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Volumn , Issue , 2012, Pages 251-281

Protease Nexin-1 - a serpin with a possible proinvasive role in cancer

Author keywords

animals; biochemistry; cancer; cell culture; expression; Glia derived nexin (GDN); metabolism; metastasis; plasminogen; prognosis; serine protease inhibitors; serpinE2

Indexed keywords


EID: 84885730237     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527649327.ch10     Document Type: Chapter
Times cited : (4)

References (175)
  • 1
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function
    • Irving, J.A., Pike, R.N., Lesk, A.M., and Whisstock, J.C. (2000) Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res., 10, 1845-1864.
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 2
    • 33746503823 scopus 로고    scopus 로고
    • Shape-shifting serpins-advantages of a mobile mechanism
    • Huntington, J.A. (2006) Shape-shifting serpins-advantages of a mobile mechanism. Trends Biochem. Sci., 31, 427-435.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 427-435
    • Huntington, J.A.1
  • 4
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P.G. (2002) Serpin structure, mechanism, and function. Chem. Rev., 102, 4751-4804.
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 6
    • 38549101559 scopus 로고    scopus 로고
    • The role of serpins in the surveillance of the secretory pathway
    • Ragg, H. (2007) The role of serpins in the surveillance of the secretory pathway. Cell. Mol. Life Sci., 64, 2763-2770.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2763-2770
    • Ragg, H.1
  • 7
    • 0032007550 scopus 로고    scopus 로고
    • Expression genetics: a different approach to cancer diagnosis and prognosis
    • Zhang, M., Martin, K.J., Sheng, S., and Sager, R. (1998) Expression genetics: a different approach to cancer diagnosis and prognosis. Trends Biotechnol., 16, 66-71.
    • (1998) Trends Biotechnol. , vol.16 , pp. 66-71
    • Zhang, M.1    Martin, K.J.2    Sheng, S.3    Sager, R.4
  • 8
    • 0033616827 scopus 로고    scopus 로고
    • Suppression of breast cancer growth and metastasis by a serpin myoepithelium-derived serine proteinase inhibitor expressed in the mammary myoepithelial cells
    • Xiao, G., Liu, Y.E., Gentz, R., Sang, Q.A., Ni, J., Goldberg, I.D., and Shi, Y.E. (1999) Suppression of breast cancer growth and metastasis by a serpin myoepithelium-derived serine proteinase inhibitor expressed in the mammary myoepithelial cells. Proc. Natl. Acad. Sci. U.S.A., 96, 3700-3705.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3700-3705
    • Xiao, G.1    Liu, Y.E.2    Gentz, R.3    Sang, Q.A.4    Ni, J.5    Goldberg, I.D.6    Shi, Y.E.7
  • 9
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: a review
    • Andreasen, P.A., Kjoller, L., Christensen, L., and Duffy, M.J. (1997) The urokinase-type plasminogen activator system in cancer metastasis: a review. Int. J. Cancer, 72, 1-22.
    • (1997) Int. J. Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjoller, L.2    Christensen, L.3    Duffy, M.J.4
  • 10
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen, P.A., Egelund, R., and Petersen, H.H. (2000) The plasminogen activation system in tumor growth, invasion, and metastasis. Cell. Mol. Life Sci., 57, 25-40.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 11
    • 0035918882 scopus 로고    scopus 로고
    • Randomized adjuvant chemotherapy trial in high-risk, lymph node-negative breast cancer patients identified by urokinase-type plasminogen activator and plasminogen activator inhibitor type 1
    • Janicke, F., Prechtl, A., Thomssen, C., Harbeck, N., Meisner, C., Untch, M., Sweep, C.G., Selbmann, H.K., Graeff, H., and Schmitt, M. (2001) Randomized adjuvant chemotherapy trial in high-risk, lymph node-negative breast cancer patients identified by urokinase-type plasminogen activator and plasminogen activator inhibitor type 1. J. Natl. Cancer Inst., 93, 913-920.
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 913-920
    • Janicke, F.1    Prechtl, A.2    Thomssen, C.3    Harbeck, N.4    Meisner, C.5    Untch, M.6    Sweep, C.G.7    Selbmann, H.K.8    Graeff, H.9    Schmitt, M.10
  • 12
    • 0037083657 scopus 로고    scopus 로고
    • Clinical relevance of invasion factors urokinase-type plasminogen activator and plasminogen activator inhibitor type 1 for individualized therapy decisions in primary breast cancer is greatest when used in combination
    • Harbeck, N., Kates, R.E., and Schmitt, M. (2002) Clinical relevance of invasion factors urokinase-type plasminogen activator and plasminogen activator inhibitor type 1 for individualized therapy decisions in primary breast cancer is greatest when used in combination. J. Clin. Oncol., 20, 1000-1007.
    • (2002) J. Clin. Oncol. , vol.20 , pp. 1000-1007
    • Harbeck, N.1    Kates, R.E.2    Schmitt, M.3
  • 14
    • 36849069347 scopus 로고    scopus 로고
    • American Society of Clinical Oncology 2007 update of recommendations for the use of tumor markers in breast cancer
    • American Society of Clinical Oncology
    • Harris, L., Fritsche, H., Mennel, R., Norton, L., Ravdin, P., Taube, S., Somerfield, M.R., Hayes, D.F., and Bast, R.C. Jr., American Society of Clinical Oncology (2007) American Society of Clinical Oncology 2007 update of recommendations for the use of tumor markers in breast cancer. J. Clin. Oncol., 25, 5287-5312.
    • (2007) J. Clin. Oncol. , vol.25 , pp. 5287-5312
    • Harris, L.1    Fritsche, H.2    Mennel, R.3    Norton, L.4    Ravdin, P.5    Taube, S.6    Somerfield, M.R.7    Hayes, D.F.8    Bast, R.C.Jr.9
  • 16
    • 35348834104 scopus 로고    scopus 로고
    • PAI-1 - a potential therapeutic target in cancer
    • Andreasen, P.A. (2007) PAI-1 - a potential therapeutic target in cancer. Curr. Drug Targets, 8, 1030-1041.
    • (2007) Curr. Drug Targets , vol.8 , pp. 1030-1041
    • Andreasen, P.A.1
  • 18
    • 0015834367 scopus 로고
    • Glia-induced morphological differentiation in neuroblastoma cells
    • Monard, D., Solomon, F., Rentsch, M., and Gysin, R. (1973) Glia-induced morphological differentiation in neuroblastoma cells. Proc. Natl. Acad. Sci. U.S.A., 70, 1894-1897.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 1894-1897
    • Monard, D.1    Solomon, F.2    Rentsch, M.3    Gysin, R.4
  • 19
    • 0017809786 scopus 로고
    • Brain development influences the appearance of glial factor-like activity in rat brain primary cultures
    • Schurch-Rathgeb, Y.M.D. (1978) Brain development influences the appearance of glial factor-like activity in rat brain primary cultures. Nature, 273, 308-309.
    • (1978) Nature , vol.273 , pp. 308-309
    • Schurch Rathgeb, Y.M.D.1
  • 20
    • 0018932068 scopus 로고
    • Protease-nexin: a cellular component that links thrombin and plasminogen activator and mediates their binding to cells
    • Baker, J.B., Low, D.A., Simmer, R.L., and Cunningham, D.D. (1980) Protease-nexin: a cellular component that links thrombin and plasminogen activator and mediates their binding to cells. Cell, 21, 37-45.
    • (1980) Cell , vol.21 , pp. 37-45
    • Baker, J.B.1    Low, D.A.2    Simmer, R.L.3    Cunningham, D.D.4
  • 21
    • 0019797849 scopus 로고
    • Released protease-nexin regulates cellular binding, internalization, and degradation of serine proteases
    • Low, D.A., Baker, J.B., Koonce, W.C., and Cunningham, D.D. (1981) Released protease-nexin regulates cellular binding, internalization, and degradation of serine proteases. Proc. Natl. Acad. Sci. U.S.A., 78, 2340-2344.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2340-2344
    • Low, D.A.1    Baker, J.B.2    Koonce, W.C.3    Cunningham, D.D.4
  • 22
    • 0020689778 scopus 로고
    • Inhibition of protease activity can lead to neurite extension in neuroblastoma cells
    • Monard, D., Niday, E., Limat, A., and Solomon, F. (1983) Inhibition of protease activity can lead to neurite extension in neuroblastoma cells. Prog. Brain Res., 58, 359-364.
    • (1983) Prog. Brain Res. , vol.58 , pp. 359-364
    • Monard, D.1    Niday, E.2    Limat, A.3    Solomon, F.4
  • 23
    • 0021091544 scopus 로고
    • Purification of human protease nexin
    • Scott, R.W. and Baker, J.B. (1983) Purification of human protease nexin. J. Biol. Chem., 258, 10439-10444.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10439-10444
    • Scott, R.W.1    Baker, J.B.2
  • 24
    • 0022110035 scopus 로고
    • A glia-derived neurite-promoting factor with protease inhibitory activity
    • Guenther, J., Nick, H., and Monard, D. (1985) A glia-derived neurite-promoting factor with protease inhibitory activity. EMBO J., 4, 1963-1966.
    • (1985) EMBO J. , vol.4 , pp. 1963-1966
    • Guenther, J.1    Nick, H.2    Monard, D.3
  • 26
    • 0022897760 scopus 로고
    • A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins
    • Gloor, S., Odink, K., Guenther, J., Nick, H., and Monard, D. (1986) A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins. Cell, 47, 687-693.
    • (1986) Cell , vol.47 , pp. 687-693
    • Gloor, S.1    Odink, K.2    Guenther, J.3    Nick, H.4    Monard, D.5
  • 27
    • 0023646684 scopus 로고
    • cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily
    • Sommer, J., Gloor, S.M., Rovelli, G.F., Hofsteenge, J., Nick, H., Meier, R., and Monard, D. (1987) cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily. Biochemistry, 26, 6407-6410.
    • (1987) Biochemistry , vol.26 , pp. 6407-6410
    • Sommer, J.1    Gloor, S.M.2    Rovelli, G.F.3    Hofsteenge, J.4    Nick, H.5    Meier, R.6    Monard, D.7
  • 28
    • 0023898838 scopus 로고
    • Monoclonal antibodies to protease nexin 1 that differentially block its inhibition of target proteases
    • Wagner, S.L., Van Nostrand, W.E., Lau, A.L., and Cunningham, D.D. (1988) Monoclonal antibodies to protease nexin 1 that differentially block its inhibition of target proteases. Biochemistry, 27, 2173-2176.
    • (1988) Biochemistry , vol.27 , pp. 2173-2176
    • Wagner, S.L.1    Van Nostr, W.E.2    Lau, A.L.3    Cunningham, D.D.4
  • 29
    • 0030054814 scopus 로고    scopus 로고
    • Characterization of the human protease nexin-1 promoter and its regulation by Sp1 through a G/C-rich activation domain
    • Guttridge, D.C. and Cunningham, D.D. (1996) Characterization of the human protease nexin-1 promoter and its regulation by Sp1 through a G/C-rich activation domain. J. Neurochem., 67, 498-507.
    • (1996) J. Neurochem. , vol.67 , pp. 498-507
    • Guttridge, D.C.1    Cunningham, D.D.2
  • 31
    • 0029053384 scopus 로고
    • The gene for the serpin thrombin inhibitor (PI7), protease nexin I, is located on human chromosome 2q33-q35 and on syntenic regions in the mouse and sheep genomes
    • Carter, R.E., Cerosaletti, K.M., Burkin, D.J., Fournier, R.E., Jones, C., Greenberg, B.D., Citron, B.A., and Festoff, B.W. (1995) The gene for the serpin thrombin inhibitor (PI7), protease nexin I, is located on human chromosome 2q33-q35 and on syntenic regions in the mouse and sheep genomes. Genomics, 27, 196-199.
    • (1995) Genomics , vol.27 , pp. 196-199
    • Carter, R.E.1    Cerosaletti, K.M.2    Burkin, D.J.3    Fournier, R.E.4    Jones, C.5    Greenberg, B.D.6    Citron, B.A.7    Festoff, B.W.8
  • 35
    • 0025721157 scopus 로고
    • Protease specificity and heparin binding and activation of recombinant protease nexin I
    • Evans, D.L., McGrogan, M., Scott, R.W., and Carrell, R.W. (1991) Protease specificity and heparin binding and activation of recombinant protease nexin I. J. Biol. Chem., 266, 22307-22312.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22307-22312
    • Evans, D.L.1    McGrogan, M.2    Scott, R.W.3    Carrell, R.W.4
  • 36
    • 0026524269 scopus 로고
    • Characterization of the heparin-binding site of glia-derived nexin/protease nexin-1
    • Rovelli, G., Stone, S.R., Guidolin, A., Sommer, J., and Monard, D. (1992) Characterization of the heparin-binding site of glia-derived nexin/protease nexin-1. Biochemistry, 31, 3542-3549.
    • (1992) Biochemistry , vol.31 , pp. 3542-3549
    • Rovelli, G.1    Stone, S.R.2    Guidolin, A.3    Sommer, J.4    Monard, D.5
  • 37
    • 0028343425 scopus 로고
    • Localization of the heparin-binding site of glia-derived nexin/protease nexin-1 by site-directed mutagenesis
    • Stone, S.R., Brown-Luedi, M.L., Rovelli, G., Guidolin, A., McGlynn, E., and Monard, D. (1994) Localization of the heparin-binding site of glia-derived nexin/protease nexin-1 by site-directed mutagenesis. Biochemistry, 33, 7731-7735.
    • (1994) Biochemistry , vol.33 , pp. 7731-7735
    • Stone, S.R.1    Brown Luedi, M.L.2    Rovelli, G.3    Guidolin, A.4    McGlynn, E.5    Monard, D.6
  • 38
    • 0030987297 scopus 로고    scopus 로고
    • Identification of a binding site in protease nexin I (PN1) required for the receptor mediated internalization of PN1-thrombin complexes
    • Knauer, M.F., Hawley, S.B., and Knauer, D.J. (1997) Identification of a binding site in protease nexin I (PN1) required for the receptor mediated internalization of PN1-thrombin complexes. J. Biol. Chem., 272, 12261-12264.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12261-12264
    • Knauer, M.F.1    Hawley, S.B.2    Knauer, D.J.3
  • 39
    • 0032957690 scopus 로고    scopus 로고
    • Analysis of a structural determinant in thrombin-protease nexin 1 complexes that mediates clearance by the low density lipoprotein receptor-related protein
    • Knauer, M.F., Crisp, R.J., Kridel, S.J., and Knauer, D.J. (1999) Analysis of a structural determinant in thrombin-protease nexin 1 complexes that mediates clearance by the low density lipoprotein receptor-related protein. J. Biol. Chem., 274, 275-281.
    • (1999) J. Biol. Chem. , vol.274 , pp. 275-281
    • Knauer, M.F.1    Crisp, R.J.2    Kridel, S.J.3    Knauer, D.J.4
  • 41
    • 33644859395 scopus 로고    scopus 로고
    • Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase
    • Dementiev, A., Dobo, J., and Gettins, P.G. (2006) Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase. J. Biol. Chem., 281, 3452-3457.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3452-3457
    • Dementiev, A.1    Dobo, J.2    Gettins, P.G.3
  • 42
    • 52949152789 scopus 로고    scopus 로고
    • High-resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1B in its proteinase-cleaved form: a new tool for detailed interaction studies and modeling
    • Jensen, J.K. and Gettins, P.G. (2008) High-resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1B in its proteinase-cleaved form: a new tool for detailed interaction studies and modeling. Protein Sci., 17, 1844-1849.
    • (2008) Protein Sci. , vol.17 , pp. 1844-1849
    • Jensen, J.K.1    Gettins, P.G.2
  • 43
    • 0024530794 scopus 로고
    • Effect of heparin on the glia-derived-nexin-thrombin interaction
    • Wallace, A., Rovelli, G., Hofsteenge, J., and Stone, S.R. (1989) Effect of heparin on the glia-derived-nexin-thrombin interaction. Biochem. J., 257, 191-196.
    • (1989) Biochem. J. , vol.257 , pp. 191-196
    • Wallace, A.1    Rovelli, G.2    Hofsteenge, J.3    Stone, S.R.4
  • 44
    • 0033043018 scopus 로고    scopus 로고
    • Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding
    • Herndon, M.E., Stipp, C.S., and Lander, A.D. (1999) Interactions of neural glycosaminoglycans and proteoglycans with protein ligands: assessment of selectivity, heterogeneity and the participation of core proteins in binding. Glycobiology, 9, 143-155.
    • (1999) Glycobiology , vol.9 , pp. 143-155
    • Herndon, M.E.1    Stipp, C.S.2    Lander, A.D.3
  • 46
    • 76249089297 scopus 로고    scopus 로고
    • Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex
    • Johnson, D.J., Langdown, J., and Huntington, J.A. (2010) Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex. Proc. Natl. Acad. Sci. U.S.A., 107, 645-650.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 645-650
    • Johnson, D.J.1    Langdown, J.2    Huntington, J.A.3
  • 47
    • 0037143655 scopus 로고    scopus 로고
    • Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
    • Baglin, T.P., Carrell, R.W., Church, F.C., Esmon, C.T., and Huntington, J.A. (2002) Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc. Natl. Acad. Sci. U.S.A., 99, 11079-11084.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11079-11084
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3    Esmon, C.T.4    Huntington, J.A.5
  • 48
    • 0026755995 scopus 로고
    • Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin
    • Ehrlich, H.J., Gebbink, R.K., Keijer, J., and Pannekoek, H. (1992) Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin. J. Biol. Chem., 267, 11606-11611.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11606-11611
    • Ehrlich, H.J.1    Gebbink, R.K.2    Keijer, J.3    Pannekoek, H.4
  • 49
    • 0025071332 scopus 로고
    • Specific interaction of vitronectin with the cell-secreted protease inhibitor glia-derived nexin and its thrombin complex
    • Rovelli, G., Stone, S.R., Preissner, K.T., and Monard, D. (1990) Specific interaction of vitronectin with the cell-secreted protease inhibitor glia-derived nexin and its thrombin complex. Eur. J. Biochem., 192, 797-803.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 797-803
    • Rovelli, G.1    Stone, S.R.2    Preissner, K.T.3    Monard, D.4
  • 50
    • 0035692792 scopus 로고    scopus 로고
    • Serpins and other covalent protease inhibitors
    • Ye, S. and Goldsmith, E.J. (2001) Serpins and other covalent protease inhibitors. Curr. Opin. Struct. Biol., 11, 740-745.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 740-745
    • Ye, S.1    Goldsmith, E.J.2
  • 51
    • 0036005954 scopus 로고    scopus 로고
    • The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment
    • Wind, T., Hansen, M., Jensen, J.K., and Andreasen, P.A. (2002) The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment. Biol. Chem., 383, 21-36.
    • (2002) Biol. Chem. , vol.383 , pp. 21-36
    • Wind, T.1    Hansen, M.2    Jensen, J.K.3    Andreasen, P.A.4
  • 53
    • 4344590703 scopus 로고    scopus 로고
    • Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin
    • Li, W., Johnson, D.J., Esmon, C.T., and Huntington, J.A. (2004) Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Nat. Struct. Mol. Biol., 11, 857-862.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 857-862
    • Li, W.1    Johnson, D.J.2    Esmon, C.T.3    Huntington, J.A.4
  • 54
    • 42449150052 scopus 로고    scopus 로고
    • Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex
    • Li, W., Adams, T.E., Nangalia, J., Esmon, C.T., and Huntington, J.A. (2008) Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex. Proc. Natl. Acad. Sci. U.S.A., 105, 4661-4666.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4661-4666
    • Li, W.1    Adams, T.E.2    Nangalia, J.3    Esmon, C.T.4    Huntington, J.A.5
  • 55
    • 33646581724 scopus 로고    scopus 로고
    • Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation
    • Johnson, D.J., Li, W., Adams, T.E., and Huntington, J.A. (2006) Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. EMBO J., 25, 2029-2037.
    • (2006) EMBO J. , vol.25 , pp. 2029-2037
    • Johnson, D.J.1    Li, W.2    Adams, T.E.3    Huntington, J.A.4
  • 56
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J.A., Read, R.J., and Carrell, R.W. (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature, 407, 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 58
    • 1642326652 scopus 로고    scopus 로고
    • Regulation of prostasin expression and function in the prostate
    • Chen, L.M., Zhang, X., and Chai, K.X. (2004) Regulation of prostasin expression and function in the prostate. Prostate, 59, 1-12.
    • (2004) Prostate , vol.59 , pp. 1-12
    • Chen, L.M.1    Zhang, X.2    Chai, K.X.3
  • 60
    • 34249816146 scopus 로고    scopus 로고
    • Inhibition of PDGF-BB by factor VII-activating protease (FSAP) is neutralized by protease nexin-1, and the FSAP-inhibitor complexes are internalized via LRP
    • Muhl, L., Nykjaer, A., Wygrecka, M., Monard, D., Preissner, K.T., and Kanse, S.M. (2007) Inhibition of PDGF-BB by factor VII-activating protease (FSAP) is neutralized by protease nexin-1, and the FSAP-inhibitor complexes are internalized via LRP. Biochem. J., 404, 191-196.
    • (2007) Biochem. J. , vol.404 , pp. 191-196
    • Muhl, L.1    Nykjaer, A.2    Wygrecka, M.3    Monard, D.4    Preissner, K.T.5    Kanse, S.M.6
  • 61
    • 0031010046 scopus 로고    scopus 로고
    • Intrinsic specificity of the reactive site loop of alpha1-antitrypsin, alpha1-antichymotrypsin, antithrombin III, and protease nexin I
    • Djie, M.Z., Stone, S.R., and Le Bonniec, B.F. (1997) Intrinsic specificity of the reactive site loop of alpha1-antitrypsin, alpha1-antichymotrypsin, antithrombin III, and protease nexin I. J. Biol. Chem., 272, 16268-16273.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16268-16273
    • Djie, M.Z.1    Stone, S.R.2    Le Bonniec, B.F.3
  • 62
    • 0037033099 scopus 로고    scopus 로고
    • Protease nexin 1 is a potent urinary plasminogen activator inhibitor in the presence of collagen type IV
    • Crisp, R.J., Knauer, M.F., and Knauer, D.J. (2002) Protease nexin 1 is a potent urinary plasminogen activator inhibitor in the presence of collagen type IV. J. Biol. Chem., 277, 47285-47291.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47285-47291
    • Crisp, R.J.1    Knauer, M.F.2    Knauer, D.J.3
  • 63
    • 0021254064 scopus 로고
    • Purification of human fibroblast urokinase proenzyme and analysis of its regulation by proteases and protease nexin
    • Eaton, D.L., Scott, R.W., and Baker, J.B. (1984) Purification of human fibroblast urokinase proenzyme and analysis of its regulation by proteases and protease nexin. J. Biol. Chem., 259, 6241-6247.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6241-6247
    • Eaton, D.L.1    Scott, R.W.2    Baker, J.B.3
  • 65
    • 0023937572 scopus 로고
    • Purification of a form of protease nexin 1 that binds heparin with a low affinity
    • Van Nostrand, W.E., Wagner, S.L., and Cunningham, D.D. (1988) Purification of a form of protease nexin 1 that binds heparin with a low affinity. Biochemistry, 27, 2176-2181.
    • (1988) Biochemistry , vol.27 , pp. 2176-2181
    • Van Nostr, W.E.1    Wagner, S.L.2    Cunningham, D.D.3
  • 66
    • 0022394350 scopus 로고
    • Mono- and bidimensional 500MHz 1H-NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: evidence for conformational peculiarity of the sulfated iduronate residue
    • Torri, G., Casu, B., Gatti, G., Petitou, M., Choay, J., Jacquinet, J.C., and Sinay, P. (1985) Mono- and bidimensional 500MHz 1H-NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: evidence for conformational peculiarity of the sulfated iduronate residue. Biochem. Biophys. Res. Commun., 128, 134-140.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 134-140
    • Torri, G.1    Casu, B.2    Gatti, G.3    Petitou, M.4    Choay, J.5    Jacquinet, J.C.6    Sinay, P.7
  • 67
    • 0024411545 scopus 로고
    • Chemically synthesized heparin-derived oligosaccharides
    • Choay, J. (1989) Chemically synthesized heparin-derived oligosaccharides. Ann. N.Y. Acad. Sci., 556, 61-74.
    • (1989) Ann. N.Y. Acad. Sci. , vol.556 , pp. 61-74
    • Choay, J.1
  • 68
    • 0141609849 scopus 로고    scopus 로고
    • Mechanisms of glycosaminoglycan activation of the serpins in hemostasis
    • Huntington, J.A. (2003) Mechanisms of glycosaminoglycan activation of the serpins in hemostasis. J. Thromb. Haemostasis, 1, 1535-1549.
    • (2003) J. Thromb. Haemostasis , vol.1 , pp. 1535-1549
    • Huntington, J.A.1
  • 69
    • 0001668795 scopus 로고
    • Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin
    • Lindahl, U., Backstrom, G., Thunberg, L., and Leder, I.G. (1980) Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin. Proc. Natl. Acad. Sci. U.S.A., 77, 6551-6555.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 6551-6555
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3    Leder, I.G.4
  • 71
    • 4344710558 scopus 로고    scopus 로고
    • The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity
    • Dementiev, A., Petitou, M., Herbert, J.M., and Gettins, P.G. (2004) The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity. Nat. Struct. Mol. Biol., 11, 863-867.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 863-867
    • Dementiev, A.1    Petitou, M.2    Herbert, J.M.3    Gettins, P.G.4
  • 73
    • 0036607597 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor gene family: a cellular Swiss army knife?
    • Nykjaer, A. and Willnow, T.E. (2002) The low-density lipoprotein receptor gene family: a cellular Swiss army knife? Trends Cell Biol., 12, 273-280.
    • (2002) Trends Cell Biol. , vol.12 , pp. 273-280
    • Nykjaer, A.1    Willnow, T.E.2
  • 74
    • 28344453429 scopus 로고    scopus 로고
    • Beyond endocytosis: LRP function in cell migration, proliferation and vascular permeability
    • Lillis, A.P., Mikhailenko, I., and Strickland, D.K. (2005) Beyond endocytosis: LRP function in cell migration, proliferation and vascular permeability. J. Thromb. Haemostasis, 3, 1884-1893.
    • (2005) J. Thromb. Haemostasis , vol.3 , pp. 1884-1893
    • Lillis, A.P.1    Mikhailenko, I.2    Strickl, D.K.3
  • 75
    • 33745284559 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein (LRP)-mediated clearance of activated blood coagulation co-factors and proteases: clearance mechanism or regulation? J
    • Strickland, D.K. and Medved, L. (2006) Low-density lipoprotein receptor-related protein (LRP)-mediated clearance of activated blood coagulation co-factors and proteases: clearance mechanism or regulation? J. Thromb. Haemostasis, 4, 1484-1486.
    • (2006) Thromb. Haemostasis , vol.4 , pp. 1484-1486
    • Strickl, D.K.1    Medved, L.2
  • 76
    • 0025666455 scopus 로고
    • Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor
    • Kristensen, T., Moestrup, S.K., Gliemann, J., Bendtsen, L., Sand, O., and Sottrup-Jensen, L. (1990) Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor. FEBS Lett., 276, 151-155.
    • (1990) FEBS Lett. , vol.276 , pp. 151-155
    • Kristensen, T.1    Moestrup, S.K.2    Gliemann, J.3    Bendtsen, L.4    Sand, O.5    Sottrup Jensen, L.6
  • 77
    • 0025080835 scopus 로고
    • Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor
    • Strickland, D.K., Ashcom, J.D., Williams, S., Burgess, W.H., Migliorini, M., and Argraves, W.S. (1990) Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor. J. Biol. Chem., 265, 17401-17404.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17401-17404
    • Strickl, D.K.1    Ashcom, J.D.2    Williams, S.3    Burgess, W.H.4    Migliorini, M.5    Argraves, W.S.6
  • 78
    • 0001665337 scopus 로고
    • Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor
    • Herz, J., Hamann, U., Rogne, S., Myklebost, O., Gausepohl, H., and Stanley, K.K. (1988) Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. EMBO J., 7, 4119-4127.
    • (1988) EMBO J. , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 79
    • 0026668601 scopus 로고
    • Complexes of tissue-type plasminogen activator and its serpin inhibitor plasminogen-activator inhibitor type 1 are internalized by means of the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor
    • Orth, K., Madison, E.L., Gething, M.J., Sambrook, J.F., and Herz, J. (1992) Complexes of tissue-type plasminogen activator and its serpin inhibitor plasminogen-activator inhibitor type 1 are internalized by means of the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor. Proc. Natl. Acad. Sci. U.S.A., 89, 7422-7426.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7422-7426
    • Orth, K.1    Madison, E.L.2    Gething, M.J.3    Sambrook, J.F.4    Herz, J.5
  • 81
    • 0141832797 scopus 로고    scopus 로고
    • Diverse role of LDL receptor-related protein in the clearance of proteases and in signaling
    • Strickland, D.K. and Ranganathan, S. (2003) Diverse role of LDL receptor-related protein in the clearance of proteases and in signaling. J. Thromb. Haemostasis, 1, 1663-1670.
    • (2003) J. Thromb. Haemostasis , vol.1 , pp. 1663-1670
    • Strickl, D.K.1    Ranganathan, S.2
  • 82
    • 67650917714 scopus 로고    scopus 로고
    • Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP
    • Jensen, J.K., Dolmer, K., Schar, C., and Gettins, P.G. (2009) Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP. Biochem. J., 421, 273-282.
    • (2009) Biochem. J. , vol.421 , pp. 273-282
    • Jensen, J.K.1    Dolmer, K.2    Schar, C.3    Gettins, P.G.4
  • 84
    • 0023279557 scopus 로고
    • Characterization of the receptor for protease nexin-I:protease complexes on human fibroblasts
    • Howard, E.W. and Knauer, D.J. (1987) Characterization of the receptor for protease nexin-I:protease complexes on human fibroblasts. J. Cell. Physiol., 131, 276-283.
    • (1987) J. Cell. Physiol. , vol.131 , pp. 276-283
    • Howard, E.W.1    Knauer, D.J.2
  • 85
    • 0028236893 scopus 로고
    • Protease nexin-1-urokinase complexes are internalized and degraded through a mechanism that requires both urokinase receptor and alpha 2-macroglobulin receptor
    • Conese, M., Olson, D., and Blasi, F. (1994) Protease nexin-1-urokinase complexes are internalized and degraded through a mechanism that requires both urokinase receptor and alpha 2-macroglobulin receptor. J. Biol. Chem., 269, 17886-17892.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17886-17892
    • Conese, M.1    Olson, D.2    Blasi, F.3
  • 86
    • 0030886795 scopus 로고    scopus 로고
    • Specificity of serine proteinase/ serpin complex binding to very-low-density lipoprotein receptor and alpha2-macroglobulin receptor/low-density-lipoproteinreceptor- related protein
    • Kasza, A., Petersen, H.H., Heegaard, C.W., Oka, K., Christensen, A., Dubin, A., Chan, L., and Andreasen, P.A. (1997) Specificity of serine proteinase/ serpin complex binding to very-low-density lipoprotein receptor and alpha2-macroglobulin receptor/low-density-lipoproteinreceptor- related protein. Eur. J. Biochem., 248, 270-281.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 270-281
    • Kasza, A.1    Petersen, H.H.2    Heegaard, C.W.3    Oka, K.4    Christensen, A.5    Dubin, A.6    Chan, L.7    Andreasen, P.A.8
  • 88
    • 0030716260 scopus 로고    scopus 로고
    • The efficient catabolism of thrombin-protease nexin 1 complexes is a synergistic mechanism that requires both the LDL receptor-related protein and cell surface heparins
    • Knauer, M.F., Kridel, S.J., Hawley, S.B., and Knauer, D.J. (1997) The efficient catabolism of thrombin-protease nexin 1 complexes is a synergistic mechanism that requires both the LDL receptor-related protein and cell surface heparins. J. Biol. Chem., 272, 29039-29045.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29039-29045
    • Knauer, M.F.1    Kridel, S.J.2    Hawley, S.B.3    Knauer, D.J.4
  • 91
    • 67650538093 scopus 로고    scopus 로고
    • Specificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1
    • Jensen, J.K., Dolmer, K., and Gettins, P.G. (2009) Specificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1. J. Biol. Chem., 284, 17989-17997.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17989-17997
    • Jensen, J.K.1    Dolmer, K.2    Gettins, P.G.3
  • 92
    • 33750571151 scopus 로고    scopus 로고
    • Binding areas of urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex for endocytosis receptors of the low-density lipoprotein receptor family, determined by site-directed mutagenesis
    • Skeldal, S., Larsen, J.V., Pedersen, K.E., Petersen, H.H., Egelund, R., Christensen, A., Jensen, J.K., Gliemann, J., and Andreasen, P.A. (2006) Binding areas of urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex for endocytosis receptors of the low-density lipoprotein receptor family, determined by site-directed mutagenesis. FEBS J., 273, 5143-5159.
    • (2006) FEBS J. , vol.273 , pp. 5143-5159
    • Skeldal, S.1    Larsen, J.V.2    Pedersen, K.E.3    Petersen, H.H.4    Egelund, R.5    Christensen, A.6    Jensen, J.K.7    Gliemann, J.8    Andreasen, P.A.9
  • 93
    • 2342648870 scopus 로고    scopus 로고
    • X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein
    • Verdaguer, N., Fita, I., Reithmayer, M., Moser, R., and Blaas, D. (2004) X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein. Nat. Struct. Mol. Biol., 11, 429-434.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 429-434
    • Verdaguer, N.1    Fita, I.2    Reithmayer, M.3    Moser, R.4    Blaas, D.5
  • 94
    • 33646046808 scopus 로고    scopus 로고
    • Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors
    • Fisher, C., Beglova, N., and Blacklow, S.C. (2006) Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors. Mol. Cell, 22, 277-283.
    • (2006) Mol. Cell , vol.22 , pp. 277-283
    • Fisher, C.1    Beglova, N.2    Blacklow, S.C.3
  • 95
    • 0009449206 scopus 로고
    • Human fibroblasts accelerate the inhibition of thrombin by protease nexin
    • Farrell, D.H. and Cunningham, D.D. (1986) Human fibroblasts accelerate the inhibition of thrombin by protease nexin. Proc. Natl. Acad. Sci. U.S.A., 83, 6858-6862.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 6858-6862
    • Farrell, D.H.1    Cunningham, D.D.2
  • 96
    • 0023655461 scopus 로고
    • Glycosaminoglycans on fibroblasts accelerate thrombin inhibition by protease nexin-1
    • Farrell, D.H. and Cunningham, D.D. (1987) Glycosaminoglycans on fibroblasts accelerate thrombin inhibition by protease nexin-1. Biochem. J., 245, 543-550.
    • (1987) Biochem. J. , vol.245 , pp. 543-550
    • Farrell, D.H.1    Cunningham, D.D.2
  • 98
    • 33749495693 scopus 로고    scopus 로고
    • Activation of ERK signaling upon alternative protease nexin-1 internalization mediated by syndecan-1
    • Li, X., Herz, J., and Monard, D. (2006) Activation of ERK signaling upon alternative protease nexin-1 internalization mediated by syndecan-1. J. Cell. Biochem., 99, 936-951.
    • (2006) J. Cell. Biochem. , vol.99 , pp. 936-951
    • Li, X.1    Herz, J.2    Monard, D.3
  • 99
    • 67651007506 scopus 로고    scopus 로고
    • The serine protease inhibitor protease nexin-1 controls mammary cancer metastasis through LRP-1-mediated MMP-9 expression
    • Fayard, B., Bianchi, F., Dey, J., Moreno, E., Djaffer, S., Hynes, N.E., and Monard, D. (2009) The serine protease inhibitor protease nexin-1 controls mammary cancer metastasis through LRP-1-mediated MMP-9 expression. Cancer Res., 69, 5690-5698.
    • (2009) Cancer Res. , vol.69 , pp. 5690-5698
    • Fayard, B.1    Bianchi, F.2    Dey, J.3    Moreno, E.4    Djaffer, S.5    Hynes, N.E.6    Monard, D.7
  • 101
    • 0022548950 scopus 로고
    • Inhibition of tumor-cell-mediated extracellular matrix destruction by a fibroblast proteinase inhibitor, protease nexin I
    • Bergman, B.L., Scott, R.W., Bajpai, A., Watts, S., and Baker, J.B. (1986) Inhibition of tumor-cell-mediated extracellular matrix destruction by a fibroblast proteinase inhibitor, protease nexin I. Proc. Natl. Acad. Sci. U.S.A., 83, 996-1000.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 996-1000
    • Bergman, B.L.1    Scott, R.W.2    Bajpai, A.3    Watts, S.4    Baker, J.B.5
  • 105
    • 0642373022 scopus 로고    scopus 로고
    • The role of serine proteases and serine protease inhibitors in the migration of gonadotropin-releasing hormone neurons
    • Drapkin, P.T., Monard, D., and Silverman, A.J. (2002) The role of serine proteases and serine protease inhibitors in the migration of gonadotropin-releasing hormone neurons. BMC Dev. Biol., 2, 1.
    • (2002) BMC Dev. Biol. , vol.2 , pp. 1
    • Drapkin, P.T.1    Monard, D.2    Silverman, A.J.3
  • 106
    • 0842323781 scopus 로고    scopus 로고
    • Reciprocal regulation of urokinase receptor (CD87)-mediated cell adhesion by plasminogen activator inhibitor-1 and protease nexin-1
    • Kanse, S.M., Chavakis, T., Al-Fakhri, N., Hersemeyer, K., Monard, D., and Preissner, K.T. (2004) Reciprocal regulation of urokinase receptor (CD87)-mediated cell adhesion by plasminogen activator inhibitor-1 and protease nexin-1. J. Cell Sci., 117, 477-485.
    • (2004) J. Cell Sci. , vol.117 , pp. 477-485
    • Kanse, S.M.1    Chavakis, T.2    Al Fakhri, N.3    Hersemeyer, K.4    Monard, D.5    Preissner, K.T.6
  • 107
    • 67650403484 scopus 로고    scopus 로고
    • Plasminogen activator inhibitors regulate cell adhesion through a uPAR-dependent mechanism
    • Czekay, R.P. and Loskutoff, D.J. (2009) Plasminogen activator inhibitors regulate cell adhesion through a uPAR-dependent mechanism. J. Cell. Physiol., 220, 655-663.
    • (2009) J. Cell. Physiol. , vol.220 , pp. 655-663
    • Czekay, R.P.1    Loskutoff, D.J.2
  • 108
    • 0024581134 scopus 로고
    • Covalent binding of human thrombin to a human endothelial cell-associated protein
    • Leroy-Viard, K., Jandrot-Perrus, M., Tobelem, G., and Guillin, M.C. (1989) Covalent binding of human thrombin to a human endothelial cell-associated protein. Exp. Cell Res., 181, 1-10.
    • (1989) Exp. Cell Res. , vol.181 , pp. 1-10
    • Leroy Viard, K.1    Jandrot Perrus, M.2    Tobelem, G.3    Guillin, M.C.4
  • 109
    • 0032910488 scopus 로고    scopus 로고
    • Protease nexin I expression is up-regulated in human skeletal muscle by injury-related factors
    • Mbebi, C., Hantai, D., Jandrot-Perrus, M., Doyennette, M.A., and Verdiere-Sahuque, M. (1999) Protease nexin I expression is up-regulated in human skeletal muscle by injury-related factors. J. Cell. Physiol., 179, 305-314.
    • (1999) J. Cell. Physiol. , vol.179 , pp. 305-314
    • Mbebi, C.1    Hantai, D.2    Jandrot Perrus, M.3    Doyennette, M.A.4    Verdiere Sahuque, M.5
  • 112
    • 80051644171 scopus 로고    scopus 로고
    • DNA methylation profiles of protease nexin 1 (SERPINE2) gene in human cell lines
    • Gao, S. and Andreasen, P.A. (2011) DNA methylation profiles of protease nexin 1 (SERPINE2) gene in human cell lines. Chin. J. Cancer Res., 23, 92-98.
    • (2011) Chin. J. Cancer Res. , vol.23 , pp. 92-98
    • Gao, S.1    Andreasen, P.A.2
  • 113
    • 0027468772 scopus 로고
    • Regulation of protease nexin-1 synthesis and secretion in cultured brain cells by injury-related factors
    • Vaughan, P.J. and Cunningham, D.D. (1993) Regulation of protease nexin-1 synthesis and secretion in cultured brain cells by injury-related factors. J. Biol. Chem., 268, 3720-3727.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3720-3727
    • Vaughan, P.J.1    Cunningham, D.D.2
  • 114
    • 0027258961 scopus 로고
    • Protease nexin-1, a thrombin inhibitor, is regulated by interleukin-1 and dexamethasone in normal human fibroblasts
    • Guttridge, D.C., Lau, A.L., and Cunningham, D.D. (1993) Protease nexin-1, a thrombin inhibitor, is regulated by interleukin-1 and dexamethasone in normal human fibroblasts. J. Biol. Chem., 268, 18966-18974.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18966-18974
    • Guttridge, D.C.1    Lau, A.L.2    Cunningham, D.D.3
  • 116
    • 0035824891 scopus 로고    scopus 로고
    • Epidermal growth factor and pro-inflammatory cytokines regulate the expression of components of plasminogen activation system in U373-MG astrocytoma cells
    • Kasza, A., Kowanetz, M., Poslednik, K., Witek, B., Kordula, T., and Koj, A. (2001) Epidermal growth factor and pro-inflammatory cytokines regulate the expression of components of plasminogen activation system in U373-MG astrocytoma cells. Cytokine, 16, 187-190.
    • (2001) Cytokine , vol.16 , pp. 187-190
    • Kasza, A.1    Kowanetz, M.2    Poslednik, K.3    Witek, B.4    Kordula, T.5    Koj, A.6
  • 117
    • 0029948143 scopus 로고    scopus 로고
    • Prevention of activity-dependent neuronal death: vasoactive intestinal polypeptide stimulates astrocytes to secrete the thrombin-inhibiting neurotrophic serpin, protease nexin I
    • Festoff, B.W., Nelson, P.G., and Brenneman, D.E. (1996) Prevention of activity-dependent neuronal death: vasoactive intestinal polypeptide stimulates astrocytes to secrete the thrombin-inhibiting neurotrophic serpin, protease nexin I. J. Neurobiol., 30, 255-266.
    • (1996) J. Neurobiol. , vol.30 , pp. 255-266
    • Festoff, B.W.1    Nelson, P.G.2    Brenneman, D.E.3
  • 118
    • 78649828934 scopus 로고    scopus 로고
    • Reprint of: Chromogranin A: a new proposal for trafficking, processing and induction of granule biogenesis
    • Koshimizu, H., Kim, T., Cawley, N.X., and Loh, Y.P. (2010) Reprint of: Chromogranin A: a new proposal for trafficking, processing and induction of granule biogenesis. Regul. Pept., 165, 95-101.
    • (2010) Regul. Pept. , vol.165 , pp. 95-101
    • Koshimizu, H.1    Kim, T.2    Cawley, N.X.3    Loh, Y.P.4
  • 119
    • 32544454980 scopus 로고    scopus 로고
    • Expression of protease nexin-1 and plasminogen activators during follicular growth and the periovulatory period in cattle
    • Cao, M., Buratini, J. Jr., Lussier, J.G., Carriere, P.D., and Price, C.A. (2006) Expression of protease nexin-1 and plasminogen activators during follicular growth and the periovulatory period in cattle. Reproduction, 131, 125-137.
    • (2006) Reproduction , vol.131 , pp. 125-137
    • Cao, M.1    Buratini, J.Jr.2    Lussier, J.G.3    Carriere, P.D.4    Price, C.A.5
  • 120
    • 65549135781 scopus 로고    scopus 로고
    • Discovery of fully human anti-MET monoclonal antibodies with antitumor activity against colon cancer tumor models in vivo
    • van der Horst, E.H., Chinn, L., Wang, M., Velilla, T., Tran, H., Madrona, Y., Lam, A., Ji, M., Hoey, T.C., and Sato, A.K. (2009) Discovery of fully human anti-MET monoclonal antibodies with antitumor activity against colon cancer tumor models in vivo. Neoplasia, 11, 355-364.
    • (2009) Neoplasia , vol.11 , pp. 355-364
    • van der Horst, E.H.1    Chinn, L.2    Wang, M.3    Velilla, T.4    Tran, H.5    Madrona, Y.6    Lam, A.7    Ji, M.8    Hoey, T.C.9    Sato, A.K.10
  • 121
    • 77957724105 scopus 로고    scopus 로고
    • The serine protease inhibitor serpinE2 is a novel target of ERK signaling involved in human colorectal tumorigenesis
    • Bergeron, S., Lemieux, E., Durand, V., Cagnol, S., Carrier, J.C., Lussier, J.G., Boucher, M.J., and Rivard, N. (2010) The serine protease inhibitor serpinE2 is a novel target of ERK signaling involved in human colorectal tumorigenesis. Mol. Cancer, 9, 271.
    • (2010) Mol. Cancer , vol.9 , pp. 271
    • Bergeron, S.1    Lemieux, E.2    Dur, V.3    Cagnol, S.4    Carrier, J.C.5    Lussier, J.G.6    Boucher, M.J.7    Rivard, N.8
  • 122
    • 0028860065 scopus 로고
    • Regulation of protease Nexin-1 expression in cultured Schwann-cells is mediated by Angiotensin-Ii receptors
    • Bleuel, A., Degasparo, M., Whitebread, S., Puttner, I., and Monard, D. (1995) Regulation of protease Nexin-1 expression in cultured Schwann-cells is mediated by Angiotensin-Ii receptors. J. Neurosci., 15, 750-761.
    • (1995) J. Neurosci. , vol.15 , pp. 750-761
    • Bleuel, A.1    Degasparo, M.2    Whitebread, S.3    Puttner, I.4    Monard, D.5
  • 123
    • 78149412476 scopus 로고    scopus 로고
    • Regulation of renal sodium handling through the interaction between serine proteases and serine protease inhibitors
    • Kitamura, K. and Tomita, K. (2010) Regulation of renal sodium handling through the interaction between serine proteases and serine protease inhibitors. Clin. Exp. Nephrol., 14, 405-410.
    • (2010) Clin. Exp. Nephrol. , vol.14 , pp. 405-410
    • Kitamura, K.1    Tomita, K.2
  • 124
    • 18344400664 scopus 로고
    • Molecular organization of the rat glia-derived nexin/protease nexin-1 promoter
    • Erno, H. and Monard, D. (1993) Molecular organization of the rat glia-derived nexin/protease nexin-1 promoter. Gene Expr., 3, 163-174.
    • (1993) Gene Expr. , vol.3 , pp. 163-174
    • Erno, H.1    Monard, D.2
  • 125
    • 0030445119 scopus 로고    scopus 로고
    • A Krox binding site regulates protease nexin-1 promoter activity in embryonic heart, cartilage and parts of the nervous system
    • Erno, H., Kury, P., Botteri, F.M., and Monard, D. (1996) A Krox binding site regulates protease nexin-1 promoter activity in embryonic heart, cartilage and parts of the nervous system. Mech. Dev., 60, 139-150.
    • (1996) Mech. Dev. , vol.60 , pp. 139-150
    • Erno, H.1    Kury, P.2    Botteri, F.M.3    Monard, D.4
  • 126
    • 33646559847 scopus 로고    scopus 로고
    • Identification of TNF-alpha-responsive NF-kappaB p65-binding element in the distal promoter of the mouse serine protease inhibitor SerpinE2
    • Suzuki, S., Singhirunnusorn, P., Nakano, H., Doi, T., Saiki, I., and Sakurai, H. (2006) Identification of TNF-alpha-responsive NF-kappaB p65-binding element in the distal promoter of the mouse serine protease inhibitor SerpinE2. FEBS Lett., 580, 3257-3262.
    • (2006) FEBS Lett. , vol.580 , pp. 3257-3262
    • Suzuki, S.1    Singhirunnusorn, P.2    Nakano, H.3    Doi, T.4    Saiki, I.5    Sakurai, H.6
  • 127
    • 43049139864 scopus 로고    scopus 로고
    • Correlative gene expression and DNA methylation profiling in lung development nominate new biomarkers in lung cancer
    • Cortese, R., Hartmann, O., Berlin, K., and Eckhardt, F. (2008) Correlative gene expression and DNA methylation profiling in lung development nominate new biomarkers in lung cancer. Int. J. Biochem. Cell Biol., 40, 1494-1508.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1494-1508
    • Cortese, R.1    Hartmann, O.2    Berlin, K.3    Eckhardt, F.4
  • 129
    • 0027379725 scopus 로고
    • Variable and multiple expression of Protease Nexin-1 during mouse organogenesis and nervous system development
    • Mansuy, I.M., van der Putten, H., Schmid, P., Meins, M., Botteri, F.M., and Monard, D. (1993) Variable and multiple expression of Protease Nexin-1 during mouse organogenesis and nervous system development. Development, 119, 1119-1134.
    • (1993) Development , vol.119 , pp. 1119-1134
    • Mansuy, I.M.1    van der Putten, H.2    Schmid, P.3    Meins, M.4    Botteri, F.M.5    Monard, D.6
  • 130
    • 0027976526 scopus 로고
    • Glia-derived nexin/protease nexin-1 is expressed by a subset of neurons in the rat brain
    • Reinhard, E., Suidan, H.S., Pavlik, A., and Monard, D. (1994) Glia-derived nexin/protease nexin-1 is expressed by a subset of neurons in the rat brain. J. Neurosci. Res., 37, 256-270.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 256-270
    • Reinhard, E.1    Suidan, H.S.2    Pavlik, A.3    Monard, D.4
  • 131
    • 77956291596 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 regulates tumor cell invasion through cleavage of protease nexin-1
    • Xu, D., McKee, C.M., Cao, Y., Ding, Y., Kessler, B.M., and Muschel, R.J. (2010) Matrix metalloproteinase-9 regulates tumor cell invasion through cleavage of protease nexin-1. Cancer Res., 70, 6988-6998.
    • (2010) Cancer Res. , vol.70 , pp. 6988-6998
    • Xu, D.1    McKee, C.M.2    Cao, Y.3    Ding, Y.4    Kessler, B.M.5    Muschel, R.J.6
  • 133
    • 0036135037 scopus 로고    scopus 로고
    • Coordinate expression of anticoagulant heparan sulfate proteoglycans and serine protease inhibitors in the rat ovary: a potent system of proteolysis control
    • Hasan, S., Hosseini, G., Princivalle, M., Dong, J.C., Birsan, D., Cagide, C., and de Agostini, A.I. (2002) Coordinate expression of anticoagulant heparan sulfate proteoglycans and serine protease inhibitors in the rat ovary: a potent system of proteolysis control. Biol. Reprod., 66, 144-158.
    • (2002) Biol. Reprod. , vol.66 , pp. 144-158
    • Hasan, S.1    Hosseini, G.2    Princivalle, M.3    Dong, J.C.4    Birsan, D.5    Cagide, C.6    de Agostini, A.I.7
  • 134
    • 0028347947 scopus 로고
    • Neuronalexpression of protease-nexin 1 mRNA in rat brain
    • Simpson, C.S., Johnston, H.M., and Morris, B.J. (1994) Neuronal expression of protease-nexin 1 mRNA in rat brain. Neurosci. Lett., 170, 286-290.
    • (1994) Neurosci. Lett. , vol.170 , pp. 286-290
    • Simpson, C.S.1    Johnston, H.M.2    Morris, B.J.3
  • 136
    • 0024520904 scopus 로고
    • A form of protease nexin I is expressed on the platelet surface during platelet activation
    • Gronke, R.S., Knauer, D.J., Veeraraghavan, S., and Baker, J.B. (1989) A form of protease nexin I is expressed on the platelet surface during platelet activation. Blood, 73, 472-478.
    • (1989) Blood , vol.73 , pp. 472-478
    • Gronke, R.S.1    Knauer, D.J.2    Veeraraghavan, S.3    Baker, J.B.4
  • 138
    • 0023009664 scopus 로고
    • Protease nexins and cellular regulation
    • Baker, J.B. and Gronke, R.S. (1986) Protease nexins and cellular regulation. Semin. Thromb. Hemost., 12, 216-220.
    • (1986) Semin. Thromb. Hemost. , vol.12 , pp. 216-220
    • Baker, J.B.1    Gronke, R.S.2
  • 139
    • 79952179780 scopus 로고    scopus 로고
    • SERPINE2, a serine protease inhibitor extensively expressed in adult male mouse reproductive tissues, may serve as a murine sperm decapacitation factor
    • Lu, C.H., Lee, R.K., Hwu, Y.M., Chu, S.L., Chen, Y.J., Chang, W.C., Lin, S.P., and Li, S.H. (2010) SERPINE2, a serine protease inhibitor extensively expressed in adult male mouse reproductive tissues, may serve as a murine sperm decapacitation factor. Biol. Reprod., 84, 514-25.
    • (2010) Biol. Reprod. , vol.84 , pp. 514-25
    • Lu, C.H.1    Lee, R.K.2    Hwu, Y.M.3    Chu, S.L.4    Chen, Y.J.5    Chang, W.C.6    Lin, S.P.7    Li, S.H.8
  • 140
    • 6344233788 scopus 로고    scopus 로고
    • Seminal clotting and fibrinolytic balance: a possible physiological role in the male reproductive system
    • Lwaleed, B.A., Greenfield, R., Stewart, A., Birch, B., and Cooper, A.J. (2004) Seminal clotting and fibrinolytic balance: a possible physiological role in the male reproductive system. Thromb. Haemost., 92, 752-766.
    • (2004) Thromb. Haemost. , vol.92 , pp. 752-766
    • Lwaleed, B.A.1    Greenfield, R.2    Stewart, A.3    Birch, B.4    Cooper, A.J.5
  • 141
    • 48249132757 scopus 로고    scopus 로고
    • Protease nexin-1 in reproductive tissues: a review
    • Price, C.A. (2008) Protease nexin-1 in reproductive tissues: a review. ARBS Annu. Rev. Biomed. Sci., 10, 75-83.
    • (2008) ARBS Annu. Rev. Biomed. Sci. , vol.10 , pp. 75-83
    • Price, C.A.1
  • 142
    • 0023263508 scopus 로고
    • Identification of a protease inhibitor produced by astrocytes that is structurally and functionally homologous to human protease nexin-I
    • Rosenblatt, D.E., Cotman, C.W., Nieto-Sampedro, M., Rowe, J.W., and Knauer, D.J. (1987) Identification of a protease inhibitor produced by astrocytes that is structurally and functionally homologous to human protease nexin-I. Brain Res., 415, 40-48.
    • (1987) Brain Res. , vol.415 , pp. 40-48
    • Rosenblatt, D.E.1    Cotman, C.W.2    Nieto Sampedro, M.3    Rowe, J.W.4    Knauer, D.J.5
  • 143
    • 0024039223 scopus 로고
    • Detection of glia-derived nexin in the olfactory system of the rat
    • Reinhard, E., Meier, R., Halfter, W., Rovelli, G., and Monard, D. (1988) Detection of glia-derived nexin in the olfactory system of the rat. Neuron, 1, 387-394.
    • (1988) Neuron , vol.1 , pp. 387-394
    • Reinhard, E.1    Meier, R.2    Halfter, W.3    Rovelli, G.4    Monard, D.5
  • 144
    • 1842377452 scopus 로고    scopus 로고
    • Protease nexin-1 is expressed at the mouse met-/mesencephalic junction and FGF signaling regulates its promoter activity in primary met-/mesencephalic cells
    • Kury, P., Schaeren-Wiemers, N., and Monard, D. (1997) Protease nexin-1 is expressed at the mouse met-/mesencephalic junction and FGF signaling regulates its promoter activity in primary met-/mesencephalic cells. Development, 124, 1251-1262.
    • (1997) Development , vol.124 , pp. 1251-1262
    • Kury, P.1    Schaeren Wiemers, N.2    Monard, D.3
  • 145
    • 77954376350 scopus 로고    scopus 로고
    • Newly generated cells are increased in hippocampus of adult mice lacking a serine protease inhibitor
    • Lino, M.M., Vaillant, C., Orolicki, S., Sticker, M., Kvajo, M., and Monard, D. (2010) Newly generated cells are increased in hippocampus of adult mice lacking a serine protease inhibitor. BMC Neurosci., 11, 70.
    • (2010) BMC Neurosci. , vol.11 , pp. 70
    • Lino, M.M.1    Vaillant, C.2    Orolicki, S.3    Sticker, M.4    Kvajo, M.5    Monard, D.6
  • 149
    • 0027067802 scopus 로고
    • Relevance of the balance between glia-derived nexin and thrombin following lesion in the nervous system
    • Monard, D., Suidan, H.S., and Nitsch, C. (1992) Relevance of the balance between glia-derived nexin and thrombin following lesion in the nervous system. Ann. N.Y. Acad. Sci., 674, 237-242.
    • (1992) Ann. N.Y. Acad. Sci. , vol.674 , pp. 237-242
    • Monard, D.1    Suidan, H.S.2    Nitsch, C.3
  • 150
    • 0027829445 scopus 로고
    • Tinkering with certain blood components can engender distinct functions in the nervous system
    • Monard, D. (1993) Tinkering with certain blood components can engender distinct functions in the nervous system. Perspect Dev. Neurobiol., 1, 165-168.
    • (1993) Perspect Dev. Neurobiol. , vol.1 , pp. 165-168
    • Monard, D.1
  • 151
    • 0030007646 scopus 로고    scopus 로고
    • Thrombin, its receptor and protease nexin I, its potent serpin, in the nervous system
    • Festoff, B.W., Smirnova, I.V., Ma, J., and Citron, B.A. (1996) Thrombin, its receptor and protease nexin I, its potent serpin, in the nervous system. Semin. Thromb. Hemost., 22, 267-271.
    • (1996) Semin. Thromb. Hemost. , vol.22 , pp. 267-271
    • Festoff, B.W.1    Smirnova, I.V.2    Ma, J.3    Citron, B.A.4
  • 152
    • 0030829885 scopus 로고    scopus 로고
    • The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system
    • Turgeon, V.L. and Houenou, L.J. (1997) The role of thrombin-like (serine) proteases in the development, plasticity and pathology of the nervous system. Brain Res. Brain Res. Rev., 25, 85-95.
    • (1997) Brain Res. Brain Res. Rev. , vol.25 , pp. 85-95
    • Turgeon, V.L.1    Houenou, L.J.2
  • 153
    • 44649148254 scopus 로고    scopus 로고
    • The expression and the role of protease nexin-1 on brain edema after intracerebral hemorrhage
    • Wu, H., Zhao, R., Qi, J., Cong, Y., Wang, D., Liu, T., Gu, Y., Ban, X., and Huang, Q. (2008) The expression and the role of protease nexin-1 on brain edema after intracerebral hemorrhage. J. Neurol. Sci., 270, 172-183.
    • (2008) J. Neurol. Sci. , vol.270 , pp. 172-183
    • Wu, H.1    Zhao, R.2    Qi, J.3    Cong, Y.4    Wang, D.5    Liu, T.6    Gu, Y.7    Ban, X.8    Huang, Q.9
  • 155
    • 0024435558 scopus 로고
    • Protease nexin I immunostaining in Alzheimer's disease
    • Rosenblatt, D.E., Geula, C., and Mesulam, M.M. (1989) Protease nexin I immunostaining in Alzheimer's disease. Ann. Neurol., 26, 628-634.
    • (1989) Ann. Neurol. , vol.26 , pp. 628-634
    • Rosenblatt, D.E.1    Geula, C.2    Mesulam, M.M.3
  • 156
    • 0028566867 scopus 로고
    • Protease nexin-1, a potent thrombin inhibitor, is reduced around cerebral blood vessels in Alzheimer's disease
    • Vaughan, P.J., Su, J., Cotman, C.W., and Cunningham, D.D. (1994) Protease nexin-1, a potent thrombin inhibitor, is reduced around cerebral blood vessels in Alzheimer's disease. Brain Res., 668, 160-170.
    • (1994) Brain Res. , vol.668 , pp. 160-170
    • Vaughan, P.J.1    Su, J.2    Cotman, C.W.3    Cunningham, D.D.4
  • 159
    • 34247634088 scopus 로고    scopus 로고
    • Protease nexin-1 interacts with thrombomodulin and modulates its anticoagulant effect
    • Bouton, M.C., Venisse, L., Richard, B., Pouzet, C., Arocas, V., and Jandrot-Perrus, M. (2007) Protease nexin-1 interacts with thrombomodulin and modulates its anticoagulant effect. Circ. Res., 100, 1174-1181.
    • (2007) Circ. Res. , vol.100 , pp. 1174-1181
    • Bouton, M.C.1    Venisse, L.2    Richard, B.3    Pouzet, C.4    Arocas, V.5    Jandrot Perrus, M.6
  • 161
  • 162
    • 0042440692 scopus 로고    scopus 로고
    • SERPINE2 (protease nexin I) promotes extracellular matrix production and local invasion of pancreatic tumors in vivo
    • Buchholz, M., Biebl, A., Neesse, A., Wagner, M., Iwamura, T., Leder, G., Adler, G., and Gress, T.M. (2003) SERPINE2 (protease nexin I) promotes extracellular matrix production and local invasion of pancreatic tumors in vivo
    • (2003) Cancer Res. , vol.63 , pp. 4945-4951
    • Buchholz, M.1    Biebl, A.2    Neesse, A.3    Wagner, M.4    Iwamura, T.5    Leder, G.6    Adler, G.7    Gress, T.M.8
  • 165
    • 0344069652 scopus 로고    scopus 로고
    • Identification of genes differentially expressed in TLS-CHOP carrying myxoid liposarcomas
    • Thelin-Jarnum, S., Lassen, C., Panagopoulos, I., Mandahl, N., and Aman, P. (1999) Identification of genes differentially expressed in TLS-CHOP carrying myxoid liposarcomas. Int. J. Cancer, 83, 30-33.
    • (1999) Int. J. Cancer , vol.83 , pp. 30-33
    • Thelin Jarnum, S.1    Lassen, C.2    Panagopoulos, I.3    Mandahl, N.4    Aman, P.5
  • 166
    • 52149124653 scopus 로고    scopus 로고
    • Prognostic breast cancer signature identified from 3D culture model accurately predicts clinical outcome across independent datasets
    • Martin, K.J., Patrick, D.R., Bissell, M.J., and Fournier, M.V. (2008) Prognostic breast cancer signature identified from 3D culture model accurately predicts clinical outcome across independent datasets. PLoS ONE, 3, e2994.
    • (2008) PLoS ONE , vol.3
    • Martin, K.J.1    Patrick, D.R.2    Bissell, M.J.3    Fournier, M.V.4
  • 169
    • 62549110829 scopus 로고    scopus 로고
    • Establishment of an experimental human lung adenocarcinoma cell line SPC-A-1BM with high bone metastases potency by (99m)Tc-MDP bone scintigraphy
    • Yang, S., Dong, Q., Yao, M., Shi, M., Ye, J., Zhao, L., Su, J., Gu, W., Xie, W., Wang, K., Du, Y., Li, Y., and Huang, Y. (2009) Establishment of an experimental human lung adenocarcinoma cell line SPC-A-1BM with high bone metastases potency by (99m)Tc-MDP bone scintigraphy. Nucl. Med. Biol., 36, 313-321.
    • (2009) Nucl. Med. Biol. , vol.36 , pp. 313-321
    • Yang, S.1    Dong, Q.2    Yao, M.3    Shi, M.4    Ye, J.5    Zhao, L.6    Su, J.7    Gu, W.8    Xie, W.9    Wang, K.10    Du, Y.11    Li, Y.12    Huang, Y.13
  • 171
    • 0037466532 scopus 로고    scopus 로고
    • Identification of genes associated with adenovirus 12 tumorigenesis by microarray
    • Guan, H., Smirnov, D.A., and Ricciardi, R.P. (2003) Identification of genes associated with adenovirus 12 tumorigenesis by microarray. Virology, 309, 114-124.
    • (2003) Virology , vol.309 , pp. 114-124
    • Guan, H.1    Smirnov, D.A.2    Ricciardi, R.P.3
  • 172
    • 59449107627 scopus 로고    scopus 로고
    • Identification and quantification of proteins differentially secreted by a pair of normal and malignant breast-cancer cell lines
    • Liang, X., Huuskonen, J., Hajivandi, M., Manzanedo, R., Predki, P., Amshey, J.R., and Pope, R.M. (2009) Identification and quantification of proteins differentially secreted by a pair of normal and malignant breast-cancer cell lines. Proteomics, 9, 182-193.
    • (2009) Proteomics , vol.9 , pp. 182-193
    • Liang, X.1    Huuskonen, J.2    Hajivandi, M.3    Manzanedo, R.4    Predki, P.5    Amshey, J.R.6    Pope, R.M.7
  • 173
    • 34748824978 scopus 로고    scopus 로고
    • Pancreatic stellate cells potentiate proinvasive effects of SERPINE2 expression in pancreatic cancer xenograft tumors
    • Neesse, A., Wagner, M., Ellenrieder, V., Bachem, M., Gress, T.M., and Buchholz, M. (2007) Pancreatic stellate cells potentiate proinvasive effects of SERPINE2 expression in pancreatic cancer xenograft tumors. Pancreatology, 7, 380-385.
    • (2007) Pancreatology , vol.7 , pp. 380-385
    • Neesse, A.1    Wagner, M.2    Ellenrieder, V.3    Bachem, M.4    Gress, T.M.5    Buchholz, M.6
  • 174
    • 78651385353 scopus 로고    scopus 로고
    • Pancreatic cancer: the role of pancreatic stellate cells in tumor progression
    • Duner, S., Lopatko Lindman, J., Ansari, D., Gundewar, C., and Andersson, R. (2011) Pancreatic cancer: the role of pancreatic stellate cells in tumor progression. Pancreatology, 10, 673-681.
    • (2011) Pancreatology , vol.10 , pp. 673-681
    • Duner, S.1    Lopatko Lindman, J.2    Ansari, D.3    Gundewar, C.4    Andersson, R.5
  • 175
    • 57049104077 scopus 로고    scopus 로고
    • Novel MMP-9 substrates in cancer cells revealed by a label-free quantitative proteomics approach
    • Xu, D., Suenaga, N., Edelmann, M.J., Fridman, R., Muschel, R.J., and Kessler, B.M. (2008) Novel MMP-9 substrates in cancer cells revealed by a label-free quantitative proteomics approach. Mol. Cell Proteomics, 7, 2215-2228.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 2215-2228
    • Xu, D.1    Suenaga, N.2    Edelmann, M.J.3    Fridman, R.4    Muschel, R.J.5    Kessler, B.M.6


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