670. 10.1016/j.immuni.2010.11.011, 21094463.
    • (2010) Immunity , vol.33 , pp. 657-670
    • Borregaard, N.1
  • 16
    • 0021838332 scopus 로고
    • Normal human granulopoiesis revisited. II. Bone marrow data
    • Mary JY. Normal human granulopoiesis revisited. II. Bone marrow data. Biomed Pharmacother 1985, 39:66-77.
    • (1985) Biomed Pharmacother , vol.39 , pp. 66-77
    • Mary, J.Y.1
  • 17
    • 0036800086 scopus 로고    scopus 로고
    • G-CSF is an essential regulator of neutrophil trafficking from the bone marrow to the blood
    • 10.1016/S1074-7613(02)00424-7, 12387736
    • Semerad CL, Liu F, Gregory AD, Stumpf K, Link DC. G-CSF is an essential regulator of neutrophil trafficking from the bone marrow to the blood. Immunity 2002, 17:413-423. 10.1016/S1074-7613(02)00424-7, 12387736.
    • (2002) Immunity , vol.17 , pp. 413-423
    • Semerad, C.L.1    Liu, F.2    Gregory, A.D.3    Stumpf, K.4    Link, D.C.5
  • 18
    • 0029070807 scopus 로고
    • Neutrophil chemoattractants generated in two phases during reperfusion of ischemic myocardium in the rabbit. Evidence for a role for C5a and interleukin-8
    • 10.1172/JCI117974, 295955, 7769111
    • Ivey CL, Williams FM, Collins PD, Jose PJ, Williams TJ. Neutrophil chemoattractants generated in two phases during reperfusion of ischemic myocardium in the rabbit. Evidence for a role for C5a and interleukin-8. J Clin Invest 1995, 95:2720-2728. 10.1172/JCI117974, 295955, 7769111.
    • (1995) J Clin Invest , vol.95 , pp. 2720-2728
    • Ivey, C.L.1    Williams, F.M.2    Collins, P.D.3    Jose, P.J.4    Williams, T.J.5
  • 19
    • 84863917989 scopus 로고    scopus 로고
    • Neutrophil chemotaxis within a competing gradient of chemoattractants
    • 10.1021/ac3009548, 22816782
    • Kim D, Haynes CL. Neutrophil chemotaxis within a competing gradient of chemoattractants. Anal Chem 2012, 84:6070-6078. 10.1021/ac3009548, 22816782.
    • (2012) Anal Chem , vol.84 , pp. 6070-6078
    • Kim, D.1    Haynes, C.L.2
  • 20
    • 84855371090 scopus 로고    scopus 로고
    • Regulation of the inflammatory response in cardiac repair
    • 10.1161/CIRCRESAHA.111.243162, 22223212
    • Frangogiannis NG. Regulation of the inflammatory response in cardiac repair. Circ Res 2012, 110:159-173. 10.1161/CIRCRESAHA.111.243162, 22223212.
    • (2012) Circ Res , vol.110 , pp. 159-173
    • Frangogiannis, N.G.1
  • 21
    • 79960923112 scopus 로고    scopus 로고
    • Neutrophil clearance: when the party is over, clean-up begins
    • 10.1016/j.it.2011.04.009, 3151332, 21782511
    • Bratton DL, Henson PM. Neutrophil clearance: when the party is over, clean-up begins. Trends Immunol 2011, 32:350-357. 10.1016/j.it.2011.04.009, 3151332, 21782511.
    • (2011) Trends Immunol , vol.32 , pp. 350-357
    • Bratton, D.L.1    Henson, P.M.2
  • 22
    • 0141705297 scopus 로고    scopus 로고
    • Toll-like receptors stimulate human neutrophil function
    • 10.1182/blood-2003-04-1078, 12829592
    • Hayashi F, Means TK, Luster AD. Toll-like receptors stimulate human neutrophil function. Blood 2003, 102:2660-2669. 10.1182/blood-2003-04-1078, 12829592.
    • (2003) Blood , vol.102 , pp. 2660-2669
    • Hayashi, F.1    Means, T.K.2    Luster, A.D.3
  • 23
    • 77952311527 scopus 로고    scopus 로고
    • Calcineurin regulates innate antifungal immunity in neutrophils
    • 10.1084/jem.20092531, 2867274, 20421389
    • Greenblatt MB, Aliprantis A, Hu B, Glimcher LH. Calcineurin regulates innate antifungal immunity in neutrophils. J Exp Med 2010, 207:923-931. 10.1084/jem.20092531, 2867274, 20421389.
    • (2010) J Exp Med , vol.207 , pp. 923-931
    • Greenblatt, M.B.1    Aliprantis, A.2    Hu, B.3    Glimcher, L.H.4
  • 25
    • 76249120134 scopus 로고    scopus 로고
    • Recognition of peptidoglycan from the microbiota by Nod1 enhances systemic innate immunity
    • 10.1038/nm.2087, 20081863
    • Clarke TB, Davis KM, Lysenko ES, Zhou AY, Yu Y, Weiser JN. Recognition of peptidoglycan from the microbiota by Nod1 enhances systemic innate immunity. Nat Med 2010, 16:228-231. 10.1038/nm.2087, 20081863.
    • (2010) Nat Med , vol.16 , pp. 228-231
    • Clarke, T.B.1    Davis, K.M.2    Lysenko, E.S.3    Zhou, A.Y.4    Yu, Y.5    Weiser, J.N.6
  • 28
    • 80051665585 scopus 로고    scopus 로고
    • The role of TLRs in neutrophil activation
    • 10.1016/j.coph.2011.06.007, 21741310
    • Prince LR, Whyte MK, Sabroe I, Parker LC. The role of TLRs in neutrophil activation. Curr Opin Pharmacol 2011, 11:397-403. 10.1016/j.coph.2011.06.007, 21741310.
    • (2011) Curr Opin Pharmacol , vol.11 , pp. 397-403
    • Prince, L.R.1    Whyte, M.K.2    Sabroe, I.3    Parker, L.C.4
  • 29
    • 84863752575 scopus 로고    scopus 로고
    • Toll-like receptor (TLR) 2 and TLR4 differentially regulate doxorubicin induced cardiomyopathy in mice
    • 10.1371/journal.pone.0040763, 3396603, 22808256
    • Ma Y, Zhang X, Bao H, Mi S, Cai W, Yan H, Wang Q, Wang Z, Yan J, Fan G, et al. Toll-like receptor (TLR) 2 and TLR4 differentially regulate doxorubicin induced cardiomyopathy in mice. PLoS One 2012, 7:e40763. 10.1371/journal.pone.0040763, 3396603, 22808256.
    • (2012) PLoS One , vol.7
    • Ma, Y.1    Zhang, X.2    Bao, H.3    Mi, S.4    Cai, W.5    Yan, H.6    Wang, Q.7    Wang, Z.8    Yan, J.9    Fan, G.10
  • 31
    • 53549133371 scopus 로고    scopus 로고
    • Neutrophil mobilization and clearance in the bone marrow
    • 10.1111/j.1365-2567.2008.02950.x, 2669132, 19128361
    • Furze RC, Rankin SM. Neutrophil mobilization and clearance in the bone marrow. Immunology 2008, 125:281-288. 10.1111/j.1365-2567.2008.02950.x, 2669132, 19128361.
    • (2008) Immunology , vol.125 , pp. 281-288
    • Furze, R.C.1    Rankin, S.M.2
  • 32
    • 77952865796 scopus 로고    scopus 로고
    • Phagocyte partnership during the onset and resolution of inflammation
    • 10.1038/nri2779, 20498669
    • Soehnlein O, Lindbom L. Phagocyte partnership during the onset and resolution of inflammation. Nat Rev Immunol 2010, 10:427-439. 10.1038/nri2779, 20498669.
    • (2010) Nat Rev Immunol , vol.10 , pp. 427-439
    • Soehnlein, O.1    Lindbom, L.2
  • 33
    • 73949115341 scopus 로고    scopus 로고
    • Phagocytosis of apoptotic cells by neutrophil granulocytes: diminished proinflammatory neutrophil functions in the presence of apoptotic cells
    • 10.4049/jimmunol.0900564, 19949068
    • Esmann L, Idel C, Sarkar A, Hellberg L, Behnen M, Moller S, van Zandbergen G, Klinger M, Kohl J, Bussmeyer U, et al. Phagocytosis of apoptotic cells by neutrophil granulocytes: diminished proinflammatory neutrophil functions in the presence of apoptotic cells. J Immunol 2010, 184:391-400. 10.4049/jimmunol.0900564, 19949068.
    • (2010) J Immunol , vol.184 , pp. 391-400
    • Esmann, L.1    Idel, C.2    Sarkar, A.3    Hellberg, L.4    Behnen, M.5    Moller, S.6    van Zandbergen, G.7    Klinger, M.8    Kohl, J.9    Bussmeyer, U.10
  • 37
    • 34250876364 scopus 로고    scopus 로고
    • Inhibition of NADPH oxidase reduces myocardial oxidative stress and apoptosis and improves cardiac function in heart failure after myocardial infarction
    • 10.1016/j.freeradbiomed.2007.04.021, 17603936
    • Qin F, Simeone M, Patel R. Inhibition of NADPH oxidase reduces myocardial oxidative stress and apoptosis and improves cardiac function in heart failure after myocardial infarction. Free Radic Biol Med 2007, 43:271-281. 10.1016/j.freeradbiomed.2007.04.021, 17603936.
    • (2007) Free Radic Biol Med , vol.43 , pp. 271-281
    • Qin, F.1    Simeone, M.2    Patel, R.3
  • 38
    • 71449098233 scopus 로고    scopus 로고
    • Reactive oxygen species promote angiogenesis in the infarcted rat heart
    • 10.1111/j.1365-2613.2009.00682.x, 2803253, 19758416
    • Zhao W, Zhao T, Chen Y, Ahokas RA, Sun Y. Reactive oxygen species promote angiogenesis in the infarcted rat heart. Int J Exp Pathol 2009, 90:621-629. 10.1111/j.1365-2613.2009.00682.x, 2803253, 19758416.
    • (2009) Int J Exp Pathol , vol.90 , pp. 621-629
    • Zhao, W.1    Zhao, T.2    Chen, Y.3    Ahokas, R.A.4    Sun, Y.5
  • 39
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • 10.1016/j.micinf.2003.09.008, 14613775
    • Faurschou M, Borregaard N. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect 2003, 5:1317-1327. 10.1016/j.micinf.2003.09.008, 14613775.
    • (2003) Microbes Infect , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 40
    • 70350005378 scopus 로고    scopus 로고
    • Neutrophil granule proteins tune monocytic cell function
    • 10.1016/j.it.2009.06.006, 19699683
    • Soehnlein O, Weber C, Lindbom L. Neutrophil granule proteins tune monocytic cell function. Trends Immunol 2009, 30:538-546. 10.1016/j.it.2009.06.006, 19699683.
    • (2009) Trends Immunol , vol.30 , pp. 538-546
    • Soehnlein, O.1    Weber, C.2    Lindbom, L.3
  • 44
    • 0037416219 scopus 로고    scopus 로고
    • Myeloperoxidase and plasminogen activator inhibitor 1 play a central role in ventricular remodeling after myocardial infarction
    • 10.1084/jem.20021426, 2193831, 12615902
    • Askari AT, Brennan ML, Zhou X, Drinko J, Morehead A, Thomas JD, Topol EJ, Hazen SL, Penn MS. Myeloperoxidase and plasminogen activator inhibitor 1 play a central role in ventricular remodeling after myocardial infarction. J Exp Med 2003, 197:615-624. 10.1084/jem.20021426, 2193831, 12615902.
    • (2003) J Exp Med , vol.197 , pp. 615-624
    • Askari, A.T.1    Brennan, M.L.2    Zhou, X.3    Drinko, J.4    Morehead, A.5    Thomas, J.D.6    Topol, E.J.7    Hazen, S.L.8    Penn, M.S.9
  • 45
    • 27844442307 scopus 로고    scopus 로고
    • Myeloperoxidase-generated oxidants modulate left ventricular remodeling but not infarct size after myocardial infarction
    • 10.1161/CIRCULATIONAHA.105.542340, 16267254
    • Vasilyev N, Williams T, Brennan ML, Unzek S, Zhou X, Heinecke JW, Spitz DR, Topol EJ, Hazen SL, Penn MS. Myeloperoxidase-generated oxidants modulate left ventricular remodeling but not infarct size after myocardial infarction. Circulation 2005, 112:2812-2820. 10.1161/CIRCULATIONAHA.105.542340, 16267254.
    • (2005) Circulation , vol.112 , pp. 2812-2820
    • Vasilyev, N.1    Williams, T.2    Brennan, M.L.3    Unzek, S.4    Zhou, X.5    Heinecke, J.W.6    Spitz, D.R.7    Topol, E.J.8    Hazen, S.L.9    Penn, M.S.10
  • 46
    • 19344371455 scopus 로고    scopus 로고
    • Neutrophil-mediated accumulation of 2-ClHDA during myocardial infarction: 2-ClHDA-mediated myocardial injury
    • 10.1152/ajpheart.00834.2004, 15681699
    • Thukkani AK, Martinson BD, Albert CJ, Vogler GA, Ford DA. Neutrophil-mediated accumulation of 2-ClHDA during myocardial infarction: 2-ClHDA-mediated myocardial injury. Am J Physiol Heart Circ Physiol 2005, 288:H2955-H2964. 10.1152/ajpheart.00834.2004, 15681699.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Thukkani, A.K.1    Martinson, B.D.2    Albert, C.J.3    Vogler, G.A.4    Ford, D.A.5
  • 47
    • 84859950056 scopus 로고    scopus 로고
    • NSP4, an elastase-related protease in human neutrophils with arginine specificity
    • 10.1073/pnas.1200470109, 3341072, 22474388
    • Perera NC, Schilling O, Kittel H, Back W, Kremmer E, Jenne DE. NSP4, an elastase-related protease in human neutrophils with arginine specificity. Proc Natl Acad Sci U S A 2012, 109:6229-6234. 10.1073/pnas.1200470109, 3341072, 22474388.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6229-6234
    • Perera, N.C.1    Schilling, O.2    Kittel, H.3    Back, W.4    Kremmer, E.5    Jenne, D.E.6
  • 48
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: specific regulators of inflammation
    • 10.1038/nri1841, 16799473
    • Pham CT. Neutrophil serine proteases: specific regulators of inflammation. Nat Rev Immunol 2006, 6:541-550. 10.1038/nri1841, 16799473.
    • (2006) Nat Rev Immunol , vol.6 , pp. 541-550
    • Pham, C.T.1
  • 49
    • 33644847888 scopus 로고    scopus 로고
    • Leukocyte adhesion and thrombosis
    • 10.1097/01.moh.0000190107.54790.de, 16319685
    • Afshar-Kharghan V, Thiagarajan P. Leukocyte adhesion and thrombosis. Curr Opin Hematol 2006, 13:34-39. 10.1097/01.moh.0000190107.54790.de, 16319685.
    • (2006) Curr Opin Hematol , vol.13 , pp. 34-39
    • Afshar-Kharghan, V.1    Thiagarajan, P.2
  • 50
    • 0037844877 scopus 로고    scopus 로고
    • JAK2/STAT3, not ERK1/2, mediates interleukin-6-induced activation of inducible nitric-oxide synthase and decrease in contractility of adult ventricular myocytes
    • 10.1074/jbc.M212321200, 12595539
    • Yu X, Kennedy RH, Liu SJ. JAK2/STAT3, not ERK1/2, mediates interleukin-6-induced activation of inducible nitric-oxide synthase and decrease in contractility of adult ventricular myocytes. J Biol Chem 2003, 278:16304-16309. 10.1074/jbc.M212321200, 12595539.
    • (2003) J Biol Chem , vol.278 , pp. 16304-16309
    • Yu, X.1    Kennedy, R.H.2    Liu, S.J.3
  • 51
    • 77951951482 scopus 로고    scopus 로고
    • Human neutrophil elastase-mediated cleavage sites of MMP-9 and TIMP-1: implications to cystic fibrosis proteolytic dysfunction
    • 2811559, 20111696
    • Jackson PL, Xu X, Wilson L, Weathington NM, Clancy JP, Blalock JE, Gaggar A. Human neutrophil elastase-mediated cleavage sites of MMP-9 and TIMP-1: implications to cystic fibrosis proteolytic dysfunction. Mol Med 2010, 16:159-166. 2811559, 20111696.
    • (2010) Mol Med , vol.16 , pp. 159-166
    • Jackson, P.L.1    Xu, X.2    Wilson, L.3    Weathington, N.M.4    Clancy, J.P.5    Blalock, J.E.6    Gaggar, A.7
  • 52
    • 0037423077 scopus 로고    scopus 로고
    • SSR69071, an elastase inhibitor, reduces myocardial infarct size following ischemia-reperfusion injury
    • 10.1016/S0014-2999(03)01298-6, 12568915
    • Bidouard JP, Duval N, Kapui Z, Herbert JM, O'Connor SE, Janiak P. SSR69071, an elastase inhibitor, reduces myocardial infarct size following ischemia-reperfusion injury. Eur J Pharmacol 2003, 461:49-52. 10.1016/S0014-2999(03)01298-6, 12568915.
    • (2003) Eur J Pharmacol , vol.461 , pp. 49-52
    • Bidouard, J.P.1    Duval, N.2    Kapui, Z.3    Herbert, J.M.4    O'Connor, S.E.5    Janiak, P.6
  • 53
    • 78149357432 scopus 로고    scopus 로고
    • Postischemic infusion of sivelestat sodium hydrate, a selective neutrophil elastase inhibitor, protects against myocardial stunning in swine
    • 10.1007/s00540-010-0948-8, 20464430
    • Akiyama D, Hara T, Yoshitomi O, Maekawa T, Cho S, Sumikawa K. Postischemic infusion of sivelestat sodium hydrate, a selective neutrophil elastase inhibitor, protects against myocardial stunning in swine. J Anesth 2010, 24:575-581. 10.1007/s00540-010-0948-8, 20464430.
    • (2010) J Anesth , vol.24 , pp. 575-581
    • Akiyama, D.1    Hara, T.2    Yoshitomi, O.3    Maekawa, T.4    Cho, S.5    Sumikawa, K.6
  • 54
    • 0346732028 scopus 로고    scopus 로고
    • Proteinase 3 sidesteps caspases and cleaves p21(Waf1/Cip1/Sdi1) to induce endothelial cell apoptosis
    • 10.1111/j.1523-1755.2004.00364.x, 14675038
    • Pendergraft WF, Rudolph EH, Falk RJ, Jahn JE, Grimmler M, Hengst L, Jennette JC, Preston GA. Proteinase 3 sidesteps caspases and cleaves p21(Waf1/Cip1/Sdi1) to induce endothelial cell apoptosis. Kidney Int 2004, 65:75-84. 10.1111/j.1523-1755.2004.00364.x, 14675038.
    • (2004) Kidney Int , vol.65 , pp. 75-84
    • Pendergraft, W.F.1    Rudolph, E.H.2    Falk, R.J.3    Jahn, J.E.4    Grimmler, M.5    Hengst, L.6    Jennette, J.C.7    Preston, G.A.8
  • 55
    • 0036324175 scopus 로고    scopus 로고
    • Release and degradation of angiotensin I and angiotensin II from angiotensinogen by neutrophil serine proteinases
    • 10.1006/abbi.2001.2687, 11747312
    • Ramaha A, Patston PA. Release and degradation of angiotensin I and angiotensin II from angiotensinogen by neutrophil serine proteinases. Arch Biochem Biophys 2002, 397:77-83. 10.1006/abbi.2001.2687, 11747312.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 77-83
    • Ramaha, A.1    Patston, P.A.2
  • 57
    • 0035813187 scopus 로고    scopus 로고
    • The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL
    • 10.1074/jbc.M106089200, 11486009
    • Yan L, Borregaard N, Kjeldsen L, Moses MA. The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL. J Biol Chem 2001, 276:37258-37265. 10.1074/jbc.M106089200, 11486009.
    • (2001) J Biol Chem , vol.276 , pp. 37258-37265
    • Yan, L.1    Borregaard, N.2    Kjeldsen, L.3    Moses, M.A.4
  • 58
    • 0033612221 scopus 로고    scopus 로고
    • The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin
    • 10.1006/jmbi.1999.2755, 10339412
    • Coles M, Diercks T, Muehlenweg B, Bartsch S, Zolzer V, Tschesche H, Kessler H. The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin. J Mol Biol 1999, 289:139-157. 10.1006/jmbi.1999.2755, 10339412.
    • (1999) J Mol Biol , vol.289 , pp. 139-157
    • Coles, M.1    Diercks, T.2    Muehlenweg, B.3    Bartsch, S.4    Zolzer, V.5    Tschesche, H.6    Kessler, H.7
  • 59
    • 66249141980 scopus 로고    scopus 로고
    • Increased systemic and myocardial expression of neutrophil gelatinase-associated lipocalin in clinical and experimental heart failure
    • 10.1093/eurheartj/ehp088, 19329498
    • Yndestad A, Landro L, Ueland T, Dahl CP, Flo TH, Vinge LE, Espevik T, Froland SS, Husberg C, Christensen G, et al. Increased systemic and myocardial expression of neutrophil gelatinase-associated lipocalin in clinical and experimental heart failure. Eur Heart J 2009, 30:1229-1236. 10.1093/eurheartj/ehp088, 19329498.
    • (2009) Eur Heart J , vol.30 , pp. 1229-1236
    • Yndestad, A.1    Landro, L.2    Ueland, T.3    Dahl, C.P.4    Flo, T.H.5    Vinge, L.E.6    Espevik, T.7    Froland, S.S.8    Husberg, C.9    Christensen, G.10
  • 60
    • 84863948170 scopus 로고    scopus 로고
    • Prognostic utility of neutrophil gelatinase-associated lipocalin in predicting mortality and cardiovascular events in patients with ST-segment elevation myocardial infarction treated with primary percutaneous coronary intervention
    • 10.1016/j.jacc.2012.04.017, 22813613
    • Lindberg S, Pedersen SH, Mogelvang R, Jensen JS, Flyvbjerg A, Galatius S, Magnusson NE. Prognostic utility of neutrophil gelatinase-associated lipocalin in predicting mortality and cardiovascular events in patients with ST-segment elevation myocardial infarction treated with primary percutaneous coronary intervention. J Am Coll Cardiol 2012, 60:339-345. 10.1016/j.jacc.2012.04.017, 22813613.
    • (2012) J Am Coll Cardiol , vol.60 , pp. 339-345
    • Lindberg, S.1    Pedersen, S.H.2    Mogelvang, R.3    Jensen, J.S.4    Flyvbjerg, A.5    Galatius, S.6    Magnusson, N.E.7
  • 61
    • 84855891599 scopus 로고    scopus 로고
    • Temporal and spatial expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases following myocardial infarction
    • 10.1111/j.1755-5922.2010.00207.x, 2972388, 20645986
    • Lindsey ML, Zamilpa R. Temporal and spatial expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases following myocardial infarction. Cardiovasc Ther 2012, 30:31-41. 10.1111/j.1755-5922.2010.00207.x, 2972388, 20645986.
    • (2012) Cardiovasc Ther , vol.30 , pp. 31-41
    • Lindsey, M.L.1    Zamilpa, R.2
  • 62
    • 46749103330 scopus 로고    scopus 로고
    • Matrix metalloproteinase-8 facilitates neutrophil migration through the corneal stromal matrix by collagen degradation and production of the chemotactic peptide Pro-Gly-Pro
    • 10.2353/ajpath.2008.080081, 2438292, 18556780
    • Lin M, Jackson P, Tester AM, Diaconu E, Overall CM, Blalock JE, Pearlman E. Matrix metalloproteinase-8 facilitates neutrophil migration through the corneal stromal matrix by collagen degradation and production of the chemotactic peptide Pro-Gly-Pro. Am J Pathol 2008, 173:144-153. 10.2353/ajpath.2008.080081, 2438292, 18556780.
    • (2008) Am J Pathol , vol.173 , pp. 144-153
    • Lin, M.1    Jackson, P.2    Tester, A.M.3    Diaconu, E.4    Overall, C.M.5    Blalock, J.E.6    Pearlman, E.7
  • 63
    • 77749264268 scopus 로고    scopus 로고
    • Neutrophil depletion blocks early collagen degradation in repairing cholestatic rat livers
    • 10.2353/ajpath.2010.090527, 2832148, 20110408
    • Harty MW, Muratore CS, Papa EF, Gart MS, Ramm GA, Gregory SH, Tracy TF. Neutrophil depletion blocks early collagen degradation in repairing cholestatic rat livers. Am J Pathol 2010, 176:1271-1281. 10.2353/ajpath.2010.090527, 2832148, 20110408.
    • (2010) Am J Pathol , vol.176 , pp. 1271-1281
    • Harty, M.W.1    Muratore, C.S.2    Papa, E.F.3    Gart, M.S.4    Ramm, G.A.5    Gregory, S.H.6    Tracy, T.F.7
  • 64
    • 34147150065 scopus 로고    scopus 로고
    • Characterization of the mechanisms by which gelatinase A, neutrophil collagenase, and membrane-type metalloproteinase MMP-14 recognize collagen I and enzymatically process the two alpha-chains
    • 10.1016/j.jmb.2007.02.076, 17379243
    • Gioia M, Monaco S, Fasciglione GF, Coletti A, Modesti A, Marini S, Coletta M. Characterization of the mechanisms by which gelatinase A, neutrophil collagenase, and membrane-type metalloproteinase MMP-14 recognize collagen I and enzymatically process the two alpha-chains. J Mol Biol 2007, 368:1101-1113. 10.1016/j.jmb.2007.02.076, 17379243.
    • (2007) J Mol Biol , vol.368 , pp. 1101-1113
    • Gioia, M.1    Monaco, S.2    Fasciglione, G.F.3    Coletti, A.4    Modesti, A.5    Marini, S.6    Coletta, M.7
  • 65
    • 57149094082 scopus 로고    scopus 로고
    • Increased matrix metalloproteinase-8 and -9 activity in patients with infarct rupture after myocardial infarction
    • 10.1016/j.carpath.2007.12.012, 18402833
    • van den Borne SW, Cleutjens JP, Hanemaaijer R, Creemers EE, Smits JF, Daemen MJ, Blankesteijn WM. Increased matrix metalloproteinase-8 and -9 activity in patients with infarct rupture after myocardial infarction. Cardiovasc Pathol 2009, 18:37-43. 10.1016/j.carpath.2007.12.012, 18402833.
    • (2009) Cardiovasc Pathol , vol.18 , pp. 37-43
    • van den Borne, S.W.1    Cleutjens, J.P.2    Hanemaaijer, R.3    Creemers, E.E.4    Smits, J.F.5    Daemen, M.J.6    Blankesteijn, W.M.7
  • 67
    • 6644223404 scopus 로고    scopus 로고
    • Matrix-dependent mechanism of neutrophil-mediated release and activation of matrix metalloproteinase 9 in myocardial ischemia/reperfusion
    • 10.1161/01.CIR.103.17.2181, 11331260
    • Lindsey M, Wedin K, Brown MD, Keller C, Evans AJ, Smolen J, Burns AR, Rossen RD, Michael L, Entman M. Matrix-dependent mechanism of neutrophil-mediated release and activation of matrix metalloproteinase 9 in myocardial ischemia/reperfusion. Circulation 2001, 103:2181-2187. 10.1161/01.CIR.103.17.2181, 11331260.
    • (2001) Circulation , vol.103 , pp. 2181-2187
    • Lindsey, M.1    Wedin, K.2    Brown, M.D.3    Keller, C.4    Evans, A.J.5    Smolen, J.6    Burns, A.R.7    Rossen, R.D.8    Michael, L.9    Entman, M.10
  • 68
    • 0035808207 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression in cardiac myocytes following myocardial infarction in the rabbit
    • 10.1016/S0024-3205(00)00982-6, 11205871
    • Romanic AM, Burns-Kurtis CL, Gout B, Berrebi-Bertrand I, Ohlstein EH. Matrix metalloproteinase expression in cardiac myocytes following myocardial infarction in the rabbit. Life Sci 2001, 68:799-814. 10.1016/S0024-3205(00)00982-6, 11205871.
    • (2001) Life Sci , vol.68 , pp. 799-814
    • Romanic, A.M.1    Burns-Kurtis, C.L.2    Gout, B.3    Berrebi-Bertrand, I.4    Ohlstein, E.H.5
  • 69
    • 33947316374 scopus 로고    scopus 로고
    • Plasma matrix metalloproteinase-9 and left ventricular remodelling after acute myocardial infarction in man: a prospective cohort study
    • 10.1093/eurheartj/ehm003, 2202923, 17339265
    • Kelly D, Cockerill G, Ng LL, Thompson M, Khan S, Samani NJ, Squire IB. Plasma matrix metalloproteinase-9 and left ventricular remodelling after acute myocardial infarction in man: a prospective cohort study. Eur Heart J 2007, 28:711-718. 10.1093/eurheartj/ehm003, 2202923, 17339265.
    • (2007) Eur Heart J , vol.28 , pp. 711-718
    • Kelly, D.1    Cockerill, G.2    Ng, L.L.3    Thompson, M.4    Khan, S.5    Samani, N.J.6    Squire, I.B.7
  • 70
    • 0033932709 scopus 로고    scopus 로고
    • Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction
    • 10.1172/JCI8768, 517910, 10880048
    • Ducharme A, Frantz S, Aikawa M, Rabkin E, Lindsey M, Rohde LE, Schoen FJ, Kelly RA, Werb Z, Libby P, Lee RT. Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction. J Clin Invest 2000, 106:55-62. 10.1172/JCI8768, 517910, 10880048.
    • (2000) J Clin Invest , vol.106 , pp. 55-62
    • Ducharme, A.1    Frantz, S.2    Aikawa, M.3    Rabkin, E.4    Lindsey, M.5    Rohde, L.E.6    Schoen, F.J.7    Kelly, R.A.8    Werb, Z.9    Libby, P.10    Lee, R.T.11
  • 73
    • 84867403208 scopus 로고    scopus 로고
    • Transgenic overexpression of matrix metalloproteinase-9 in macrophages attenuates the inflammatory response and improves left ventricular function post-myocardial infarction
    • 10.1016/j.yjmcc.2012.07.017, 22884843
    • Zamilpa R, Ibarra J, de Castro Bras LE, Ramirez TA, Nguyen N, Halade GV, Zhang J, Dai Q, Dayah T, Chiao YA, et al. Transgenic overexpression of matrix metalloproteinase-9 in macrophages attenuates the inflammatory response and improves left ventricular function post-myocardial infarction. J Mol Cell Cardiol 2012, 53:599-608. 10.1016/j.yjmcc.2012.07.017, 22884843.
    • (2012) J Mol Cell Cardiol , vol.53 , pp. 599-608
    • Zamilpa, R.1    Ibarra, J.2    de Castro Bras, L.E.3    Ramirez, T.A.4    Nguyen, N.5    Halade, G.V.6    Zhang, J.7    Dai, Q.8    Dayah, T.9    Chiao, Y.A.10
  • 75
    • 43049112108 scopus 로고    scopus 로고
    • Neutrophil serine proteases fine-tune the inflammatory response
    • 10.1016/j.biocel.2007.11.008, 2440796, 18180196
    • Pham CT. Neutrophil serine proteases fine-tune the inflammatory response. Int J Biochem Cell Biol 2008, 40:1317-1333. 10.1016/j.biocel.2007.11.008, 2440796, 18180196.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1317-1333
    • Pham, C.T.1
  • 76
    • 33845418941 scopus 로고    scopus 로고
    • N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
    • 10.1189/jlb.0406290, 16963625
    • Lim JK, Lu W, Hartley O, DeVico AL. N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant. J Leukoc Biol 2006, 80:1395-1404. 10.1189/jlb.0406290, 16963625.
    • (2006) J Leukoc Biol , vol.80 , pp. 1395-1404
    • Lim, J.K.1    Lu, W.2    Hartley, O.3    DeVico, A.L.4
  • 78
    • 0036493524 scopus 로고    scopus 로고
    • Secretion of heparin-binding protein from human neutrophils is determined by its localization in azurophilic granules and secretory vesicles
    • 10.1182/blood.V99.5.1785, 11861296
    • Tapper H, Karlsson A, Morgelin M, Flodgaard H, Herwald H. Secretion of heparin-binding protein from human neutrophils is determined by its localization in azurophilic granules and secretory vesicles. Blood 2002, 99:1785-1793. 10.1182/blood.V99.5.1785, 11861296.
    • (2002) Blood , vol.99 , pp. 1785-1793
    • Tapper, H.1    Karlsson, A.2    Morgelin, M.3    Flodgaard, H.4    Herwald, H.5
  • 79
    • 61449103585 scopus 로고    scopus 로고
    • Neutrophil-derived azurocidin alarms the immune system
    • Soehnlein O, Lindbom L. Neutrophil-derived azurocidin alarms the immune system. J Leukoc Biol 2009, 85:344-351.
    • (2009) J Leukoc Biol , vol.85 , pp. 344-351
    • Soehnlein, O.1    Lindbom, L.2
  • 80
    • 0030586281 scopus 로고    scopus 로고
    • Characterization of recombinant human HBP/CAP37/azurocidin, a pleiotropic mediator of inflammation-enhancing LPS-induced cytokine release from monocytes
    • 10.1016/0014-5793(96)00639-4, 8706818
    • Rasmussen PB, Bjorn S, Hastrup S, Nielsen PF, Norris K, Thim L, Wiberg FC, Flodgaard H. Characterization of recombinant human HBP/CAP37/azurocidin, a pleiotropic mediator of inflammation-enhancing LPS-induced cytokine release from monocytes. FEBS Lett 1996, 390:109-112. 10.1016/0014-5793(96)00639-4, 8706818.
    • (1996) FEBS Lett , vol.390 , pp. 109-112
    • Rasmussen, P.B.1    Bjorn, S.2    Hastrup, S.3    Nielsen, P.F.4    Norris, K.5    Thim, L.6    Wiberg, F.C.7    Flodgaard, H.8
  • 82
    • 79958143846 scopus 로고    scopus 로고
    • Neutrophil-derived azurocidin cleaves insulin-like growth factor-binding protein-1, -2 and -4
    • 10.1016/j.ghir.2011.04.003, 21550830
    • Brandt K, Lundell K, Brismar K. Neutrophil-derived azurocidin cleaves insulin-like growth factor-binding protein-1, -2 and -4. Growth Horm IGF Res 2011, 21:167-173. 10.1016/j.ghir.2011.04.003, 21550830.
    • (2011) Growth Horm IGF Res , vol.21 , pp. 167-173
    • Brandt, K.1    Lundell, K.2    Brismar, K.3
  • 83
    • 67649373005 scopus 로고    scopus 로고
    • Leukotriene B4-induced changes in vascular permeability are mediated by neutrophil release of heparin-binding protein (HBP/CAP37/azurocidin)
    • 10.1096/fj.08-121277, 19151333
    • Di Gennaro A, Kenne E, Wan M, Soehnlein O, Lindbom L, Haeggstrom JZ. Leukotriene B4-induced changes in vascular permeability are mediated by neutrophil release of heparin-binding protein (HBP/CAP37/azurocidin). FASEB J 2009, 23:1750-1757. 10.1096/fj.08-121277, 19151333.
    • (2009) FASEB J , vol.23 , pp. 1750-1757
    • Di Gennaro, A.1    Kenne, E.2    Wan, M.3    Soehnlein, O.4    Lindbom, L.5    Haeggstrom, J.Z.6
  • 84
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • 10.1146/annurev.immunol.22.012703.104603, 15032578
    • Yang D, Biragyn A, Hoover DM, Lubkowski J, Oppenheim JJ. Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu Rev Immunol 2004, 22:181-215. 10.1146/annurev.immunol.22.012703.104603, 15032578.
    • (2004) Annu Rev Immunol , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 85
    • 0033844287 scopus 로고    scopus 로고
    • Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells
    • Yang D, Chen Q, Chertov O, Oppenheim JJ. Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells. J Leukoc Biol 2000, 68:9-14.
    • (2000) J Leukoc Biol , vol.68 , pp. 9-14
    • Yang, D.1    Chen, Q.2    Chertov, O.3    Oppenheim, J.J.4
  • 86
    • 0024797674 scopus 로고
    • Monocyte-chemotactic activity of defensins from human neutrophils
    • 10.1172/JCI114394, 304087, 2592571
    • Territo MC, Ganz T, Selsted ME, Lehrer R. Monocyte-chemotactic activity of defensins from human neutrophils. J Clin Invest 1989, 84:2017-2020. 10.1172/JCI114394, 304087, 2592571.
    • (1989) J Clin Invest , vol.84 , pp. 2017-2020
    • Territo, M.C.1    Ganz, T.2    Selsted, M.E.3    Lehrer, R.4
  • 87
    • 69249158954 scopus 로고    scopus 로고
    • Human defensins activate monocyte-derived dendritic cells, promote the production of proinflammatory cytokines, and up-regulate the surface expression of CD91
    • 10.1189/jlb.0708412, 19477909
    • Presicce P, Giannelli S, Taddeo A, Villa ML, Della Bella S. Human defensins activate monocyte-derived dendritic cells, promote the production of proinflammatory cytokines, and up-regulate the surface expression of CD91. J Leukoc Biol 2009, 86:941-948. 10.1189/jlb.0708412, 19477909.
    • (2009) J Leukoc Biol , vol.86 , pp. 941-948
    • Presicce, P.1    Giannelli, S.2    Taddeo, A.3    Villa, M.L.4    Della Bella, S.5
  • 88
    • 28344447990 scopus 로고    scopus 로고
    • Multifunctional roles of lactoferrin: a critical overview
    • 10.1007/s00018-005-5369-8, 16261256
    • Ward PP, Paz E, Conneely OM. Multifunctional roles of lactoferrin: a critical overview. Cell Mol Life Sci 2005, 62:2540-2548. 10.1007/s00018-005-5369-8, 16261256.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2540-2548
    • Ward, P.P.1    Paz, E.2    Conneely, O.M.3
  • 89
    • 0026716209 scopus 로고
    • Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin
    • Crouch SP, Slater KJ, Fletcher J. Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood 1992, 80:235-240.
    • (1992) Blood , vol.80 , pp. 235-240
    • Crouch, S.P.1    Slater, K.J.2    Fletcher, J.3
  • 91
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense
    • 10.1016/j.it.2008.12.003, 2765035, 19217824
    • Lai Y, Gallo RL. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 2009, 30:131-141. 10.1016/j.it.2008.12.003, 2765035, 19217824.
    • (2009) Trends Immunol , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 92
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott MG, Davidson DJ, Gold MR, Bowdish D, Hancock RE. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J Immunol 2002, 169:3883-3891.
    • (2002) J Immunol , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.5
  • 95
    • 77955039982 scopus 로고    scopus 로고
    • MT6-MMP is present in lipid rafts and faces inward in living human PMNs but translocates to the cell surface during neutrophil apoptosis
    • 10.1093/intimm/dxq048, 2915617, 20501611
    • Fortin CF, Sohail A, Sun Q, McDonald PP, Fridman R, Fulop T. MT6-MMP is present in lipid rafts and faces inward in living human PMNs but translocates to the cell surface during neutrophil apoptosis. Int Immunol 2010, 22:637-649. 10.1093/intimm/dxq048, 2915617, 20501611.
    • (2010) Int Immunol , vol.22 , pp. 637-649
    • Fortin, C.F.1    Sohail, A.2    Sun, Q.3    McDonald, P.P.4    Fridman, R.5    Fulop, T.6
  • 96
    • 84859738660 scopus 로고    scopus 로고
    • Biochemical characterization and N-terminomics analysis of leukolysin, the membrane-type 6 matrix metalloprotease (MMP25): chemokine and vimentin cleavages enhance cell migration and macrophage phagocytic activities
    • 10.1074/jbc.M111.314179, 3339980, 22367194
    • Starr AE, Bellac CL, Dufour A, Goebeler V, Overall CM. Biochemical characterization and N-terminomics analysis of leukolysin, the membrane-type 6 matrix metalloprotease (MMP25): chemokine and vimentin cleavages enhance cell migration and macrophage phagocytic activities. J Biol Chem 2012, 287:13382-13395. 10.1074/jbc.M111.314179, 3339980, 22367194.
    • (2012) J Biol Chem , vol.287 , pp. 13382-13395
    • Starr, A.E.1    Bellac, C.L.2    Dufour, A.3    Goebeler, V.4    Overall, C.M.5
  • 97
    • 79952622190 scopus 로고    scopus 로고
    • Dying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality
    • 10.1038/cdd.2011.1, 3131909, 21293492
    • Remijsen Q, Kuijpers TW, Wirawan E, Lippens S, Vandenabeele P, Vanden Berghe T. Dying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality. Cell Death Differ 2011, 18:581-588. 10.1038/cdd.2011.1, 3131909, 21293492.
    • (2011) Cell Death Differ , vol.18 , pp. 581-588
    • Remijsen, Q.1    Kuijpers, T.W.2    Wirawan, E.3    Lippens, S.4    Vandenabeele, P.5    Vanden Berghe, T.6
  • 99
    • 84859375702 scopus 로고    scopus 로고
    • Neutrophil extracellular traps that are not degraded in systemic lupus erythematosus activate complement exacerbating the disease
    • 10.4049/jimmunol.1102404, 22345666
    • Leffler J, Martin M, Gullstrand B, Tyden H, Lood C, Truedsson L, Bengtsson AA, Blom AM. Neutrophil extracellular traps that are not degraded in systemic lupus erythematosus activate complement exacerbating the disease. J Immunol 2012, 188:3522-3531. 10.4049/jimmunol.1102404, 22345666.
    • (2012) J Immunol , vol.188 , pp. 3522-3531
    • Leffler, J.1    Martin, M.2    Gullstrand, B.3    Tyden, H.4    Lood, C.5    Truedsson, L.6    Bengtsson, A.A.7    Blom, A.M.8
  • 102
    • 4143115478 scopus 로고    scopus 로고
    • Three different neutrophil subsets exhibited in mice with different susceptibilities to infection by methicillin-resistant Staphylococcus aureus
    • 10.1016/j.immuni.2004.07.006, 15308102
    • Tsuda Y, Takahashi H, Kobayashi M, Hanafusa T, Herndon DN, Suzuki F. Three different neutrophil subsets exhibited in mice with different susceptibilities to infection by methicillin-resistant Staphylococcus aureus. Immunity 2004, 21:215-226. 10.1016/j.immuni.2004.07.006, 15308102.
    • (2004) Immunity , vol.21 , pp. 215-226
    • Tsuda, Y.1    Takahashi, H.2    Kobayashi, M.3    Hanafusa, T.4    Herndon, D.N.5    Suzuki, F.6
  • 103
    • 79960829290 scopus 로고    scopus 로고
    • Neutrophils in the activation and regulation of innate and adaptive immunity
    • 10.1038/nri3024, 21785456
    • Mantovani A, Cassatella MA, Costantini C, Jaillon S. Neutrophils in the activation and regulation of innate and adaptive immunity. Nat Rev Immunol 2011, 11:519-531. 10.1038/nri3024, 21785456.
    • (2011) Nat Rev Immunol , vol.11 , pp. 519-531
    • Mantovani, A.1    Cassatella, M.A.2    Costantini, C.3    Jaillon, S.4
  • 104
    • 69249222379 scopus 로고    scopus 로고
    • Polarization of tumor-associated neutrophil phenotype by TGF-beta: " N1" versus " N2" TAN
    • 10.1016/j.ccr.2009.06.017, 2754404, 19732719
    • Fridlender ZG, Sun J, Kim S, Kapoor V, Cheng G, Ling L, Worthen GS, Albelda SM. Polarization of tumor-associated neutrophil phenotype by TGF-beta: " N1" versus " N2" TAN. Cancer Cell 2009, 16:183-194. 10.1016/j.ccr.2009.06.017, 2754404, 19732719.
    • (2009) Cancer Cell , vol.16 , pp. 183-194
    • Fridlender, Z.G.1    Sun, J.2    Kim, S.3    Kapoor, V.4    Cheng, G.5    Ling, L.6    Worthen, G.S.7    Albelda, S.M.8
  • 105
    • 50249155297 scopus 로고    scopus 로고
    • Transforming growth factor beta inhibition increases mortality and left ventricular dilatation after myocardial infarction
    • 10.1007/s00395-008-0739-7, 18651091
    • Frantz S, Hu K, Adamek A, Wolf J, Sallam A, Maier SK, Lonning S, Ling H, Ertl G, Bauersachs J. Transforming growth factor beta inhibition increases mortality and left ventricular dilatation after myocardial infarction. Basic Res Cardiol 2008, 103:485-492. 10.1007/s00395-008-0739-7, 18651091.
    • (2008) Basic Res Cardiol , vol.103 , pp. 485-492
    • Frantz, S.1    Hu, K.2    Adamek, A.3    Wolf, J.4    Sallam, A.5    Maier, S.K.6    Lonning, S.7    Ling, H.8    Ertl, G.9    Bauersachs, J.10
  • 106
    • 84874285627 scopus 로고    scopus 로고
    • Matrix metalloproteinase-28 deletion exacerbates cardiac dysfunction and rupture after myocardial infarction in mice by inhibiting m2 macrophage activation
    • 10.1161/CIRCRESAHA.111.300502, 23261783
    • Ma Y, Halade GV, Zhang J, Ramirez TA, Levin D, Voorhees A, Jin YF, Han HC, Manicone AM, Lindsey ML. Matrix metalloproteinase-28 deletion exacerbates cardiac dysfunction and rupture after myocardial infarction in mice by inhibiting m2 macrophage activation. Circ Res 2013, 112:675-688. 10.1161/CIRCRESAHA.111.300502, 23261783.
    • (2013) Circ Res , vol.112 , pp. 675-688
    • Ma, Y.1    Halade, G.V.2    Zhang, J.3    Ramirez, T.A.4    Levin, D.5    Voorhees, A.6    Jin, Y.F.7    Han, H.C.8    Manicone, A.M.9    Lindsey, M.L.10
  • 107
    • 84878193034 scopus 로고    scopus 로고
    • Extracellular matrix and fibroblast communication following myocardial infarction
    • 10.1007/s12265-012-9398-z, 22926488
    • Ma Y, Halade GV, Lindsey ML. Extracellular matrix and fibroblast communication following myocardial infarction. J Cardiovasc Transl Res 2012, 5:848-857. 10.1007/s12265-012-9398-z, 22926488.
    • (2012) J Cardiovasc Transl Res , vol.5 , pp. 848-857
    • Ma, Y.1    Halade, G.V.2    Lindsey, M.L.3


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