메뉴 건너뛰기




Volumn 294, Issue 3, 2008, Pages

Cleavage of high-molecular-weight kininogen by elastase and tryptase is inhibited by ferritin

Author keywords

Bradykinin; Inflammation

Indexed keywords

APOFERRITIN; ELASTASE; FERRITIN; HIGH MOLECULAR WEIGHT KININOGEN; TRYPTASE;

EID: 41549140461     PISSN: 10400605     EISSN: 15221504     Source Type: Journal    
DOI: 10.1152/ajplung.00347.2007     Document Type: Article
Times cited : (40)

References (57)
  • 1
    • 34547693434 scopus 로고    scopus 로고
    • Myeloperoxidase interacts with endothelial cellsurface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system
    • Astern JM, Pendergraft WF 3rd, Falk RJ, Jennette JC, Schmaier AH, Mahdi F, Preston GA. Myeloperoxidase interacts with endothelial cellsurface cytokeratin 1 and modulates bradykinin production by the plasma Kallikrein-Kinin system. Am J Pathol 171: 349-360, 2007.
    • (2007) Am J Pathol , vol.171 , pp. 349-360
    • Astern, J.M.1    Pendergraft 3rd, W.F.2    Falk, R.J.3    Jennette, J.C.4    Schmaier, A.H.5    Mahdi, F.6    Preston, G.A.7
  • 2
    • 0026795798 scopus 로고
    • Effect of bradykinin on airway function
    • Barnes PJ. Effect of bradykinin on airway function. Agents Actions Suppl 38: 432-438, 1992.
    • (1992) Agents Actions Suppl , vol.38 , pp. 432-438
    • Barnes, P.J.1
  • 3
    • 0032445151 scopus 로고    scopus 로고
    • Inflammatory mediators of asthma: An update
    • Barnes PJ, Chung KF, Page CP. Inflammatory mediators of asthma: an update. Pharmacol Rev 50: 515-596, 1998.
    • (1998) Pharmacol Rev , vol.50 , pp. 515-596
    • Barnes, P.J.1    Chung, K.F.2    Page, C.P.3
  • 4
    • 0024430531 scopus 로고
    • Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity
    • Campbell EJ, Silverman EK, Campbell MA. Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity. J Immunol 143: 2961-2968, 1989.
    • (1989) J Immunol , vol.143 , pp. 2961-2968
    • Campbell, E.J.1    Silverman, E.K.2    Campbell, M.A.3
  • 5
    • 0027189793 scopus 로고
    • Regulation of kininogen gene expression and localization in the lung after monocrotaline-induced pulmonary hypertension in rats
    • Chao J, Simson JA, Chung P, Chen LM, Chao L. Regulation of kininogen gene expression and localization in the lung after monocrotaline-induced pulmonary hypertension in rats. Proc Soc Exp Biol Med 203: 243-250, 1993.
    • (1993) Proc Soc Exp Biol Med , vol.203 , pp. 243-250
    • Chao, J.1    Simson, J.A.2    Chung, P.3    Chen, L.M.4    Chao, L.5
  • 8
    • 0026557831 scopus 로고
    • Elevation of tissue kallikrein and kinin in the airways of asthmatic subjects after endobronchial allergen challenge
    • Christiansen SC, Proud D, Sarnoff RB, Juergens U, Cochrane CG, Zuraw BL. Elevation of tissue kallikrein and kinin in the airways of asthmatic subjects after endobronchial allergen challenge. Am Rev Respir Dis 145: 900-905, 1992.
    • (1992) Am Rev Respir Dis , vol.145 , pp. 900-905
    • Christiansen, S.C.1    Proud, D.2    Sarnoff, R.B.3    Juergens, U.4    Cochrane, C.G.5    Zuraw, B.L.6
  • 9
    • 0020021627 scopus 로고
    • The biochemistry and pathophysiology of the contact system of plasma
    • Cochrane CG, Griffin JH. The biochemistry and pathophysiology of the contact system of plasma. Adv Immunol 33: 241-306, 1982.
    • (1982) Adv Immunol , vol.33 , pp. 241-306
    • Cochrane, C.G.1    Griffin, J.H.2
  • 10
    • 41549134888 scopus 로고    scopus 로고
    • Colman RW. Contact activation pathway: inflammatory, fibrinolytic, anticoagulation, antiadhesive, and antiangiogenic activities. In: Hemostasis and Thrombosis: Basic Principles and Clinical Practice, edited by Colman RW, Hirsh J, Marder VJ, Salzman EW. Philadelphia: Lippincott, 1998, p. 1567-1583.
    • Colman RW. Contact activation pathway: inflammatory, fibrinolytic, anticoagulation, antiadhesive, and antiangiogenic activities. In: Hemostasis and Thrombosis: Basic Principles and Clinical Practice, edited by Colman RW, Hirsh J, Marder VJ, Salzman EW. Philadelphia: Lippincott, 1998, p. 1567-1583.
  • 11
    • 0030830360 scopus 로고    scopus 로고
    • Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes
    • Colman RW, Schmaier AH. Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood 90: 3819-3843, 1997.
    • (1997) Blood , vol.90 , pp. 3819-3843
    • Colman, R.W.1    Schmaier, A.H.2
  • 12
    • 0032746388 scopus 로고    scopus 로고
    • Role of the kallikrein-kinin system in the maturation of cardiovascular phenotype
    • Emanueli C, Madeddu P. Role of the kallikrein-kinin system in the maturation of cardiovascular phenotype. Am J Hypertens 12: 988-999, 1999.
    • (1999) Am J Hypertens , vol.12 , pp. 988-999
    • Emanueli, C.1    Madeddu, P.2
  • 14
    • 21644457354 scopus 로고    scopus 로고
    • Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells
    • Fernando AN, Fernando LP, Fukuda Y, Kaplan AP. Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells. Am J Physiol Heart Circ Physiol 289: H251-H257, 2005.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Fernando, A.N.1    Fernando, L.P.2    Fukuda, Y.3    Kaplan, A.P.4
  • 19
    • 0034825602 scopus 로고    scopus 로고
    • Zinc-dependent conformational changes in domain D5 of high molecular mass kininogen modulate contact activation
    • Herwald H, Morgelin M, Svensson HG, Sjobring U. Zinc-dependent conformational changes in domain D5 of high molecular mass kininogen modulate contact activation. Eur J Biochem/FEBS 268: 396-404, 2001.
    • (2001) Eur J Biochem/FEBS , vol.268 , pp. 396-404
    • Herwald, H.1    Morgelin, M.2    Svensson, H.G.3    Sjobring, U.4
  • 20
    • 0024334658 scopus 로고
    • Coagulation, fibrinolysis, and kallikrein systems in sepsis: Relation to outcome
    • Hesselvik JF, Blomback M, Brodin B, Maller R. Coagulation, fibrinolysis, and kallikrein systems in sepsis: relation to outcome. Crit Care Med 17: 724-733, 1989.
    • (1989) Crit Care Med , vol.17 , pp. 724-733
    • Hesselvik, J.F.1    Blomback, M.2    Brodin, B.3    Maller, R.4
  • 21
    • 0036297145 scopus 로고    scopus 로고
    • Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase
    • Imamura T, Tanase S, Hayashi I, Potempa J, Kozik A, Travis J. Release of a new vascular permeability enhancing peptide from kininogens by human neutrophil elastase. Biochem Biophys Res Commun 294: 423-428, 2002.
    • (2002) Biochem Biophys Res Commun , vol.294 , pp. 423-428
    • Imamura, T.1    Tanase, S.2    Hayashi, I.3    Potempa, J.4    Kozik, A.5    Travis, J.6
  • 23
    • 0021871268 scopus 로고
    • Activation and inhibition of Hageman factor-dependent pathways and the complement system in uncomplicated bacteremia or bacterial shock
    • Kalter ES, Daha MR, ten Cate JW, Verhoef J, Bouma BN. Activation and inhibition of Hageman factor-dependent pathways and the complement system in uncomplicated bacteremia or bacterial shock. J Infect Dis 151: 1019-1027, 1985.
    • (1985) J Infect Dis , vol.151 , pp. 1019-1027
    • Kalter, E.S.1    Daha, M.R.2    ten Cate, J.W.3    Verhoef, J.4    Bouma, B.N.5
  • 25
    • 0032509201 scopus 로고    scopus 로고
    • A novel mechanism for bradykinin production at inflammatory sites. Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versus tissue and plasma kallikreins on native and oxidized kininogens
    • Kozik A, Moore RB, Potempa J, Imamura T, Rapala-Kozik M, Travis J. A novel mechanism for bradykinin production at inflammatory sites. Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versus tissue and plasma kallikreins on native and oxidized kininogens. J Biol Chem 273: 33224-33229, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 33224-33229
    • Kozik, A.1    Moore, R.B.2    Potempa, J.3    Imamura, T.4    Rapala-Kozik, M.5    Travis, J.6
  • 26
    • 33644634175 scopus 로고    scopus 로고
    • Foam cell death induced by 7beta-hydroxycholesterol is mediated by labile iron-driven oxidative injury: Mechanisms underlying induction of ferritin in human atheroma
    • Li W, Hellsten A, Xu LH, Zhuang DM, Jansson K, Brunk UT, Yuan XM. Foam cell death induced by 7beta-hydroxycholesterol is mediated by labile iron-driven oxidative injury: mechanisms underlying induction of ferritin in human atheroma. Free Radic Biol Med 39: 864-875, 2005.
    • (2005) Free Radic Biol Med , vol.39 , pp. 864-875
    • Li, W.1    Hellsten, A.2    Xu, L.H.3    Zhuang, D.M.4    Jansson, K.5    Brunk, U.T.6    Yuan, X.M.7
  • 27
  • 28
    • 0028903558 scopus 로고
    • Human mast cell tryptase isoforms: Separation and examination of substrate-specificity differences
    • Little SS, Johnson DA. Human mast cell tryptase isoforms: separation and examination of substrate-specificity differences. Biochem J 307: 341-346, 1995.
    • (1995) Biochem J , vol.307 , pp. 341-346
    • Little, S.S.1    Johnson, D.A.2
  • 29
    • 0242415187 scopus 로고    scopus 로고
    • The relative priority of prekallikrein and factors XI/XIa assembly on cultured endothelial cells
    • Mahdi F, Shariat-Madar Z, Schmaier AH. The relative priority of prekallikrein and factors XI/XIa assembly on cultured endothelial cells. J Biol Chem 278: 43983-43990, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 43983-43990
    • Mahdi, F.1    Shariat-Madar, Z.2    Schmaier, A.H.3
  • 30
    • 0020627947 scopus 로고
    • Inactivation of human high molecular weight kininogen by human mast cell tryptase
    • Maier M, Spragg J, Schwartz LB. Inactivation of human high molecular weight kininogen by human mast cell tryptase. J Immunol 130: 2352-2356, 1983.
    • (1983) J Immunol , vol.130 , pp. 2352-2356
    • Maier, M.1    Spragg, J.2    Schwartz, L.B.3
  • 31
    • 0033770564 scopus 로고    scopus 로고
    • Kinin B(1) receptors and the cardiovascular system: Regulation of expression and function
    • McLean PG, Perretti M, Ahluwalia A. Kinin B(1) receptors and the cardiovascular system: regulation of expression and function. Cardiovasc Res 48: 194-210, 2000.
    • (2000) Cardiovasc Res , vol.48 , pp. 194-210
    • McLean, P.G.1    Perretti, M.2    Ahluwalia, A.3
  • 34
    • 0036646141 scopus 로고    scopus 로고
    • Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release
    • Parthasarathy N, Torti SV, Torti FM. Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release. Biochem J 365: 279-286, 2002.
    • (2002) Biochem J , vol.365 , pp. 279-286
    • Parthasarathy, N.1    Torti, S.V.2    Torti, F.M.3
  • 36
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567, 1999.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 37
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka P, Beaumont C, Richardson DR. Function and regulation of transferrin and ferritin. Semin Hematol 35: 35-54, 1998.
    • (1998) Semin Hematol , vol.35 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 38
    • 0033954194 scopus 로고    scopus 로고
    • High-molecular-weight kininogen is a binding protein for tissue prokallikrein
    • Raab A, Kemme M. High-molecular-weight kininogen is a binding protein for tissue prokallikrein. FEBS Lett 467: 165-168, 2000.
    • (2000) FEBS Lett , vol.467 , pp. 165-168
    • Raab, A.1    Kemme, M.2
  • 39
    • 0031255314 scopus 로고    scopus 로고
    • Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12
    • Ren S, Lawson AE, Carr M, Baumgarten CM, Schwartz LB. Human tryptase fibrinogenolysis is optimal at acidic pH and generates anticoagulant fragments in the presence of the anti-tryptase monoclonal antibody B12. J Immunol 159: 3540-3548, 1997.
    • (1997) J Immunol , vol.159 , pp. 3540-3548
    • Ren, S.1    Lawson, A.E.2    Carr, M.3    Baumgarten, C.M.4    Schwartz, L.B.5
  • 40
    • 0017732786 scopus 로고
    • Elastase release from human alveolar macrophages: Comparison between smokers and nonsmokers
    • Rodriguez RJ, White RR, Senior RM, Levine EA. Elastase release from human alveolar macrophages: comparison between smokers and nonsmokers. Science 198: 313-314, 1977.
    • (1977) Science , vol.198 , pp. 313-314
    • Rodriguez, R.J.1    White, R.R.2    Senior, R.M.3    Levine, E.A.4
  • 41
    • 0023797442 scopus 로고
    • The expression of high molecular weight kininogen on human umbilical vein endothelial cells
    • Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB. The expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 263: 16327-16333, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 16327-16333
    • Schmaier, A.H.1    Kuo, A.2    Lundberg, D.3    Murray, S.4    Cines, D.B.5
  • 42
    • 0022388692 scopus 로고
    • The fibrinogenolytic activity of purified tryptase from human lung mast cells
    • Schwartz LB, Bradford TR, Littman BH, Wintroub BU. The fibrinogenolytic activity of purified tryptase from human lung mast cells. J Immunol 135: 2762-2767, 1985.
    • (1985) J Immunol , vol.135 , pp. 2762-2767
    • Schwartz, L.B.1    Bradford, T.R.2    Littman, B.H.3    Wintroub, B.U.4
  • 43
    • 7244239304 scopus 로고    scopus 로고
    • Therapeutic prospects for bradykinin receptor agonists in the treatment of cardiovascular diseases
    • Sharma JN, Thani RB. Therapeutic prospects for bradykinin receptor agonists in the treatment of cardiovascular diseases. IDrugs 7: 926-934, 2004.
    • (2004) IDrugs , vol.7 , pp. 926-934
    • Sharma, J.N.1    Thani, R.B.2
  • 44
    • 32344431514 scopus 로고    scopus 로고
    • Kinin- and angiotensin-converting enzyme (ACE) inhibitor-mediated nitric oxide production in endothelial cells
    • Skidgel RA, Stanisavljevic S, Erdos EG. Kinin- and angiotensin-converting enzyme (ACE) inhibitor-mediated nitric oxide production in endothelial cells. Biol Chem 387: 159-165, 2006.
    • (2006) Biol Chem , vol.387 , pp. 159-165
    • Skidgel, R.A.1    Stanisavljevic, S.2    Erdos, E.G.3
  • 48
    • 0035997492 scopus 로고    scopus 로고
    • Expression of ferritin, transferrin receptor, and non-specific resistance associated macrophage proteins 1 and 2 (Nramp1 and Nramp2) in the human rheumatoid synovium
    • Telfer JF, Brock JH. Expression of ferritin, transferrin receptor, and non-specific resistance associated macrophage proteins 1 and 2 (Nramp1 and Nramp2) in the human rheumatoid synovium. Ann Rheum Dis 61: 741-744, 2002.
    • (2002) Ann Rheum Dis , vol.61 , pp. 741-744
    • Telfer, J.F.1    Brock, J.H.2
  • 49
    • 0032562226 scopus 로고    scopus 로고
    • Human mast cell tryptase fibrinogenolysis: Kinetics, anticoagulation mechanism, and cell adhesion disruption
    • Thomas VA, Wheeless CJ, Stack MS, Johnson DA. Human mast cell tryptase fibrinogenolysis: kinetics, anticoagulation mechanism, and cell adhesion disruption. Biochemistry 37: 2291-2298, 1998.
    • (1998) Biochemistry , vol.37 , pp. 2291-2298
    • Thomas, V.A.1    Wheeless, C.J.2    Stack, M.S.3    Johnson, D.A.4
  • 50
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti FM, Torti SV. Regulation of ferritin genes and protein. Blood 99: 3505-3516, 2002.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 51
    • 0032577485 scopus 로고    scopus 로고
    • Human H-kininogen is a ferritin-binding protein
    • Torti SV, Torti FM. Human H-kininogen is a ferritin-binding protein. J Biol Chem 273: 13630-13635, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 13630-13635
    • Torti, S.V.1    Torti, F.M.2
  • 53
    • 0024208268 scopus 로고
    • Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions
    • Vogel R, Assfalg-Machleidt I, Esterl A, Machleidt W, Muller-Esterl W. Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions. J Biol Chem 263: 12661-12668, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 12661-12668
    • Vogel, R.1    Assfalg-Machleidt, I.2    Esterl, A.3    Machleidt, W.4    Muller-Esterl, W.5
  • 56
    • 0035199853 scopus 로고    scopus 로고
    • Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100
    • Yang C, Wang J, Krutchinsky AN, Chait BT, Morrisett JD, Smith CV. Selective oxidation in vitro by myeloperoxidase of the N-terminal amine in apolipoprotein B-100. J Lipid Res 42: 1891-1896, 2001.
    • (2001) J Lipid Res , vol.42 , pp. 1891-1896
    • Yang, C.1    Wang, J.2    Krutchinsky, A.N.3    Chait, B.T.4    Morrisett, J.D.5    Smith, C.V.6
  • 57
    • 0036369436 scopus 로고    scopus 로고
    • Neshkova Contact system EA. New concepts on activation mechanisms and bioregulatory functions
    • Yarovaya GA, Blokhina TB, Neshkova Contact system EA. New concepts on activation mechanisms and bioregulatory functions. Biochemistry 67: 13-24, 2002.
    • (2002) Biochemistry , vol.67 , pp. 13-24
    • Yarovaya, G.A.1    Blokhina, T.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.