메뉴 건너뛰기




Volumn 57, Issue 2, 2017, Pages 238-247

Alpha-1 antitrypsin-deficient macrophages have increased matriptase-mediated proteolytic activity

Author keywords

Alpha 1 antitrypsin deficiency; Extracellular matrix degradation; Macrophages; Matriptase; Matrix metalloproteinase 14

Indexed keywords

ALPHA 1 ANTITRYPSIN; APROTININ; BATIMASTAT; COLONY STIMULATING FACTOR 1; ENZYME PRECURSOR; GELATINASE A; GELATINASE B; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; LIPOPOLYSACCHARIDE; MATRIPTASE; MATRIX METALLOPROTEINASE 14; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PROTEIN DISULFIDE ISOMERASE; SCLEROPROTEIN; SERINE PROTEINASE; SERPINA1 PROTEIN, HUMAN; ST14 PROTEIN, HUMAN;

EID: 85026874971     PISSN: 10441549     EISSN: 15354989     Source Type: Journal    
DOI: 10.1165/rcmb.2016-0366OC     Document Type: Article
Times cited : (15)

References (49)
  • 1
    • 84893667261 scopus 로고    scopus 로고
    • The molecular and cellular pathology of a1-antitrypsin deficiency
    • Gooptu B, Dickens JA, Lomas DA. The molecular and cellular pathology of a1-antitrypsin deficiency. Trends Mol Med 2014;20: 116-127.
    • (2014) Trends Mol Med , vol.20 , pp. 116-127
    • Gooptu, B.1    Dickens, J.A.2    Lomas, D.A.3
  • 2
    • 84875674428 scopus 로고    scopus 로고
    • The electrophoretic a1-globulin pattern of serum in a1-antitrypsin deficiency. 1963
    • Laurell C-B, Eriksson S. The electrophoretic a1-globulin pattern of serum in a1-antitrypsin deficiency. 1963. COPD 2013;10:3-8.
    • COPD 2013 , vol.10 , pp. 3-8
    • Laurell, C.-B.1    Eriksson, S.2
  • 3
    • 0000461577 scopus 로고
    • Pulmonary emphysema and alpha1-antitrypsin deficiency
    • Eriksson S. Pulmonary emphysema and alpha1-antitrypsin deficiency. Acta Med Scand 1964;175:197-205.
    • (1964) Acta Med Scand , vol.175 , pp. 197-205
    • Eriksson, S.1
  • 4
    • 0014530551 scopus 로고
    • Cirrhosis associated with alpha-1-antitrypsin deficiency: A previously unrecognized inherited disorder
    • Sharp HL, Bridges RA, Krivit W, Freier EF. Cirrhosis associated with alpha-1-antitrypsin deficiency: A previously unrecognized inherited disorder. J Lab Clin Med 1969;73:934-939.
    • (1969) J Lab Clin Med , vol.73 , pp. 934-939
    • Sharp, H.L.1    Bridges, R.A.2    Krivit, W.3    Freier, E.F.4
  • 5
    • 0025350658 scopus 로고
    • Alpha 1-antitrypsin deficiency, emphysema, and liver disease: Genetic basis and strategies for therapy
    • Crystal RG. Alpha 1-antitrypsin deficiency, emphysema, and liver disease: Genetic basis and strategies for therapy. J Clin Invest 1990;85:1343-1352.
    • (1990) J Clin Invest , vol.85 , pp. 1343-1352
    • Crystal, R.G.1
  • 6
    • 84937969384 scopus 로고    scopus 로고
    • Intravenous augmentation treatment and lung density in severe a1 antitrypsin deficiency (RAPID): A randomised, double-blind, placebo-controlled trial
    • RAPID Trial Study Group
    • Chapman KR, Burdon JGW, Piitulainen E, Sandhaus RA, Seersholm N, Stocks JM, Stoel BC, Huang L, Yao Z, Edelman JM, et al.; RAPID Trial Study Group. Intravenous augmentation treatment and lung density in severe a1 antitrypsin deficiency (RAPID): A randomised, double-blind, placebo-controlled trial. Lancet 2015; 386:360-368.
    • (2015) Lancet , vol.386 , pp. 360-368
    • Chapman, K.R.1    Burdon, J.G.W.2    Piitulainen, E.3    Sandhaus, R.A.4    Seersholm, N.5    Stocks, J.M.6    Stoel, B.C.7    Huang, L.8    Yao, Z.9    Edelman, J.M.10
  • 7
    • 33645999061 scopus 로고    scopus 로고
    • Alveolar macrophage in the driver's seat
    • Lambrecht BN. Alveolar macrophage in the driver's seat. Immunity 2006;24:366-368.
    • (2006) Immunity , vol.24 , pp. 366-368
    • Lambrecht, B.N.1
  • 8
    • 0036257599 scopus 로고    scopus 로고
    • Macrophages and the pathogenesis of COPD
    • Tetley TD. Macrophages and the pathogenesis of COPD. Chest 2002; 121(5 suppl):156S-159S.
    • (2002) Chest , vol.121 , Issue.5 , pp. 156S-159S
    • Tetley, T.D.1
  • 9
    • 84924405916 scopus 로고    scopus 로고
    • Alendronate inhalation ameliorates elastase-induced pulmonary emphysema in mice by induction of apoptosis of alveolar macrophages
    • Ueno M, Maeno T, Nishimura S, Ogata F, Masubuchi H, Hara K, Yamaguchi K, Aoki F, Suga T, Nagai R, et al. Alendronate inhalation ameliorates elastase-induced pulmonary emphysema in mice by induction of apoptosis of alveolar macrophages. Nat Commun 2015;6:6332.
    • (2015) Nat Commun , vol.6 , pp. 6332
    • Ueno, M.1    Maeno, T.2    Nishimura, S.3    Ogata, F.4    Masubuchi, H.5    Hara, K.6    Yamaguchi, K.7    Aoki, F.8    Suga, T.9    Nagai, R.10
  • 10
    • 0036347640 scopus 로고    scopus 로고
    • Sputum chemotactic activity in chronic obstructive pulmonary disease: Effect of a(1)-antitrypsin deficiency and the role of leukotriene B(4) and interleukin 8
    • Woolhouse IS, Bayley DL, Stockley RA. Sputum chemotactic activity in chronic obstructive pulmonary disease: Effect of a(1)-antitrypsin deficiency and the role of leukotriene B(4) and interleukin 8. Thorax 2002; 57:709-714.
    • (2002) Thorax , vol.57 , pp. 709-714
    • Woolhouse, I.S.1    Bayley, D.L.2    Stockley, R.A.3
  • 11
    • 0026229834 scopus 로고
    • Neutrophil accumulation in the lung in alpha 1-antitrypsin deficiency: Spontaneous release of leukotriene B4 by alveolar macrophages
    • Hubbard RC, Fells G, Gadek J, Pacholok S, Humes J, Crystal RG. Neutrophil accumulation in the lung in alpha 1-antitrypsin deficiency: Spontaneous release of leukotriene B4 by alveolar macrophages. J Clin Invest 1991;88:891-897.
    • (1991) J Clin Invest , vol.88 , pp. 891-897
    • Hubbard, R.C.1    Fells, G.2    Gadek, J.3    Pacholok, S.4    Humes, J.5    Crystal, R.G.6
  • 13
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • Hautamaki RD, Kobayashi DK, Senior RM, Shapiro SD. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 1997;277:2002-2004.
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 15
    • 84898636342 scopus 로고    scopus 로고
    • Urokinase plasminogen activator is a central regulator of macrophage three-dimensional invasion, matrix degradation, and adhesion
    • Fleetwood AJ, Achuthan A, Schultz H, Nansen A, Almholt K, Usher P, Hamilton JA. Urokinase plasminogen activator is a central regulator of macrophage three-dimensional invasion, matrix degradation, and adhesion. J Immunol 2014;192:3540-3547.
    • (2014) J Immunol , vol.192 , pp. 3540-3547
    • Fleetwood, A.J.1    Achuthan, A.2    Schultz, H.3    Nansen, A.4    Almholt, K.5    Usher, P.6    Hamilton, J.A.7
  • 16
    • 0019159671 scopus 로고
    • Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages
    • Werb Z, Banda MJ, Jones PA. Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages. J Exp Med 1980;152:1340-1357.
    • (1980) J Exp Med , vol.152 , pp. 1340-1357
    • Werb, Z.1    Banda, M.J.2    Jones, P.A.3
  • 17
    • 0026408814 scopus 로고
    • Role of enzyme receptors and inhibitors in regulating proteolytic activities of macrophages
    • Chapman HA Jr. Role of enzyme receptors and inhibitors in regulating proteolytic activities of macrophages. Ann N Y Acad Sci 1991;624:87-96.
    • (1991) Ann N y Acad Sci , vol.624 , pp. 87-96
    • Chapman, H.A.1
  • 19
    • 0019161545 scopus 로고
    • Degradation of connective tissue matrices by macrophages. II. Influence of matrix composition on proteolysis of glycoproteins, elastin, and collagen by macrophages in culture
    • Jones PA, Werb Z. Degradation of connective tissue matrices by macrophages. II. Influence of matrix composition on proteolysis of glycoproteins, elastin, and collagen by macrophages in culture. J Exp Med 1980;152:1527-1536.
    • (1980) J Exp Med , vol.152 , pp. 1527-1536
    • Jones, P.A.1    Werb, Z.2
  • 22
    • 0027474797 scopus 로고
    • Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells
    • Shi YE, Torri J, Yieh L, Wellstein A, Lippman ME, Dickson RB. Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells. Cancer Res 1993;53:1409-1415.
    • (1993) Cancer Res , vol.53 , pp. 1409-1415
    • Shi, Y.E.1    Torri, J.2    Yieh, L.3    Wellstein, A.4    Lippman, M.E.5    Dickson, R.B.6
  • 23
    • 0034714379 scopus 로고    scopus 로고
    • Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
    • Takeuchi T, Harris JL, Huang W, Yan KW, Coughlin SR, Craik CS. Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J Biol Chem 2000;275:26333-26342.
    • (2000) J Biol Chem , vol.275 , pp. 26333-26342
    • Takeuchi, T.1    Harris, J.L.2    Huang, W.3    Yan, K.W.4    Coughlin, S.R.5    Craik, C.S.6
  • 24
    • 0035081038 scopus 로고    scopus 로고
    • Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor
    • Benaud C, Dickson RB, Lin C-Y. Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor. Eur J Biochem 2001;268:1439-1447.
    • (2001) Eur J Biochem , vol.268 , pp. 1439-1447
    • Benaud, C.1    Dickson, R.B.2    Lin, C.-Y.3
  • 27
    • 63049086099 scopus 로고    scopus 로고
    • Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
    • Béliveau F, Désilets A, Leduc R. Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides. FEBS J 2009;276:2213-2226.
    • (2009) FEBS J , vol.276 , pp. 2213-2226
    • Béliveau, F.1    Désilets, A.2    Leduc, R.3
  • 28
    • 0033944447 scopus 로고    scopus 로고
    • Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases
    • Yana I, Weiss SJ. Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol Biol Cell 2000;11:2387-2401.
    • (2000) Mol Biol Cell , vol.11 , pp. 2387-2401
    • Yana, I.1    Weiss, S.J.2
  • 29
    • 33748644942 scopus 로고    scopus 로고
    • Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP
    • Remacle AG, Rozanov DV, Fugere M, Day R, Strongin AY. Furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP. Oncogene 2006;25:5648-5655.
    • (2006) Oncogene , vol.25 , pp. 5648-5655
    • Remacle, A.G.1    Rozanov, D.V.2    Fugere, M.3    Day, R.4    Strongin, A.Y.5
  • 30
    • 0022472015 scopus 로고
    • Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals
    • Mornex JF, Chytil-Weir A, Martinet Y, Courtney M, LeCocq JP, Crystal RG. Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals. J Clin Invest 1986;77:1952-1961.
    • (1986) J Clin Invest , vol.77 , pp. 1952-1961
    • Mornex, J.F.1    Chytil-Weir, A.2    Martinet, Y.3    Courtney, M.4    LeCocq, J.P.5    Crystal, R.G.6
  • 33
  • 34
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • Kroeger H, Miranda E, MacLeod I, Pérez J, Crowther DC, Marciniak SJ, Lomas DA. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J Biol Chem 2009;284:22793-22802.
    • (2009) J Biol Chem , vol.284 , pp. 22793-22802
    • Kroeger, H.1    Miranda, E.2    MacLeod, I.3    Pérez, J.4    Crowther, D.C.5    Marciniak, S.J.6    Lomas, D.A.7
  • 35
    • 28244499949 scopus 로고    scopus 로고
    • Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response
    • Hidvegi T, Schmidt BZ, Hale P, Perlmutter DH. Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response. J Biol Chem 2005;280:39002-39015.
    • (2005) J Biol Chem , vol.280 , pp. 39002-39015
    • Hidvegi, T.1    Schmidt, B.Z.2    Hale, P.3    Perlmutter, D.H.4
  • 36
    • 33748419472 scopus 로고    scopus 로고
    • The role of autophagy in alpha-1-antitrypsin deficiency: A specific cellular response in genetic diseases associated with aggregation-prone proteins
    • Perlmutter DH. The role of autophagy in alpha-1-antitrypsin deficiency: A specific cellular response in genetic diseases associated with aggregation-prone proteins. Autophagy 2006;2:258-263.
    • (2006) Autophagy , vol.2 , pp. 258-263
    • Perlmutter, D.H.1
  • 37
    • 2142768895 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z a 1-antitrypsin deficiency
    • Lawless MW, Greene CM, Mulgrew A, Taggart CC, O'Neill SJ, McElvaney NG. Activation of endoplasmic reticulum-specific stress responses associated with the conformational disease Z a 1-antitrypsin deficiency. J Immunol 2004;172:5722-5726.
    • (2004) J Immunol , vol.172 , pp. 5722-5726
    • Lawless, M.W.1    Greene, C.M.2    Mulgrew, A.3    Taggart, C.C.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 38
    • 77952770299 scopus 로고    scopus 로고
    • Evidence for unfolded protein response activation in monocytes from individuals with alpha-1 antitrypsin deficiency
    • Carroll TP, Greene CM, O'Connor CA, Nolan AM, O'Neill SJ, McElvaney NG. Evidence for unfolded protein response activation in monocytes from individuals with alpha-1 antitrypsin deficiency. J Immunol 2010;184:4538-4546.
    • (2010) J Immunol , vol.184 , pp. 4538-4546
    • Carroll, T.P.1    Greene, C.M.2    O'Connor, C.A.3    Nolan, A.M.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 39
    • 33847276695 scopus 로고    scopus 로고
    • In search of partners: Linking extracellular proteases to substrates
    • Overall CM, Blobel CP. In search of partners: Linking extracellular proteases to substrates. Nat Rev Mol Cell Biol 2007;8:245-257.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 245-257
    • Overall, C.M.1    Blobel, C.P.2
  • 40
    • 23844554460 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase by alpha1-protease inhibitor at the surface of human polymorphonuclear neutrophils
    • Korkmaz B, Attucci S, Jourdan ML, Juliano L, Gauthier F. Inhibition of neutrophil elastase by alpha1-protease inhibitor at the surface of human polymorphonuclear neutrophils. J Immunol 2005;175:3329-3338.
    • (2005) J Immunol , vol.175 , pp. 3329-3338
    • Korkmaz, B.1    Attucci, S.2    Jourdan, M.L.3    Juliano, L.4    Gauthier, F.5
  • 41
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen CA, Campbell MA, Sannes PL, Boukedes SS, Campbell EJ. Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J Cell Biol 1995;131:775-789.
    • (1995) J Cell Biol , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 43
    • 33750614146 scopus 로고    scopus 로고
    • Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase
    • Kilpatrick LM, Harris RL, Owen KA, Bass R, Ghorayeb C, Bar-Or A, Ellis V. Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase. Blood 2006;108:2616-2623.
    • (2006) Blood , vol.108 , pp. 2616-2623
    • Kilpatrick, L.M.1    Harris, R.L.2    Owen, K.A.3    Bass, R.4    Ghorayeb, C.5    Bar-Or, A.6    Ellis, V.7
  • 44
    • 5144234312 scopus 로고    scopus 로고
    • Addition of b1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin
    • Ihara S, Miyoshi E, Nakahara S, Sakiyama H, Ihara H, Akinaga A, Honke K, Dickson RB, Lin C-Y, Taniguchi N. Addition of b1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. Glycobiology 2004;14:139-146.
    • (2004) Glycobiology , vol.14 , pp. 139-146
    • Ihara, S.1    Miyoshi, E.2    Nakahara, S.3    Sakiyama, H.4    Ihara, H.5    Akinaga, A.6    Honke, K.7    Dickson, R.B.8    Lin, C.-Y.9    Taniguchi, N.10
  • 47
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: A potent modifier of pericellular microenvironment
    • Itoh Y, Seiki M. MT1-MMP: A potent modifier of pericellular microenvironment. J Cell Physiol 2006;206:1-8.
    • (2006) J Cell Physiol , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 48
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)
    • Osenkowski P, Toth M, Fridman R. Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP). J Cell Physiol 2004;200:2-10.
    • (2004) J Cell Physiol , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.