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Volumn 121, Issue 19, 2013, Pages 3900-3907

SerpinB1 is critical for neutrophil survival through cell-autonomous inhibition of cathepsin G

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CATHEPSIN G; LEUCYLLEUCINE METHYL ESTER; LEUKOCYTE ELASTASE; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; SERINE PROTEINASE INHIBITOR; SERPIN B1; UNCLASSIFIED DRUG; SERPINB1A PROTEIN, MOUSE;

EID: 84880449571     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2012-09-455022     Document Type: Article
Times cited : (49)

References (50)
  • 3
    • 0030003411 scopus 로고    scopus 로고
    • Effect of recombinant granulocyte colony-stimulating factor on neutrophil kinetics in normal young and elderly humans
    • Price TH, Chatta GS, Dale DC. Effect of recombinant granulocyte colony-stimulating factor on neutrophil kinetics in normal young and elderly humans. Blood. 1996;88(1):335-340.
    • (1996) Blood , vol.88 , Issue.1 , pp. 335-340
    • Price, T.H.1    Chatta, G.S.2    Dale, D.C.3
  • 4
    • 0028954304 scopus 로고
    • Analysis of hematopoiesis in max 41 transgenic mice that exhibit sustained elevations of blood granulocytes and monocytes
    • Metcalf D, Lindeman GJ, Nicola NA. Analysis of hematopoiesis in max 41 transgenic mice that exhibit sustained elevations of blood granulocytes and monocytes. Blood. 1995;85(9):2364-2370.
    • (1995) Blood , vol.85 , Issue.9 , pp. 2364-2370
    • Metcalf, D.1    Lindeman, G.J.2    Nicola, N.A.3
  • 5
    • 82655162053 scopus 로고    scopus 로고
    • Educational paper: Defects in number and function of neutrophilic granulocytes causing primary immunodeficiency
    • van den Berg JM, Kuijpers TW. Educational paper: defects in number and function of neutrophilic granulocytes causing primary immunodeficiency. Eur J Pediatr. 2011;170(11): 1369-1376.
    • (2011) Eur J Pediatr , vol.170 , Issue.11 , pp. 1369-1376
    • Van Den Berg, J.M.1    Kuijpers, T.W.2
  • 6
    • 41449105534 scopus 로고    scopus 로고
    • Constitutive neutrophil apoptosis: Mechanisms and regulation
    • Luo HR, Loison F. Constitutive neutrophil apoptosis: mechanisms and regulation. Am J Hematol. 2008;83(4):288-295.
    • (2008) Am J Hematol , vol.83 , Issue.4 , pp. 288-295
    • Luo, H.R.1    Loison, F.2
  • 7
    • 0038171416 scopus 로고    scopus 로고
    • Neutrophil apoptosis pathways and their modifications in inflammation
    • Simon HU. Neutrophil apoptosis pathways and their modifications in inflammation. Immunol Rev. 2003;193:101-110.
    • (2003) Immunol Rev , vol.193 , pp. 101-110
    • Simon, H.U.1
  • 8
    • 34247849157 scopus 로고    scopus 로고
    • Cathepsin-cleaved bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization
    • Blomgran R, Zheng L, Stendahl O. Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization. J Leukoc Biol. 2007; 81(5):1213-1223.
    • (2007) J Leukoc Biol , vol.81 , Issue.5 , pp. 1213-1223
    • Blomgran, R.1    Zheng, L.2    Stendahl, O.3
  • 9
    • 1242316976 scopus 로고    scopus 로고
    • Calpain-1 regulates bax and subsequent smac-dependent caspase-3 activation in neutrophil apoptosis
    • Altznauer F, Conus S, Cavalli A, Folkers G, Simon HU. Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis. J Biol Chem. 2004;279(7): 5947-5957.
    • (2004) J Biol Chem , vol.279 , Issue.7 , pp. 5947-5957
    • Altznauer, F.1    Conus, S.2    Cavalli, A.3    Folkers, G.4    Simon, H.U.5
  • 10
    • 52649179807 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor delays neutrophil apoptosis by inhibition of calpains upstream of caspase-3
    • van Raam BJ, Drewniak A, Groenewold V, van den Berg TK, Kuijpers TW. Granulocyte colony-stimulating factor delays neutrophil apoptosis by inhibition of calpains upstream of caspase-3. Blood. 2008;112(5):2046-2054.
    • (2008) Blood , vol.112 , Issue.5 , pp. 2046-2054
    • Van Raam, B.J.1    Drewniak, A.2    Groenewold, V.3    Van Den Berg, T.K.4    Kuijpers, T.W.5
  • 11
    • 41149098534 scopus 로고    scopus 로고
    • Caspase-8 is activated by cathepsin d initiating neutrophil apoptosis during the resolution of inflammation
    • Conus S, Perozzo R, Reinheckel T, et al. Caspase-8 is activated by cathepsin D initiating neutrophil apoptosis during the resolution of inflammation. J Exp Med. 2008;205(3):685-698.
    • (2008) J Exp Med , vol.205 , Issue.3 , pp. 685-698
    • Conus, S.1    Perozzo, R.2    Reinheckel, T.3
  • 12
    • 78649375771 scopus 로고    scopus 로고
    • Neutrophils, from marrow to microbes
    • Borregaard N. Neutrophils, from marrow to microbes. Immunity. 2010;33(5):657-670.
    • (2010) Immunity , vol.33 , Issue.5 , pp. 657-670
    • Borregaard, N.1
  • 13
    • 78650096176 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3, and cathepsin g as therapeutic targets in human diseases
    • Korkmaz B, Horwitz MS, Jenne DE, Gauthier F. Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacol Rev. 2010;62(4):726-759.
    • (2010) Pharmacol Rev , vol.62 , Issue.4 , pp. 726-759
    • Korkmaz, B.1    Horwitz, M.S.2    Jenne, D.E.3    Gauthier, F.4
  • 14
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Specific regulators of inflammation
    • Pham CT. Neutrophil serine proteases: specific regulators of inflammation. Nat Rev Immunol. 2006;6(7):541-550.
    • (2006) Nat Rev Immunol , vol.6 , Issue.7 , pp. 541-550
    • Pham, C.T.1
  • 16
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • Belaaouaj A, McCarthy R, Baumann M, et al. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat Med. 1998;4(5):615-618.
    • (1998) Nat Med , vol.4 , Issue.5 , pp. 615-618
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3
  • 17
    • 0037149510 scopus 로고    scopus 로고
    • Killing activity of neutrophils is mediated through activation of proteases by k1 flux
    • Reeves EP, Lu H, Jacobs HL, et al. Killing activity of neutrophils is mediated through activation of proteases by K1 flux. Nature. 2002;416(6878): 291-297.
    • (2002) Nature , vol.416 , Issue.6878 , pp. 291-297
    • Reeves, E.P.1    Lu, H.2    Jacobs, H.L.3
  • 18
    • 0036168150 scopus 로고    scopus 로고
    • Dipeptidyl peptidase i activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis
    • Adkison AM, Raptis SZ, Kelley DG, Pham CT. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. J Clin Invest. 2002; 109(3):363-371.
    • (2002) J Clin Invest , vol.109 , Issue.3 , pp. 363-371
    • Adkison, A.M.1    Raptis, S.Z.2    Kelley, D.G.3    Pham, C.T.4
  • 20
    • 34547734976 scopus 로고    scopus 로고
    • The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in pseudomonas aeruginosa infection
    • Benarafa C, Priebe GP, Remold-O’Donnell E. The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection. J Exp Med. 2007;204(8):1901-1909.
    • (2007) J Exp Med , vol.204 , Issue.8 , pp. 1901-1909
    • Benarafa, C.1    Priebe, G.P.2    Remold-O’Donnell, E.3
  • 21
    • 0036830129 scopus 로고    scopus 로고
    • Characterization of four murine homologs of the human ov-serpin monocyte neutrophil elastase inhibitor Mnei (serpinb1)
    • Benarafa C, Cooley J, Zeng W, Bird PI, Remold-O’Donnell E. Characterization of four murine homologs of the human ov-serpin monocyte neutrophil elastase inhibitor MNEI (SERPINB1). J Biol Chem. 2002;277(44):42028-42033.
    • (2002) J Biol Chem , vol.277 , Issue.44 , pp. 42028-42033
    • Benarafa, C.1    Cooley, J.2    Zeng, W.3    Bird, P.I.4    Remold-O’Donnell, E.5
  • 22
    • 0035951076 scopus 로고    scopus 로고
    • The serpin mnei inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites
    • Cooley J, Takayama TK, Shapiro SD, Schechter NM, Remold-O’Donnell E. The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites. Biochemistry. 2001;40(51):15762-15770.
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15762-15770
    • Cooley, J.1    Takayama, T.K.2    Shapiro, S.D.3    Schechter, N.M.4    Remold-O’Donnell, E.5
  • 23
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase i is required for the processing and activation of granzymes a and b in vivo
    • Pham CT, Ley TJ. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc Natl Acad Sci U S A. 1999;96(15):8627-8632.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.15 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 24
    • 0030627476 scopus 로고    scopus 로고
    • Characterization of the mouse neutrophil elastase gene and localization to chromosome 10
    • Belaaouaj A, Walsh BC, Jenkins NA, Copeland NG, Shapiro SD. Characterization of the mouse neutrophil elastase gene and localization to chromosome 10. Mamm Genome. 1997;8(1):5-8.
    • (1997) Mamm Genome , vol.8 , Issue.1 , pp. 5-8
    • Belaaouaj, A.1    Walsh, B.C.2    Jenkins, N.A.3    Copeland, N.G.4    Shapiro, S.D.5
  • 25
    • 79959338677 scopus 로고    scopus 로고
    • The serpinb1 knockout mouse a model for studying neutrophil protease regulation in homeostasis and inflammation
    • Benarafa C. The SerpinB1 knockout mouse a model for studying neutrophil protease regulation in homeostasis and inflammation. Methods Enzymol. 2011;499:135-148.
    • (2011) Methods Enzymol , vol.499 , pp. 135-148
    • Benarafa, C.1
  • 26
    • 33749365853 scopus 로고    scopus 로고
    • Serpinb1 upregulation is associated with in vivo complex formation with neutrophil elastase and cathepsin g in a baboon model of bronchopulmonary dysplasia
    • Yasumatsu R, Altiok O, Benarafa C, et al. SERPINB1 upregulation is associated with in vivo complex formation with neutrophil elastase and cathepsin G in a baboon model of bronchopulmonary dysplasia. Am J Physiol Lung Cell Mol Physiol. 2006;291(4):L619-L627.
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.291 , Issue.4 , pp. L619-L627
    • Yasumatsu, R.1    Altiok, O.2    Benarafa, C.3
  • 27
    • 0036800759 scopus 로고    scopus 로고
    • Neutrophil-independent mechanisms of caspase-1- and il-18-mediated ischemic acute tubular necrosis in mice
    • Melnikov VY, Faubel S, Siegmund B, Lucia MS, Ljubanovic D, Edelstein CL. Neutrophil-independent mechanisms of caspase-1- and IL-18-mediated ischemic acute tubular necrosis in mice. J Clin Invest. 2002;110(8):1083-1091.
    • (2002) J Clin Invest , vol.110 , Issue.8 , pp. 1083-1091
    • Melnikov, V.Y.1    Faubel, S.2    Siegmund, B.3    Lucia, M.S.4    Ljubanovic, D.5    Edelstein, C.L.6
  • 28
    • 68749094973 scopus 로고    scopus 로고
    • Application of specific cell permeable cathepsin g inhibitors resulted in reduced antigen processing in primary dendritic cells
    • Reich M, Lesner A, Legowska A, et al. Application of specific cell permeable cathepsin G inhibitors resulted in reduced antigen processing in primary dendritic cells. Mol Immunol. 2009;46(15): 2994-2999.
    • (2009) Mol Immunol , vol.46 , Issue.15 , pp. 2994-2999
    • Reich, M.1    Lesner, A.2    Legowska, A.3
  • 29
    • 0025044550 scopus 로고
    • Mechanism of l-leucyl-l-leucine methyl ester-mediated killing of cytotoxic lymphocytes: Dependence on a lysosomal thiol protease, dipeptidyl peptidase i, that is enriched in these cells
    • Thiele DL, Lipsky PE. Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes: dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. Proc Natl Acad Sci U S A. 1990;87(1):83-87.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.1 , pp. 83-87
    • Thiele, D.L.1    Lipsky, P.E.2
  • 30
    • 0025374741 scopus 로고
    • The action of leucyl-leucine methyl ester on cytotoxic lymphocytes requires uptake by a novel dipeptide-specific facilitated transport system and dipeptidyl peptidase i-mediated conversion to membranolytic products
    • Thiele DL, Lipsky PE. The action of leucyl-leucine methyl ester on cytotoxic lymphocytes requires uptake by a novel dipeptide-specific facilitated transport system and dipeptidyl peptidase I-mediated conversion to membranolytic products. J Exp Med. 1990;172(1):183-194.
    • (1990) J Exp Med , vol.172 , Issue.1 , pp. 183-194
    • Thiele, D.L.1    Lipsky, P.E.2
  • 31
    • 0033026169 scopus 로고    scopus 로고
    • Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins
    • Bird PI. Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. Immunol Cell Biol. 1999;77(1):47-57.
    • (1999) Immunol Cell Biol , vol.77 , Issue.1 , pp. 47-57
    • Bird, P.I.1
  • 32
    • 23844473263 scopus 로고    scopus 로고
    • The ovalbumin serpins revisited: Perspective from the chicken genome of clade b serpin evolution in vertebrates
    • Benarafa C, Remold-O’Donnell E. The ovalbumin serpins revisited: perspective from the chicken genome of clade B serpin evolution in vertebrates. Proc Natl Acad Sci U S A. 2005;102(32): 11367-11372.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.32 , pp. 11367-11372
    • Benarafa, C.1    Remold-O’Donnell, E.2
  • 33
    • 20444433960 scopus 로고    scopus 로고
    • Serine protease cathepsin g regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
    • Raptis SZ, Shapiro SD, Simmons PM, Cheng AM, Pham CT. Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering. Immunity. 2005; 22(6):679-691.
    • (2005) Immunity , vol.22 , Issue.6 , pp. 679-691
    • Raptis, S.Z.1    Shapiro, S.D.2    Simmons, P.M.3    Cheng, A.M.4    Pham, C.T.5
  • 34
    • 0037592155 scopus 로고    scopus 로고
    • Neutrophil cathepsin g promotes detachment-induced cardiomyocyte apoptosis via a protease-activated receptor-independent mechanism
    • Sabri A, Alcott SG, Elouardighi H, et al. Neutrophil cathepsin G promotes detachment-induced cardiomyocyte apoptosis via a protease-activated receptor-independent mechanism. J Biol Chem. 2003;278(26):23944-23954.
    • (2003) J Biol Chem , vol.278 , Issue.26 , pp. 23944-23954
    • Sabri, A.1    Alcott, S.G.2    Elouardighi, H.3
  • 35
    • 37849053036 scopus 로고    scopus 로고
    • Novel mode for neutrophil protease cathepsin g-mediated signaling: Membrane shedding of epidermal growth factor is required for cardiomyocyte anoikis
    • Rafiq K, Hanscom M, Valerie K, Steinberg SF, Sabri A. Novel mode for neutrophil protease cathepsin G-mediated signaling: membrane shedding of epidermal growth factor is required for cardiomyocyte anoikis. Circ Res. 2008;102(1): 32-41.
    • (2008) Circ Res , vol.102 , Issue.1 , pp. 32-41
    • Rafiq, K.1    Hanscom, M.2    Valerie, K.3    Steinberg, S.F.4    Sabri, A.5
  • 36
    • 84857327342 scopus 로고    scopus 로고
    • C-CBL ubiquitin ligase regulates focal adhesion protein turnover and myofibril degeneration induced by neutrophil protease cathepsin G
    • Rafiq K, Guo J, Vlasenko L, et al. c-Cbl ubiquitin ligase regulates focal adhesion protein turnover and myofibril degeneration induced by neutrophil protease cathepsin G. J Biol Chem. 2012;287(8): 5327-5339.
    • (2012) J Biol Chem , vol.287 , Issue.8 , pp. 5327-5339
    • Rafiq, K.1    Guo, J.2    Vlasenko, L.3
  • 37
    • 13544263218 scopus 로고    scopus 로고
    • The transcriptional program of terminal granulocytic differentiation
    • Theilgaard-Mönch K, Jacobsen LC, Borup R, et al. The transcriptional program of terminal granulocytic differentiation. Blood. 2005;105(4): 1785-1796.
    • (2005) Blood , vol.105 , Issue.4 , pp. 1785-1796
    • Theilgaard-Mönch, K.1    Jacobsen, L.C.2    Borup, R.3
  • 38
    • 34248398513 scopus 로고    scopus 로고
    • Neutrophil elastase depends on serglycin proteoglycan for localization in granules
    • Niemann CU, Abrink M, Pejler G, et al. Neutrophil elastase depends on serglycin proteoglycan for localization in granules. Blood. 2007;109(10): 4478-4486.
    • (2007) Blood , vol.109 , Issue.10 , pp. 4478-4486
    • Niemann, C.U.1    Abrink, M.2    Pejler, G.3
  • 39
    • 0030970351 scopus 로고    scopus 로고
    • Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity
    • Zhou Q, Salvesen GS. Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity. Biochem J. 1997;324(Pt 2):361-364.
    • (1997) Biochem J , vol.324 , pp. 361-364
    • Zhou, Q.1    Salvesen, G.S.2
  • 40
    • 69249140641 scopus 로고    scopus 로고
    • Lysosomes as “suicide bags” in cell death: myth or reality?
    • Turk B, Turk V. Lysosomes as “suicide bags” in cell death: myth or reality? J Biol Chem. 2009; 284(33):21783-21787.
    • (2009) J Biol Chem , vol.284 , Issue.33 , pp. 21783-21787
    • Turk, B.1    Turk, V.2
  • 41
    • 42949098879 scopus 로고    scopus 로고
    • Death by a thousand cuts: Granzyme pathways of programmed cell death
    • Chowdhury D, Lieberman J. Death by a thousand cuts: granzyme pathways of programmed cell death. Annu Rev Immunol. 2008;26:389-420.
    • (2008) Annu Rev Immunol , vol.26 , pp. 389-420
    • Chowdhury, D.1    Lieberman, J.2
  • 42
    • 33746110374 scopus 로고    scopus 로고
    • Granzyme-like sequences in bony fish shed light on the emergence of hematopoietic serine proteases during vertebrate evolution
    • Wernersson S, Reimer JM, Poorafshar M, et al. Granzyme-like sequences in bony fish shed light on the emergence of hematopoietic serine proteases during vertebrate evolution. Dev Comp Immunol. 2006;30(10):901-918.
    • (2006) Dev Comp Immunol , vol.30 , Issue.10 , pp. 901-918
    • Wernersson, S.1    Reimer, J.M.2    Poorafshar, M.3
  • 43
    • 84872743281 scopus 로고    scopus 로고
    • Identification of serpinb1 as a physiological inhibitor of human granzyme H
    • Wang L, Li Q, Wu L, et al. Identification of SERPINB1 as a physiological inhibitor of human granzyme H. J Immunol. 2013;190(3):1319-1330.
    • (2013) J Immunol , vol.190 , Issue.3 , pp. 1319-1330
    • Wang, L.1    Li, Q.2    Wu, L.3
  • 44
    • 33751252804 scopus 로고    scopus 로고
    • The major human and mouse granzymes are structurally and functionally divergent
    • Kaiserman D, Bird CH, Sun J, et al. The major human and mouse granzymes are structurally and functionally divergent. J Cell Biol. 2006;175(4): 619-630.
    • (2006) J Cell Biol , vol.175 , Issue.4 , pp. 619-630
    • Kaiserman, D.1    Bird, C.H.2    Sun, J.3
  • 45
    • 0031032401 scopus 로고    scopus 로고
    • Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin g and mast cell chymase
    • Schick C, Kamachi Y, Bartuski AJ, et al. Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase. J Biol Chem. 1997;272(3):1849-1855.
    • (1997) J Biol Chem , vol.272 , Issue.3 , pp. 1849-1855
    • Schick, C.1    Kamachi, Y.2    Bartuski, A.J.3
  • 46
    • 17944376032 scopus 로고    scopus 로고
    • Expression of the serpin serine protease inhibitor 6 protects dendritic cells from cytotoxic t lymphocyte-induced apoptosis: Differential modulation by t helper type 1 and type 2 cells
    • Medema JP, Schuurhuis DH, Rea D, et al. Expression of the serpin serine protease inhibitor 6 protects dendritic cells from cytotoxic T lymphocyte-induced apoptosis: differential modulation by T helper type 1 and type 2 cells. J Exp Med. 2001;194(5):657-667.
    • (2001) J Exp Med , vol.194 , Issue.5 , pp. 657-667
    • Medema, J.P.1    Schuurhuis, D.H.2    Rea, D.3
  • 47
    • 33847357051 scopus 로고    scopus 로고
    • Expression of the granzyme b inhibitor pi9 predicts outcome in nasal Nk/t-cell lymphoma: results of a western series of 48 patients treated with first-line polychemotherapy within the groupe d’etude des lymphomes de l’adulte (gela) trials
    • Bossard C, Belhadj K, Reyes F, et al. Expression of the granzyme B inhibitor PI9 predicts outcome in nasal NK/T-cell lymphoma: results of a Western series of 48 patients treated with first-line polychemotherapy within the Groupe d’Etude des Lymphomes de l’Adulte (GELA) trials. Blood. 2007;109(5):2183-2189.
    • (2007) Blood , vol.109 , Issue.5 , pp. 2183-2189
    • Bossard, C.1    Belhadj, K.2    Reyes, F.3
  • 48
    • 0036095702 scopus 로고    scopus 로고
    • Expression of the granzyme b inhibitor, protease inhibitor 9, by tumor cells in patients with non-hodgkin and hodgkin lymphoma: A novel protective mechanism for tumor cells to circumvent the immune system?
    • ten
    • Bladergroen BA, Meijer CJ, ten Berge RL, et al. Expression of the granzyme B inhibitor, protease inhibitor 9, by tumor cells in patients with non-Hodgkin and Hodgkin lymphoma: a novel protective mechanism for tumor cells to circumvent the immune system? Blood. 2002; 99(1):232-237.
    • (2002) Blood , vol.99 , Issue.1 , pp. 232-237
    • Bladergroen, B.A.1    Meijer, C.J.2    Berge, R.L.3
  • 49
    • 0034144636 scopus 로고    scopus 로고
    • Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G
    • Tkalcevic J, Novelli M, Phylactides M, Iredale JP, Segal AW, Roes J. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity. 2000;12(2): 201-210.
    • (2000) Immunity , vol.12 , Issue.2 , pp. 201-210
    • Tkalcevic, J.1    Novelli, M.2    Phylactides, M.3    Iredale, J.P.4    Segal, A.W.5    Roes, J.6
  • 50
    • 79960862858 scopus 로고    scopus 로고
    • Critical role of serpinb1 in regulating inflammatory responses in pulmonary influenza infection
    • Gong D, Farley K, White M, Hartshorn KL, Benarafa C, Remold-O’Donnell E. Critical role of serpinB1 in regulating inflammatory responses in pulmonary influenza infection. J Infect Dis. 2011; 204(4):592-600.
    • (2011) J Infect Dis , vol.204 , Issue.4 , pp. 592-600
    • Gong, D.1    Farley, K.2    White, M.3    Hartshorn, K.L.4    Benarafa, C.5    Remold-O’Donnell, E.6


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