메뉴 건너뛰기




Volumn 109, Issue 4, 2015, Pages 366-374

HNA antibody-mediated neutrophil aggregation is dependent on serine protease activity

Author keywords

Aggregation; HNA 2; HNA 3a; Inhibitors; Neutrophil; TRALI

Indexed keywords

4 (2 AMINOETHYL)BENZENESULFONYL FLUORIDE; ALLOANTIGEN; ASPARTIC PROTEINASE; CATHEPSIN G; CYSTEINE PROTEINASE; CYTOCHALASIN D; FORMALDEHYDE; HUMAN NEUTROPHIL ALLOANTIGEN 2 ANTIBODY; HUMAN NEUTROPHIL ALLOANTIGEN 3A ANTIBODY; INDOLEACETIC ACID; IODOACETAMIDE; LEUKOCYTE ELASTASE; LUCIGENIN; METALLOPROTEINASE; MYELOBLASTIN; N ALPHA TOSYL LEVO LYSINE CHLOROMETHYL KETONE HYDROCHLORIDE; PHORBOL 13 ACETATE 12 MYRISTATE; REACTIVE OXYGEN METABOLITE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; TOSYLPHENYLALANYL CHLOROMETHYL KETONE; UNCLASSIFIED DRUG; CD177 PROTEIN, HUMAN; CELL SURFACE RECEPTOR; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HNA-3A ANTIGEN, HUMAN;

EID: 84944281427     PISSN: 00429007     EISSN: 14230410     Source Type: Journal    
DOI: 10.1111/vox.12292     Document Type: Article
Times cited : (1)

References (37)
  • 1
    • 78650374651 scopus 로고    scopus 로고
    • Antibody-mediated (immune) transfusion-related acute lung injury
    • Bux J: Antibody-mediated (immune) transfusion-related acute lung injury. Vox Sang 2011; 100:122-128
    • (2011) Vox Sang , vol.100 , pp. 122-128
    • Bux, J.1
  • 2
    • 73649127274 scopus 로고    scopus 로고
    • Frequency and severity of transfusion-related acute lung injury-German haemovigilance data (2006-2007)
    • Keller-Stanislawski B, Reil A, Günay S, et al.: Frequency and severity of transfusion-related acute lung injury-German haemovigilance data (2006-2007). Vox Sang 2010; 98:70-77
    • (2010) Vox Sang , vol.98 , pp. 70-77
    • Keller-Stanislawski, B.1    Reil, A.2    Günay, S.3
  • 3
    • 79958724687 scopus 로고    scopus 로고
    • TRALI-new challenges for histocompatibility and immunogenetics in transfusion medicine
    • Flesch B, Petershofen E, Bux J: TRALI-new challenges for histocompatibility and immunogenetics in transfusion medicine. Tissue Antigens 2011; 78:1-7
    • (2011) Tissue Antigens , vol.78 , pp. 1-7
    • Flesch, B.1    Petershofen, E.2    Bux, J.3
  • 4
    • 27744530096 scopus 로고    scopus 로고
    • Albumin attenuates neutrophil activation induced by stimulators including antibodies against neutrophil-specific antigens
    • Hashimoto M, Saigo K, Jyokei Y, et al.: Albumin attenuates neutrophil activation induced by stimulators including antibodies against neutrophil-specific antigens. Transfus Apher Sci 2005; 33:289-298
    • (2005) Transfus Apher Sci , vol.33 , pp. 289-298
    • Hashimoto, M.1    Saigo, K.2    Jyokei, Y.3
  • 5
    • 0037406184 scopus 로고    scopus 로고
    • TRALI due to granulocyte-agglutinating human neutrophil antigen-3a (5b) alloantibodies in donor plasma: a report of 2 fatalities
    • Davoren A, Curtis B, Shulman I, et al.: TRALI due to granulocyte-agglutinating human neutrophil antigen-3a (5b) alloantibodies in donor plasma: a report of 2 fatalities. Transfusion 2003; 43:641-645
    • (2003) Transfusion , vol.43 , pp. 641-645
    • Davoren, A.1    Curtis, B.2    Shulman, I.3
  • 6
    • 77954331275 scopus 로고    scopus 로고
    • Systemic neutrophilic aggregates in transfusion-related acute lung injury
    • Lima J, Reddy VV, Marques MB: Systemic neutrophilic aggregates in transfusion-related acute lung injury. Transfusion 2010; 50:1427-1428
    • (2010) Transfusion , vol.50 , pp. 1427-1428
    • Lima, J.1    Reddy, V.V.2    Marques, M.B.3
  • 7
    • 73849152488 scopus 로고    scopus 로고
    • Characterization of the human neutrophil alloantigen-3a
    • Greinacher A, Wesche J, Hammer E, et al.: Characterization of the human neutrophil alloantigen-3a. Nat Med 2010; 16:45-48
    • (2010) Nat Med , vol.16 , pp. 45-48
    • Greinacher, A.1    Wesche, J.2    Hammer, E.3
  • 8
    • 0034119167 scopus 로고    scopus 로고
    • Neutrophils: molecules, functions and pathophysiological aspects
    • Witko-Sarsat V, Rieu P, Descamps-Latscha B, et al.: Neutrophils: molecules, functions and pathophysiological aspects. Lab Invest 2000; 80:617-653
    • (2000) Lab Invest , vol.80 , pp. 617-653
    • Witko-Sarsat, V.1    Rieu, P.2    Descamps-Latscha, B.3
  • 9
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengeløv H, Kjeldsen L, Borregaard N: Control of exocytosis in early neutrophil activation. J Immunol 1993; 150:1535-1543
    • (1993) J Immunol , vol.150 , pp. 1535-1543
    • Sengeløv, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 10
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • Faurschou M, Borregaard N: Neutrophil granules and secretory vesicles in inflammation. Microbes Infect 2003; 5:1317-1327
    • (2003) Microbes Infect , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 11
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard N, Cowland JB: Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 1997; 89:3503-3521
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 12
    • 43049112108 scopus 로고    scopus 로고
    • Neutrophil serine proteases fine-tune the inflammatory response
    • Pham CT. Neutrophil serine proteases fine-tune the inflammatory response. Int J Biochem Cell Biol 2008; 40:1317-1333.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1317-1333
    • Pham, C.T.1
  • 13
    • 0037678914 scopus 로고    scopus 로고
    • Metalloproteinase inhibition reduces lung injury and improves survival after cecal ligation and puncture in rats
    • Steinberg J, Halter J, Schiller HJ, et al.: Metalloproteinase inhibition reduces lung injury and improves survival after cecal ligation and puncture in rats. J Surg Res 2003; 111:185-195
    • (2003) J Surg Res , vol.111 , pp. 185-195
    • Steinberg, J.1    Halter, J.2    Schiller, H.J.3
  • 14
    • 33644842000 scopus 로고    scopus 로고
    • Neutrophil granule contents in the pathogenesis of lung injury
    • Moraes TJ, Zurawska JH, Downey GP: Neutrophil granule contents in the pathogenesis of lung injury. Curr Opin Hematol 2006; 13:21-27
    • (2006) Curr Opin Hematol , vol.13 , pp. 21-27
    • Moraes, T.J.1    Zurawska, J.H.2    Downey, G.P.3
  • 15
    • 0031729271 scopus 로고    scopus 로고
    • Neutrophil serine proteinases and defensins in chronic obstructive pulmonary disease: effects on pulmonary epithelium
    • Hiemstra P, Van Wetering S, Stolk J: Neutrophil serine proteinases and defensins in chronic obstructive pulmonary disease: effects on pulmonary epithelium. Eur Respir J 1998; 12:1200-1208
    • (1998) Eur Respir J , vol.12 , pp. 1200-1208
    • Hiemstra, P.1    Van Wetering, S.2    Stolk, J.3
  • 16
    • 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; 6:541-550
    • (2006) Nat Rev Immunol , vol.6 , pp. 541-550
    • Pham, C.T.1
  • 17
    • 80051951092 scopus 로고    scopus 로고
    • Membrane-bound proteinase 3 and PAR2 mediate phagocytosis of non-opsonized bacteria in human neutrophils
    • Kim YC, Shin JE, Lee SH, et al.: Membrane-bound proteinase 3 and PAR2 mediate phagocytosis of non-opsonized bacteria in human neutrophils. Mol Immunol 2011; 48:1966-1974
    • (2011) Mol Immunol , vol.48 , pp. 1966-1974
    • Kim, Y.C.1    Shin, J.E.2    Lee, S.H.3
  • 18
    • 0029087868 scopus 로고
    • Inhibition of neutrophil chemotaxis by protease inhibitors. Differential effect of inhibitors of serine and thiol proteases
    • Barna JB, Kew RR: Inhibition of neutrophil chemotaxis by protease inhibitors. Differential effect of inhibitors of serine and thiol proteases. Inflammation 1995; 19:561-574
    • (1995) Inflammation , vol.19 , pp. 561-574
    • Barna, J.B.1    Kew, R.R.2
  • 19
    • 78650096176 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases
    • Korkmaz B, Horwitz MS, Jenne DE, et al.: Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacol Rev 2010; 62:726-759
    • (2010) Pharmacol Rev , vol.62 , pp. 726-759
    • Korkmaz, B.1    Horwitz, M.S.2    Jenne, D.E.3
  • 20
    • 78651368689 scopus 로고    scopus 로고
    • Geno-and phenotyping and immunogenicity of HNA-3
    • Reil A, Wesche J, Greinacher A, et al.: Geno-and phenotyping and immunogenicity of HNA-3. Transfusion 2011; 51:18-24
    • (2011) Transfusion , vol.51 , pp. 18-24
    • Reil, A.1    Wesche, J.2    Greinacher, A.3
  • 21
    • 0017714543 scopus 로고
    • The detection of granulocyte alloantibodies with an indirect immunofluorescence test
    • Verheugt F, Borne A, Decary F, et al.: The detection of granulocyte alloantibodies with an indirect immunofluorescence test. Br J Haematol 1977; 36:533-544
    • (1977) Br J Haematol , vol.36 , pp. 533-544
    • Verheugt, F.1    Borne, A.2    Decary, F.3
  • 22
    • 84931442972 scopus 로고    scopus 로고
    • Impact of priming on the response of neutrophils to human neutrophil alloantigen-3a antibodies
    • [Epub ahead of print].
    • Berthold T, Muschter S, Schubert N, et al.: Impact of priming on the response of neutrophils to human neutrophil alloantigen-3a antibodies. Transfusion 2014; doi:10.1111/trf.12898 [Epub ahead of print].
    • (2014) Transfusion
    • Berthold, T.1    Muschter, S.2    Schubert, N.3
  • 23
    • 84890426136 scopus 로고    scopus 로고
    • Expression of the CTL2 transcript variants in human peripheral blood cells and human tissues
    • Flesch BK, Wesche J, Berthold T, et al.: Expression of the CTL2 transcript variants in human peripheral blood cells and human tissues. Transfusion 2013; 53:3217-3223
    • (2013) Transfusion , vol.53 , pp. 3217-3223
    • Flesch, B.K.1    Wesche, J.2    Berthold, T.3
  • 24
    • 33846699482 scopus 로고    scopus 로고
    • Proteinase 3 and CD177 are expressed on the plasma membrane of the same subset of neutrophils
    • Bauer S, Abdgawad M, Gunnarsson L, et al.: Proteinase 3 and CD177 are expressed on the plasma membrane of the same subset of neutrophils. J Leukoc Biol 2007; 81:458-464
    • (2007) J Leukoc Biol , vol.81 , pp. 458-464
    • Bauer, S.1    Abdgawad, M.2    Gunnarsson, L.3
  • 25
    • 70249087300 scopus 로고    scopus 로고
    • The role of neutrophils in the pathogenesis of transfusion-related acute lung injury
    • Fung YL, Silliman CC: The role of neutrophils in the pathogenesis of transfusion-related acute lung injury. Transfus Med Rev 2009; 23:266-283
    • (2009) Transfus Med Rev , vol.23 , pp. 266-283
    • Fung, Y.L.1    Silliman, C.C.2
  • 26
    • 0034940957 scopus 로고    scopus 로고
    • Reduction and alkylation of proteins in preparation of two-dimensional map analysis: Why, when, and how?
    • Herbert B, Galvani M, Hamdan M, et al.: Reduction and alkylation of proteins in preparation of two-dimensional map analysis: Why, when, and how? Electrophoresis 2001; 22:2046-2057
    • (2001) Electrophoresis , vol.22 , pp. 2046-2057
    • Herbert, B.1    Galvani, M.2    Hamdan, M.3
  • 27
    • 0034665315 scopus 로고    scopus 로고
    • Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition
    • Campbell EJ, Campbell MA, Owen CA: Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J Immunol 2000; 165:3366-3374
    • (2000) J Immunol , vol.165 , pp. 3366-3374
    • Campbell, E.J.1    Campbell, M.A.2    Owen, C.A.3
  • 28
    • 0017063195 scopus 로고
    • The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin
    • Feinstein G, Malemud C, Janoff A. The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin. Biochim Biophys Acta 1976; 429:925-932.
    • (1976) Biochim Biophys Acta , vol.429 , pp. 925-932
    • Feinstein, G.1    Malemud, C.2    Janoff, A.3
  • 29
    • 0029935481 scopus 로고    scopus 로고
    • Two crystal structures of the leupeptin-trypsin complex
    • Kurinov I, Harrison R: Two crystal structures of the leupeptin-trypsin complex. Protein Sci 1996; 5:752-758
    • (1996) Protein Sci , vol.5 , pp. 752-758
    • Kurinov, I.1    Harrison, R.2
  • 30
    • 2642593603 scopus 로고
    • Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts
    • O'Donnell-Tormey J, Quigley JP: Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts. Proc Natl Acad Sci 1983; 80:344-348
    • (1983) Proc Natl Acad Sci , vol.80 , pp. 344-348
    • O'Donnell-Tormey, J.1    Quigley, J.P.2
  • 31
    • 0027446410 scopus 로고
    • Leupeptin-binding site (s) in the mammalian multicatalytic proteinase complex
    • Savory PJ, Rivett AJ: Leupeptin-binding site (s) in the mammalian multicatalytic proteinase complex. Biochem J 1993; 289:45-48
    • (1993) Biochem J , vol.289 , pp. 45-48
    • Savory, P.J.1    Rivett, A.J.2
  • 32
    • 84887852110 scopus 로고    scopus 로고
    • Neutrophil elastase and proteinase-3 trigger G protein-biased signaling through proteinase-activated receptor-1 (PAR1)
    • Mihara K, Ramachandran R, Renaux B, et al.: Neutrophil elastase and proteinase-3 trigger G protein-biased signaling through proteinase-activated receptor-1 (PAR1). J Biol Chem 2013; 288:32979-32990
    • (2013) J Biol Chem , vol.288 , pp. 32979-32990
    • Mihara, K.1    Ramachandran, R.2    Renaux, B.3
  • 33
    • 0030943738 scopus 로고    scopus 로고
    • Human neutrophil elastase proteolytically activates the platelet integrin alphaIIb\beta3 through cleavage of the carboxyl terminus of the alphaIIb subunit heavy chain
    • Si-Tahar M, Pidard D, Balloy V, et al.: Human neutrophil elastase proteolytically activates the platelet integrin alphaIIb\beta3 through cleavage of the carboxyl terminus of the alphaIIb subunit heavy chain. J Biol Chem 1997; 272:11636-11647
    • (1997) J Biol Chem , vol.272 , pp. 11636-11647
    • Si-Tahar, M.1    Pidard, D.2    Balloy, V.3
  • 34
    • 0034629468 scopus 로고    scopus 로고
    • Cathepsin G activates protease-activated receptor-4 in human platelets
    • Sambrano GR, Huang W, Faruqi T, et al.: Cathepsin G activates protease-activated receptor-4 in human platelets. J Biol Chem 2000; 275:6819-6823
    • (2000) J Biol Chem , vol.275 , pp. 6819-6823
    • Sambrano, G.R.1    Huang, W.2    Faruqi, T.3
  • 35
    • 84887050089 scopus 로고    scopus 로고
    • Anti-human neutrophil antigen-3a induced transfusion-related acute lung injury in mice by direct disturbance of lung endothelial cells
    • Bayat B, Tjahjono Y, Sydykov A, et al.: Anti-human neutrophil antigen-3a induced transfusion-related acute lung injury in mice by direct disturbance of lung endothelial cells. Arterioscler Thromb Vasc Biol 2013; 33:2538-2548
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , pp. 2538-2548
    • Bayat, B.1    Tjahjono, Y.2    Sydykov, A.3
  • 36
    • 33846914829 scopus 로고    scopus 로고
    • Donor antibodies to HNA-3a implicated in TRALI reactions prime neutrophils and cause PMN-mediated damage to human pulmonary microvascular endothelial cells in a two-event in vitro model
    • Silliman CC, Curtis BR, Kopko PM, et al.: Donor antibodies to HNA-3a implicated in TRALI reactions prime neutrophils and cause PMN-mediated damage to human pulmonary microvascular endothelial cells in a two-event in vitro model. Blood 2007; 109:1752-1755
    • (2007) Blood , vol.109 , pp. 1752-1755
    • Silliman, C.C.1    Curtis, B.R.2    Kopko, P.M.3
  • 37
    • 83455200396 scopus 로고    scopus 로고
    • Serine protease inhibition reduces post-ischemic granulocyte recruitment in mouse intestine
    • Gobbetti T, Cenac N, Motta J-P, et al.: Serine protease inhibition reduces post-ischemic granulocyte recruitment in mouse intestine. Am J Pathol 2012; 180:141-152
    • (2012) Am J Pathol , vol.180 , pp. 141-152
    • Gobbetti, T.1    Cenac, N.2    Motta, J.-P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.