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Volumn 9, Issue 5, 2010, Pages 2347-2357

Proteomic analysis of plasma from patients undergoing coronary artery bypass grafting reveals a protease/antiprotease imbalance in favor of the serpin α1-antichymotrypsin

Author keywords

Coronary artery bypass grafting; Protease inhibitor; Proteases; Proteomics

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; APOLIPOPROTEIN E; CATHEPSIN G; CLUSTERIN; GLYCOPROTEIN; HAPTOGLOBIN; LEUCINE RICH ALPHA 2 GLYCOPROTEIN; PREALBUMIN; PROTEINASE; UNCLASSIFIED DRUG;

EID: 77952085953     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr901079v     Document Type: Article
Times cited : (15)

References (44)
  • 3
    • 17744412884 scopus 로고    scopus 로고
    • The past 50 years of cardiovascular surgery
    • Cooley, D. A.; Frazier, O. H. The past 50 years of cardiovascular surgery Circulation 2000, 102, IV87-93
    • (2000) Circulation , vol.102 , pp. 87-93
    • Cooley, D.A.1    Frazier, O.H.2
  • 4
    • 0035118319 scopus 로고    scopus 로고
    • Aprotinin and the systemic inflammatory response after cardiopulmonary bypass
    • Mojcik, C. F.; Levy, J. H. Aprotinin and the systemic inflammatory response after cardiopulmonary bypass Ann. Thorac. Surg. 2001, 71, 745-754
    • (2001) Ann. Thorac. Surg. , vol.71 , pp. 745-754
    • Mojcik, C.F.1    Levy, J.H.2
  • 5
    • 0035665697 scopus 로고    scopus 로고
    • The systemic factor: The comparative roles of cardiopulmonary bypass and off-pump surgery in the genesis of patient injury during and following cardiac surgery
    • Menasché, P. The systemic factor: the comparative roles of cardiopulmonary bypass and off-pump surgery in the genesis of patient injury during and following cardiac surgery Ann. Thorac. Surg. 2001, 72, S2260-2265
    • (2001) Ann. Thorac. Surg. , vol.72 , pp. 2260-2265
    • Menasché, P.1
  • 7
    • 0036305603 scopus 로고    scopus 로고
    • The systemic inflammatory response to cardiac surgery: Implications for the anesthesiologist
    • Laffey, J. G.; Boylan, J. F.; Cheng, D. C. The systemic inflammatory response to cardiac surgery: implications for the anesthesiologist Anesthesiology 2002, 97, 215-252
    • (2002) Anesthesiology , vol.97 , pp. 215-252
    • Laffey, J.G.1    Boylan, J.F.2    Cheng, D.C.3
  • 10
    • 0013895324 scopus 로고
    • Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies
    • Laurell, C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies Anal. Biochem. 1966, 15, 45-52
    • (1966) Anal. Biochem. , vol.15 , pp. 45-52
    • Laurell, C.B.1
  • 11
    • 0028816887 scopus 로고
    • Presence, activities, and molecular forms of cathepsin G, elastase, alpha 1-antitrypsin, and alpha1-antichymotrypsin in bronchiectasis
    • Sepper, R.; Konttinen, Y. T.; Ingman, T.; Sorsa, T. Presence, activities, and molecular forms of cathepsin G, elastase, alpha 1-antitrypsin, and alpha1-antichymotrypsin in bronchiectasis J. Clin. Immunol. 1995, 15, 27-34
    • (1995) J. Clin. Immunol. , vol.15 , pp. 27-34
    • Sepper, R.1    Konttinen, Y.T.2    Ingman, T.3    Sorsa, T.4
  • 12
    • 0023018786 scopus 로고
    • Alpha1-Antichymotrypsin in lung secretions is not an effective proteinase inhibitor
    • Berman, G.; Afford, S. C.; Burnett, D.; Stockley, R. A. alpha1-Antichymotrypsin in lung secretions is not an effective proteinase inhibitor J. Biol. Chem. 1986, 261, 14095-14099
    • (1986) J. Biol. Chem. , vol.261 , pp. 14095-14099
    • Berman, G.1    Afford, S.C.2    Burnett, D.3    Stockley, R.A.4
  • 13
    • 0033597961 scopus 로고    scopus 로고
    • Very low density lipoprotein-mediated signal transduction and plasminogen activator inhibitor type-1 in cultured HepG2 cells
    • Banfi, C.; Mussoni, L.; Risé, P.; Cattaneo, M. G.; Vicentini, L.; Battaini, F.; Galli, C.; Tremoli, E. Very low density lipoprotein-mediated signal transduction and plasminogen activator inhibitor type-1 in cultured HepG2 cells Circ. Res. 1999, 85, 208-217
    • (1999) Circ. Res. , vol.85 , pp. 208-217
    • Banfi, C.1    Mussoni, L.2    Risé, P.3    Cattaneo, M.G.4    Vicentini, L.5    Battaini, F.6    Galli, C.7    Tremoli, E.8
  • 15
    • 0018215999 scopus 로고
    • Human alpha-1-antichymotrypsin: Interaction with chymotrypsin-like proteinases
    • Travis, J.; Bowen, J.; Baugh, R. Human alpha-1-antichymotrypsin: interaction with chymotrypsin-like proteinases Biochemistry 1978, 17, 5651-5656
    • (1978) Biochemistry , vol.17 , pp. 5651-5656
    • Travis, J.1    Bowen, J.2    Baugh, R.3
  • 19
    • 16244397365 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Potential key regulators of cell signalling during inflammation
    • Wiedow, O.; Meyer-Hoffert, U. Neutrophil serine proteases: potential key regulators of cell signalling during inflammation J. Intern. Med. 2005, 257, 319-328
    • (2005) J. Intern. Med. , vol.257 , pp. 319-328
    • Wiedow, O.1    Meyer-Hoffert, U.2
  • 21
    • 0028890305 scopus 로고
    • Human coagulation factor v is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface
    • Allen, D. H.; Tracy, P. B. Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface J. Biol. Chem. 1995, 270, 1408-1415
    • (1995) J. Biol. Chem. , vol.270 , pp. 1408-1415
    • Allen, D.H.1    Tracy, P.B.2
  • 22
    • 0029961449 scopus 로고    scopus 로고
    • Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation
    • Plescia, J.; Altieri, D. C. Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation Biochem. J. 1996, 319, 873-879
    • (1996) Biochem. J. , vol.319 , pp. 873-879
    • Plescia, J.1    Altieri, D.C.2
  • 23
    • 38349162791 scopus 로고    scopus 로고
    • Cathepsin G, a leukocyte protease, activates coagulation factor VIII
    • Gale, A. J.; Rozenshteyn, D. Cathepsin G, a leukocyte protease, activates coagulation factor VIII Thromb. Haemost. 2008, 99, 44-51
    • (2008) Thromb. Haemost. , vol.99 , pp. 44-51
    • Gale, A.J.1    Rozenshteyn, D.2
  • 25
    • 0034634512 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase inhibition reverses platelet aggregation triggered by the combination of the neutrophil proteinases elastase and cathepsin G without impairing alpha(IIb)beta(3) integrin activation
    • Trumel, C.; Si-Tahar, M.; Balloy, V.; Chignard, M.; Chap, H.; Payrastre, B.; Plantavid, M.; Pidard, D. Phosphoinositide 3-kinase inhibition reverses platelet aggregation triggered by the combination of the neutrophil proteinases elastase and cathepsin G without impairing alpha(IIb)beta(3) integrin activation FEBS Lett. 2000, 484, 184-188
    • (2000) FEBS Lett. , vol.484 , pp. 184-188
    • Trumel, C.1    Si-Tahar, M.2    Balloy, V.3    Chignard, M.4    Chap, H.5    Payrastre, B.6    Plantavid, M.7    Pidard, D.8
  • 28
    • 0025614486 scopus 로고
    • Acute phase protein stimulation by alpha1-antichymotrypsin-cathepsin G complexes. Evidence for the involvement of interleukin-6
    • Kurdowska, A.; Travis, J. Acute phase protein stimulation by alpha1-antichymotrypsin-cathepsin G complexes. Evidence for the involvement of interleukin-6 J. Biol. Chem. 1990, 265, 21023-21026
    • (1990) J. Biol. Chem. , vol.265 , pp. 21023-21026
    • Kurdowska, A.1    Travis, J.2
  • 29
    • 33644745116 scopus 로고    scopus 로고
    • Cellular, molecular and immunological mechanisms in the pathophysiology of vein graft intimal hyperplasia
    • Mitra, A. K.; Gangahar, D. M.; Agrawal, D. K. Cellular, molecular and immunological mechanisms in the pathophysiology of vein graft intimal hyperplasia Immunol. Cell. Biol. 2006, 84, 115-124
    • (2006) Immunol. Cell. Biol. , vol.84 , pp. 115-124
    • Mitra, A.K.1    Gangahar, D.M.2    Agrawal, D.K.3
  • 30
    • 0141707669 scopus 로고    scopus 로고
    • Serum concentration of alpha1-proteinase inhibitor and alpha2-macroglobulin correlates with late lumen loss following coronary stent implantation
    • Ikari, Y.; Hashimoto, H.; Nakajima, H.; Hara, K. Serum concentration of alpha1-proteinase inhibitor and alpha2-macroglobulin correlates with late lumen loss following coronary stent implantation J. Thromb. Haemost. 2003, 1, 193-194
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 193-194
    • Ikari, Y.1    Hashimoto, H.2    Nakajima, H.3    Hara, K.4
  • 31
    • 0032502337 scopus 로고    scopus 로고
    • Aortocoronary saphenous vein graft disease: Pathogenesis, predisposition, and prevention
    • Motwani, J. G.; Topol, E. J. Aortocoronary saphenous vein graft disease: pathogenesis, predisposition, and prevention Circulation 1998, 97, 916-931
    • (1998) Circulation , vol.97 , pp. 916-931
    • Motwani, J.G.1    Topol, E.J.2
  • 32
    • 33947609131 scopus 로고    scopus 로고
    • Clinical indications for plasma protein assays: Transthyretin (prealbumin) in inflammation and malnutrition
    • Myron Johnson, A.; Merlini, G.; Sheldon, J.; Ichihara, K. Clinical indications for plasma protein assays: transthyretin (prealbumin) in inflammation and malnutrition Clin. Chem. Lab. Med. 2007, 45, 419-426
    • (2007) Clin. Chem. Lab. Med. , vol.45 , pp. 419-426
    • Myron Johnson, A.1    Merlini, G.2    Sheldon, J.3    Ichihara, K.4
  • 33
    • 0036914688 scopus 로고    scopus 로고
    • Assessment of nutritional status in organ transplant: Is transthyretin a reliable indicator
    • Raguso, C. A.; Genton, L.; Dupertuis, Y. M.; Pichard, C. Assessment of nutritional status in organ transplant: is transthyretin a reliable indicator Clin. Chem. Lab. Med. 2002, 40, 1325-1328
    • (2002) Clin. Chem. Lab. Med. , vol.40 , pp. 1325-1328
    • Raguso, C.A.1    Genton, L.2    Dupertuis, Y.M.3    Pichard, C.4
  • 35
    • 0036745069 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of leucine-rich alpha2-glycoprotein, a novel marker of granulocytic differentiation
    • ODonnell, L. C.; Druhan, L. J.; Avalos, B. R. Molecular characterization and expression analysis of leucine-rich alpha2-glycoprotein, a novel marker of granulocytic differentiation J. Leukoc. Biol. 2002, 72, 478-485
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 478-485
    • Odonnell, L.C.1    Druhan, L.J.2    Avalos, B.R.3
  • 36
    • 0037312501 scopus 로고    scopus 로고
    • Inflammatory response to cardiopulmonary bypass
    • Levy, J. H.; Tanaka, K. A. Inflammatory response to cardiopulmonary bypass Ann. Thorac. Surg. 2003, 75 S715-720
    • (2003) Ann. Thorac. Surg. , vol.75
    • Levy, J.H.1    Tanaka, K.A.2
  • 39
    • 0034849342 scopus 로고    scopus 로고
    • Haemolysis during cardiopulmonary bypass:update
    • Wright, G. Haemolysis during cardiopulmonary bypass:update Perfusion 2001, 16, 345-351
    • (2001) Perfusion , vol.16 , pp. 345-351
    • Wright, G.1
  • 42
    • 0033866873 scopus 로고    scopus 로고
    • Effects of new polymer-coated extracorporeal circuits on biocompatibility during cardiopulmonary bypass
    • Saito, N.; Motoyama, S.; Sawamoto, J. Effects of new polymer-coated extracorporeal circuits on biocompatibility during cardiopulmonary bypass Artif. Organs 2000, 24, 547-554
    • (2000) Artif. Organs , vol.24 , pp. 547-554
    • Saito, N.1    Motoyama, S.2    Sawamoto, J.3
  • 43
    • 28544437885 scopus 로고    scopus 로고
    • Quality control of protein folding in extracellular space
    • Yerbury, J. J.; Stewart, E. M.; Wyatt, A. R.; Wilson, M. R. Quality control of protein folding in extracellular space EMBO Rep. 2005, 6, 1131-1136
    • (2005) EMBO Rep. , vol.6 , pp. 1131-1136
    • Yerbury, J.J.1    Stewart, E.M.2    Wyatt, A.R.3    Wilson, M.R.4
  • 44
    • 0034575124 scopus 로고    scopus 로고
    • Apolipoprotein E: Far more than a lipid transport protein
    • Mahley, R. W.; Rall, S. C. Apolipoprotein E: far more than a lipid transport protein Annu. Rev. Genomics Hum. Genet. 2000, 1, 507-537
    • (2000) Annu. Rev. Genomics Hum. Genet. , vol.1 , pp. 507-537
    • Mahley, R.W.1    Rall, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.