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Volumn 303, Issue 2, 2011, Pages 118-127

Molecular competition between plasminogen activator inhibitors type -1 and -2 for urokinase: Implications for cellular proteolysis and adhesion in cancer

Author keywords

Adhesion; Migration; PAI 1 SERPINE1; PAI 2 SERPINB2; Urokinase

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1; PLASMINOGEN ACTIVATOR INHIBITOR 2; SERINE PROTEINASE INHIBITOR; UROKINASE; VITRONECTIN;

EID: 79952041524     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2011.01.018     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 77951883821 scopus 로고    scopus 로고
    • The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling
    • Blasi F., Sidenius N. The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling. FEBS Lett. 2009, 584:1923-1930.
    • (2009) FEBS Lett. , vol.584 , pp. 1923-1930
    • Blasi, F.1    Sidenius, N.2
  • 2
    • 0037622867 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility
    • Kjoller L. The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility. Biol. Chem. 2002, 383:5-19.
    • (2002) Biol. Chem. , vol.383 , pp. 5-19
    • Kjoller, L.1
  • 3
    • 0042895837 scopus 로고    scopus 로고
    • Plasminogen binding and cancer: promises and pitfalls
    • Ranson M., Andronicos N.M. Plasminogen binding and cancer: promises and pitfalls. Front Biosci. 2003, 8:s294-s304.
    • (2003) Front Biosci. , vol.8
    • Ranson, M.1    Andronicos, N.M.2
  • 4
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: diversity and escape mechanisms
    • Friedl P., Wolf K. Tumour-cell invasion and migration: diversity and escape mechanisms. Nat. Rev. Cancer 2003, 3:362-374.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 5
    • 63049104211 scopus 로고    scopus 로고
    • Microenvironmental regulation of metastasis
    • Joyce J.A., Pollard J.W. Microenvironmental regulation of metastasis. Nat. Rev. Cancer 2009, 9:239-252.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 239-252
    • Joyce, J.A.1    Pollard, J.W.2
  • 7
    • 0025288990 scopus 로고
    • Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors
    • Ellis V., Wun T.C., Behrendt N., Ronne E., Dano K. Inhibition of receptor-bound urokinase by plasminogen-activator inhibitors. J. Biol. Chem. 1990, 265:9904-9908.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9904-9908
    • Ellis, V.1    Wun, T.C.2    Behrendt, N.3    Ronne, E.4    Dano, K.5
  • 8
    • 36749093009 scopus 로고    scopus 로고
    • A structural basis for differential cell signalling by PAI-1 and PAI-2 in breast cancer cells
    • Croucher D.R., Saunders D.N., Stillfried G.E., Ranson M. A structural basis for differential cell signalling by PAI-1 and PAI-2 in breast cancer cells. Biochem. J. 2007, 408:203-210.
    • (2007) Biochem. J. , vol.408 , pp. 203-210
    • Croucher, D.R.1    Saunders, D.N.2    Stillfried, G.E.3    Ranson, M.4
  • 9
    • 33744512466 scopus 로고    scopus 로고
    • The urokinase/PAI-2 complex - a new high affinity ligand for the endocytosis receptor low density lipoprotein receptor-related protein
    • Croucher D., Saunders D.N., Ranson M. The urokinase/PAI-2 complex - a new high affinity ligand for the endocytosis receptor low density lipoprotein receptor-related protein. J. Biol. Chem. 2006, 281:10206-10213.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10206-10213
    • Croucher, D.1    Saunders, D.N.2    Ranson, M.3
  • 10
    • 0141832797 scopus 로고    scopus 로고
    • Diverse role of LDL receptor-related protein in the clearance of proteases and in signaling
    • Strickland D.K., Ranganathan S. Diverse role of LDL receptor-related protein in the clearance of proteases and in signaling. J. Thromb. Haemost. 2003, 1:1663-1670.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1663-1670
    • Strickland, D.K.1    Ranganathan, S.2
  • 11
  • 12
    • 34247569975 scopus 로고    scopus 로고
    • Does the urokinase receptor exist in a latent form?
    • Yuan C., Huang M. Does the urokinase receptor exist in a latent form?. Cell Mol. Life Sci. 2007, 64:1033-1037.
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 1033-1037
    • Yuan, C.1    Huang, M.2
  • 13
    • 34250318934 scopus 로고    scopus 로고
    • Mapping of the vitronectin-binding site on the urokinase receptor: involvement of a coherent receptor interface consisting of residues from both domain I and the flanking interdomain linker region
    • Gardsvoll H., Ploug M. Mapping of the vitronectin-binding site on the urokinase receptor: involvement of a coherent receptor interface consisting of residues from both domain I and the flanking interdomain linker region. J. Biol. Chem. 2007, 282:13561-13572.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13561-13572
    • Gardsvoll, H.1    Ploug, M.2
  • 16
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • Kjoller L., Kanse S.M., Kirkegaard T., Rodenburg K.W., Ronne E., Goodman S.L., Preissner K.T., Ossowski L., Andreasen P.A. Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation. Exp. Cell Res. 1997, 232:420-429.
    • (1997) Exp. Cell Res. , vol.232 , pp. 420-429
    • Kjoller, L.1    Kanse, S.M.2    Kirkegaard, T.3    Rodenburg, K.W.4    Ronne, E.5    Goodman, S.L.6    Preissner, K.T.7    Ossowski, L.8    Andreasen, P.A.9
  • 17
    • 0042304087 scopus 로고    scopus 로고
    • Old dogs and new tricks: proteases, inhibitors, and cell migration
    • Stefansson S., Lawrence D.A. Old dogs and new tricks: proteases, inhibitors, and cell migration. Sci. STKE 2003, 2003:pe24.
    • (2003) Sci. STKE , vol.2003
    • Stefansson, S.1    Lawrence, D.A.2
  • 18
    • 0037416209 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins
    • Czekay R.P., Aertgeerts K., Curriden S.A., Loskutoff D.J. Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins. J. Cell Biol. 2003, 160:781-791.
    • (2003) J. Cell Biol. , vol.160 , pp. 781-791
    • Czekay, R.P.1    Aertgeerts, K.2    Curriden, S.A.3    Loskutoff, D.J.4
  • 20
    • 33846804080 scopus 로고    scopus 로고
    • Preclinical evaluation of Bi-213-labeled plasminogen activator inhibitor type 2 in an orthotopic murine xenogenic model of human breast carcinoma
    • Stutchbury T.K., Al-Ejeh F., Stillfried G.E., Croucher D.R., Andrews J., Irving D., Links M., Ranson M. Preclinical evaluation of Bi-213-labeled plasminogen activator inhibitor type 2 in an orthotopic murine xenogenic model of human breast carcinoma. Mol. Cancer Therap. 2007, 6:203-212.
    • (2007) Mol. Cancer Therap. , vol.6 , pp. 203-212
    • Stutchbury, T.K.1    Al-Ejeh, F.2    Stillfried, G.E.3    Croucher, D.R.4    Andrews, J.5    Irving, D.6    Links, M.7    Ranson, M.8
  • 21
    • 0031759137 scopus 로고    scopus 로고
    • Pharmacokinetics of recombinant human plasminogen activator inhibitor type 2 (PAI-2) in control and tumour xenograft bearing mice
    • Hang M.T.N., Ranson M., Saunders D.N., Liang X.M., Bunn C.L., Baker M.S. Pharmacokinetics of recombinant human plasminogen activator inhibitor type 2 (PAI-2) in control and tumour xenograft bearing mice. Fibrinolysis 1998, 12:145-154.
    • (1998) Fibrinolysis , vol.12 , pp. 145-154
    • Hang, M.T.N.1    Ranson, M.2    Saunders, D.N.3    Liang, X.M.4    Bunn, C.L.5    Baker, M.S.6
  • 22
    • 67549102402 scopus 로고    scopus 로고
    • The CD-loop of PAI-2 (SERPINB2) is redundant in the targeting, inhibition and clearance of cell surface uPA activity
    • Cochran B.J., Gunawardhana L.P., Vine K.L., Lee J.A., Lobov S., Ranson M. The CD-loop of PAI-2 (SERPINB2) is redundant in the targeting, inhibition and clearance of cell surface uPA activity. BMC Biotechnol. 2009, 9:43.
    • (2009) BMC Biotechnol. , vol.9 , pp. 43
    • Cochran, B.J.1    Gunawardhana, L.P.2    Vine, K.L.3    Lee, J.A.4    Lobov, S.5    Ranson, M.6
  • 23
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas M.B., Lawrence D.A., Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J. 1995, 14:2969-2977.
    • (1995) EMBO J. , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 24
    • 27144501119 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution - implications for serpin mechanistic model and prediction of nsSNP activities
    • Di Giusto D.A., Sutherland A.P., Jankova L., Harrop S.J., Curmi P.M., King G.C. Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution - implications for serpin mechanistic model and prediction of nsSNP activities. J. Mol. Biol. 2005, 353:1069-1080.
    • (2005) J. Mol. Biol. , vol.353 , pp. 1069-1080
    • Di Giusto, D.A.1    Sutherland, A.P.2    Jankova, L.3    Harrop, S.J.4    Curmi, P.M.5    King, G.C.6
  • 25
    • 2942551117 scopus 로고    scopus 로고
    • Kinetic analysis of plasminogen activator inhibitor type-2: urokinase complex formation and subsequent internalisation by carcinoma cell lines
    • Al-Ejeh F., Croucher D., Ranson M. Kinetic analysis of plasminogen activator inhibitor type-2: urokinase complex formation and subsequent internalisation by carcinoma cell lines. Exp. Cell Res. 2004, 297:259-271.
    • (2004) Exp. Cell Res. , vol.297 , pp. 259-271
    • Al-Ejeh, F.1    Croucher, D.2    Ranson, M.3
  • 26
    • 48949088564 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type 2 inhibits cell surface associated tissue plasminogen activator in vitro: potential receptor interactions
    • Lobov S., Croucher D.R., Saunders D.N., Ranson M. Plasminogen activator inhibitor type 2 inhibits cell surface associated tissue plasminogen activator in vitro: potential receptor interactions. Thromb. Haemost. 2008, 100:319-329.
    • (2008) Thromb. Haemost. , vol.100 , pp. 319-329
    • Lobov, S.1    Croucher, D.R.2    Saunders, D.N.3    Ranson, M.4
  • 27
    • 0027174189 scopus 로고
    • The CD-loop of PAI-2 (SERPINB2) is redundant in the targeting, inhibition and clearance of cell surface uPA activity
    • Waltz D.A., Sailor L.Z., Chapman H.A. The CD-loop of PAI-2 (SERPINB2) is redundant in the targeting, inhibition and clearance of cell surface uPA activity. J. Clin. Invest. 1993, 91:1541-1552.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1541-1552
    • Waltz, D.A.1    Sailor, L.Z.2    Chapman, H.A.3
  • 29
    • 0031972273 scopus 로고    scopus 로고
    • Increased plasminogen binding is associated with metastatic breast cancer cells: differential expression of plasminogen binding proteins
    • Ranson M., Andronicos N.M., O'Mullane M.J., Baker M.S. Increased plasminogen binding is associated with metastatic breast cancer cells: differential expression of plasminogen binding proteins. Br. J. Cancer 1998, 77:1586-1597.
    • (1998) Br. J. Cancer , vol.77 , pp. 1586-1597
    • Ranson, M.1    Andronicos, N.M.2    O'Mullane, M.J.3    Baker, M.S.4
  • 32
    • 67449123333 scopus 로고    scopus 로고
    • Extracellular engagement of alpha6 integrin inhibited urokinase-type plasminogen activator-mediated cleavage and delayed human prostate bone metastasis
    • Ports M.O., Nagle R.B., Pond G.D., Cress A.E. Extracellular engagement of alpha6 integrin inhibited urokinase-type plasminogen activator-mediated cleavage and delayed human prostate bone metastasis. Cancer Res. 2009, 69:5007-5014.
    • (2009) Cancer Res. , vol.69 , pp. 5007-5014
    • Ports, M.O.1    Nagle, R.B.2    Pond, G.D.3    Cress, A.E.4
  • 33
    • 18844375381 scopus 로고    scopus 로고
    • Pleiotropic functions of plasminogen activator inhibitor-1
    • Lijnen H.R. Pleiotropic functions of plasminogen activator inhibitor-1. J. Thromb. Haemost. 2005, 3:35-45.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 35-45
    • Lijnen, H.R.1
  • 34
    • 0037967300 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 in tumor growth, angiogenesis and vascular remodeling
    • Stefansson S., McMahon G.A., Petitclerc E., Lawrence D.A. Plasminogen activator inhibitor-1 in tumor growth, angiogenesis and vascular remodeling. Curr. Pharm. Des. 2003, 9:1545-1564.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1545-1564
    • Stefansson, S.1    McMahon, G.A.2    Petitclerc, E.3    Lawrence, D.A.4
  • 35
    • 0031728717 scopus 로고    scopus 로고
    • Significance of the plasminogen activator inhibitor of placental type (PAI-2) in pregnancy
    • Astedt B., Lindoff C., Lecander I. Significance of the plasminogen activator inhibitor of placental type (PAI-2) in pregnancy. Semin. Thromb. Hemost. 1998, 24:431-435.
    • (1998) Semin. Thromb. Hemost. , vol.24 , pp. 431-435
    • Astedt, B.1    Lindoff, C.2    Lecander, I.3
  • 36
    • 0029360521 scopus 로고
    • Molecular characterization of plasminogen activators in human gingival crevicular fluid
    • Brown J.M., Watanabe K., Cohen R.L., Chambers D.A. Molecular characterization of plasminogen activators in human gingival crevicular fluid. Arch. Oral Biol. 1995, 40:839-845.
    • (1995) Arch. Oral Biol. , vol.40 , pp. 839-845
    • Brown, J.M.1    Watanabe, K.2    Cohen, R.L.3    Chambers, D.A.4
  • 37
    • 0036005961 scopus 로고    scopus 로고
    • The plasminogen activating system in periodontal health and disease
    • Kinnby B. The plasminogen activating system in periodontal health and disease. Biol. Chem. 2002, 383:85-92.
    • (2002) Biol. Chem. , vol.383 , pp. 85-92
    • Kinnby, B.1
  • 38
    • 49049092569 scopus 로고    scopus 로고
    • The interaction between urokinase receptor and vitronectin in cell adhesion and signalling
    • Madsen C.D., Sidenius N. The interaction between urokinase receptor and vitronectin in cell adhesion and signalling. Eur. J. Cell Biol. 2008, 87:617-629.
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 617-629
    • Madsen, C.D.1    Sidenius, N.2
  • 39
    • 0028334672 scopus 로고
    • Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy
    • Waltz D.A., Chapman H.A. Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy. J. Biol. Chem. 1994, 269:14746-14750.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14746-14750
    • Waltz, D.A.1    Chapman, H.A.2
  • 41
    • 10044284103 scopus 로고    scopus 로고
    • Unexpected role of plasminogen activator inhibitor 1 in cell adhesion and detachment
    • Czekay R.P., Loskutoff D.J. Unexpected role of plasminogen activator inhibitor 1 in cell adhesion and detachment. Exp. Biol. Med. (Maywood) 2004, 229:1090-1096.
    • (2004) Exp. Biol. Med. (Maywood) , vol.229 , pp. 1090-1096
    • Czekay, R.P.1    Loskutoff, D.J.2
  • 42
    • 0034830757 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 regulates cell adhesion by binding to the somatomedin B domain of vitronectin
    • Deng G., Curriden S.A., Hu G., Czekay R.P., Loskutoff D.J. Plasminogen activator inhibitor-1 regulates cell adhesion by binding to the somatomedin B domain of vitronectin. J. Cell Physiol. 2001, 189:23-33.
    • (2001) J. Cell Physiol. , vol.189 , pp. 23-33
    • Deng, G.1    Curriden, S.A.2    Hu, G.3    Czekay, R.P.4    Loskutoff, D.J.5
  • 43
    • 0030971579 scopus 로고    scopus 로고
    • Binding of urokinase to plasminogen activator inhibitor type-1 mediates cell adhesion and spreading
    • Planus E., Barlovatz-Meimon G., Rogers R.A., Bonavaud S., Ingber D.E., Wang N. Binding of urokinase to plasminogen activator inhibitor type-1 mediates cell adhesion and spreading. J. Cell Sci. 1997, 110:1091-1098.
    • (1997) J. Cell Sci. , vol.110 , pp. 1091-1098
    • Planus, E.1    Barlovatz-Meimon, G.2    Rogers, R.A.3    Bonavaud, S.4    Ingber, D.E.5    Wang, N.6
  • 44
    • 34447499051 scopus 로고    scopus 로고
    • The contributions of integrin affinity and integrin-cytoskeletal engagement in endothelial and smooth muscle cell adhesion to vitronectin
    • Stefansson S., Su E.J., Ishigami S., Cale J.M., Gao Y., Gorlatova N., Lawrence D.A. The contributions of integrin affinity and integrin-cytoskeletal engagement in endothelial and smooth muscle cell adhesion to vitronectin. J. Biol. Chem. 2007, 282:15679-15689.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15679-15689
    • Stefansson, S.1    Su, E.J.2    Ishigami, S.3    Cale, J.M.4    Gao, Y.5    Gorlatova, N.6    Lawrence, D.A.7
  • 45
    • 58149293068 scopus 로고    scopus 로고
    • Vitronectin inhibits plasminogen activator inhibitor-1-induced signalling and chemotaxis by blocking plasminogen activator inhibitor-1 binding to the low-density lipoprotein receptor-related protein
    • Kamikubo Y., Neels J.G., Degryse B. Vitronectin inhibits plasminogen activator inhibitor-1-induced signalling and chemotaxis by blocking plasminogen activator inhibitor-1 binding to the low-density lipoprotein receptor-related protein. Int. J. Biochem. Cell Biol. 2009, 41:578-585.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 578-585
    • Kamikubo, Y.1    Neels, J.G.2    Degryse, B.3
  • 46
    • 0029745109 scopus 로고    scopus 로고
    • The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin
    • Stefansson S., Lawrence D.A. The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin. Nature 1996, 383:441-443.
    • (1996) Nature , vol.383 , pp. 441-443
    • Stefansson, S.1    Lawrence, D.A.2
  • 47
    • 79952038460 scopus 로고    scopus 로고
    • SERPINB2 (A004139), UCSD-Nature Molecule Pages, doi:. doi:10.1038/mp.a004139.01.
    • D.R. Croucher, M. Ranson, D.N. Saunders, SERPINB2 (A004139), UCSD-Nature Molecule Pages, 2010. doi:. doi:10.1038/mp.a004139.01.
    • (2010)
    • Croucher, D.R.1    Ranson, M.2    Saunders, D.N.3
  • 50
    • 0029816265 scopus 로고    scopus 로고
    • Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?
    • Deng G., Curriden S.A., Wang S., Rosenberg S., Loskutoff D.J. Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?. J. Cell Biol. 1996, 134:1563-1571.
    • (1996) J. Cell Biol. , vol.134 , pp. 1563-1571
    • Deng, G.1    Curriden, S.A.2    Wang, S.3    Rosenberg, S.4    Loskutoff, D.J.5


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