메뉴 건너뛰기




Volumn 5, Issue 7, 2010, Pages

Quantifying the proteolytic release of extracellular matrix-sequestered VEGF with a computational model

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE; NEUROPILIN 1; PLASMIN; PROTEINASE; PROTEOHEPARAN SULFATE; UNCLASSIFIED DRUG; VASCULOTROPIN; VASCULOTROPIN 114; VASCULOTROPIN 165; VASCULOTROPIN RECEPTOR;

EID: 77955636443     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011860     Document Type: Article
Times cited : (62)

References (97)
  • 1
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers G, Brekken R, McMahon G, Vu TH, Itoh T, et al. (2000) Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol 2: 737-744.
    • (2000) Nat Cell Biol , vol.2 , pp. 737-744
    • Bergers, G.1    Brekken, R.2    McMahon, G.3    Vu, T.H.4    Itoh, T.5
  • 2
    • 0027064888 scopus 로고
    • Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms
    • Houck KA, Leung DW, Rowland AM, Winer J, Ferrara N (1992) Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms. J Biol Chem 267: 26031-26037.
    • (1992) J Biol Chem , vol.267 , pp. 26031-26037
    • Houck, K.A.1    Leung, D.W.2    Rowland, A.M.3    Winer, J.4    Ferrara, N.5
  • 3
    • 22344437713 scopus 로고    scopus 로고
    • Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors
    • Lee S, Jilani SM, Nikolova GV, Carpizo D, Iruela-Arispe ML (2005) Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. J Cell Biol 169: 681-691.
    • (2005) J Cell Biol , vol.169 , pp. 681-691
    • Lee, S.1    Jilani, S.M.2    Nikolova, G.V.3    Carpizo, D.4    Iruela-Arispe, M.L.5
  • 4
    • 0027751890 scopus 로고
    • The vascular endothelial growth factor (VEGF) isoforms: Differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF
    • Park JE, Keller GA, Ferrara N (1993) The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF. Mol Biol Cell 4: 1317-1326.
    • (1993) Mol Biol Cell , vol.4 , pp. 1317-1326
    • Park, J.E.1    Keller, G.A.2    Ferrara, N.3
  • 5
    • 0037108152 scopus 로고    scopus 로고
    • Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis
    • Ruhrberg C, Gerhardt H, Golding M, Watson R, Ioannidou S, et al. (2002) Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. Genes Dev 16: 2684-2698.
    • (2002) Genes Dev , vol.16 , pp. 2684-2698
    • Ruhrberg, C.1    Gerhardt, H.2    Golding, M.3    Watson, R.4    Ioannidou, S.5
  • 6
    • 0029937679 scopus 로고    scopus 로고
    • The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency
    • Keyt BA, Berleau LT, Nguyen HV, Chen H, Heinsohn H, et al. (1996) The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency. J Biol Chem 271: 7788-7795.
    • (1996) J Biol Chem , vol.271 , pp. 7788-7795
    • Keyt, B.A.1    Berleau, L.T.2    Nguyen, H.V.3    Chen, H.4    Heinsohn, H.5
  • 7
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M (1998) Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 92: 735-745.
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 8
    • 49549089512 scopus 로고    scopus 로고
    • VEGF release by MMP-9 mediated heparan sulphate cleavage induces colorectal cancer angiogenesis
    • Hawinkels LJ, Zuidwijk K, Verspaget HW, de Jonge-Muller ES, van Duijn W, et al. (2008) VEGF release by MMP-9 mediated heparan sulphate cleavage induces colorectal cancer angiogenesis. Eur J Cancer 44: 1904-1913.
    • (2008) Eur J Cancer , vol.44 , pp. 1904-1913
    • Hawinkels, L.J.1    Zuidwijk, K.2    Verspaget, H.W.3    de Jonge-Muller, E.S.4    van Duijn, W.5
  • 9
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock JM, Murdoch AD, Iozzo RV, Underwood PA (1996) The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J Biol Chem 271: 10079-10086.
    • (1996) J Biol Chem , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 10
    • 4544340505 scopus 로고    scopus 로고
    • Type I collagen can function as a reservoir of basic fibroblast growth factor
    • Kanematsu A, Marui A, Yamamoto S, Ozeki M, Hirano Y, et al. (2004) Type I collagen can function as a reservoir of basic fibroblast growth factor. J Control Release 99: 281-292.
    • (2004) J Control Release , vol.99 , pp. 281-292
    • Kanematsu, A.1    Marui, A.2    Yamamoto, S.3    Ozeki, M.4    Hirano, Y.5
  • 11
    • 28444480280 scopus 로고    scopus 로고
    • Theimpactof proteinase-induced matrix degradation on the release of VEGF from heparinized collagen matrices
    • Yao C, Roderfeld M, Rath T, Roeb E, Bernhagen J, et al.(2006) Theimpactof proteinase-induced matrix degradation on the release of VEGF from heparinized collagen matrices. Biomaterials 27: 1608-1616.
    • (2006) Biomaterials , vol.27 , pp. 1608-1616
    • Yao, C.1    Roderfeld, M.2    Rath, T.3    Roeb, E.4    Bernhagen, J.5
  • 12
    • 0033646579 scopus 로고    scopus 로고
    • Controlled release of vascular endothelial growth factor by use of collagen hydrogels
    • Tabata Y, Miyao M, Ozeki M, Ikada Y (2000) Controlled release of vascular endothelial growth factor by use of collagen hydrogels. J Biomater Sci Polym Ed 11: 915-930.
    • (2000) J Biomater Sci Polym Ed , vol.11 , pp. 915-930
    • Tabata, Y.1    Miyao, M.2    Ozeki, M.3    Ikada, Y.4
  • 13
    • 0037815292 scopus 로고    scopus 로고
    • VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia
    • Gerhardt H, Golding M, Fruttiger M, Ruhrberg C, Lundkvist A, et al. (2003) VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia. J Cell Biol 161: 1163-1177.
    • (2003) J Cell Biol , vol.161 , pp. 1163-1177
    • Gerhardt, H.1    Golding, M.2    Fruttiger, M.3    Ruhrberg, C.4    Lundkvist, A.5
  • 15
    • 0042704757 scopus 로고    scopus 로고
    • Extracellular matrix-bound vascular endothelial growth factor promotes endothelial cell adhesion, migration, and survival through integrin ligation
    • Hutchings H, Ortega N, Plouet J (2003) Extracellular matrix-bound vascular endothelial growth factor promotes endothelial cell adhesion, migration, and survival through integrin ligation. FASEB J17: 1520-1522.
    • (2003) FASEB , vol.J17 , pp. 1520-1522
    • Hutchings, H.1    Ortega, N.2    Plouet, J.3
  • 16
    • 77149150968 scopus 로고    scopus 로고
    • Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells
    • Chen TT, Luque A, Lee S, Anderson SM, Segura T, et al. (2010) Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells. J Cell Biol 188: 595-609.
    • (2010) J Cell Biol , vol.188 , pp. 595-609
    • Chen, T.T.1    Luque, A.2    Lee, S.3    Anderson, S.M.4    Segura, T.5
  • 18
    • 0035940429 scopus 로고    scopus 로고
    • Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor
    • Rodriguez-Manzaneque JC, Lane TF, Ortega MA, Hynes RO, Lawler J, et al. (2001) Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor. Proc Natl Acad Sci U S A 98: 12485-12490.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12485-12490
    • Rodriguez-Manzaneque, J.C.1    Lane, T.F.2    Ortega, M.A.3    Hynes, R.O.4    Lawler, J.5
  • 19
    • 27644453468 scopus 로고    scopus 로고
    • Synergy between interstitial flow and VEGF directs capillary morphogenesis in vitro through a gradient amplification mechanism
    • Helm CL, Fleury ME, Zisch AH, Boschetti F, Swartz MA (2005) Synergy between interstitial flow and VEGF directs capillary morphogenesis in vitro through a gradient amplification mechanism. Proc Natl Acad Sci U S A 102: 15779-15784.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15779-15784
    • Helm, C.L.1    Fleury, M.E.2    Zisch, A.H.3    Boschetti, F.4    Swartz, M.A.5
  • 20
    • 33144457649 scopus 로고    scopus 로고
    • Plasmin modulates vascular endothelial growth factor-A-mediated angiogenesis during wound repair
    • Roth D, Piekarek M, Paulsson M, Christ H, Bloch W, et al. (2006) Plasmin modulates vascular endothelial growth factor-A-mediated angiogenesis during wound repair. Am J Pathol 168: 670-684.
    • (2006) Am J Pathol , vol.168 , pp. 670-684
    • Roth, D.1    Piekarek, M.2    Paulsson, M.3    Christ, H.4    Bloch, W.5
  • 21
    • 0033910462 scopus 로고    scopus 로고
    • Expression and proteolysis of vascular endothelial growth factor is increased in chronic wounds
    • Lauer G, Sollberg S, Cole M, Flamme I, Sturzebecher J, et al. (2000) Expression and proteolysis of vascular endothelial growth factor is increased in chronic wounds. J Invest Dermatol 115: 12-18.
    • (2000) J Invest Dermatol , vol.115 , pp. 12-18
    • Lauer, G.1    Sollberg, S.2    Cole, M.3    Flamme, I.4    Sturzebecher, J.5
  • 23
    • 0030976894 scopus 로고    scopus 로고
    • Extracellular cleavage of the vascular endothelial growth factor 189-amino acid form by urokinase is required for its mitogenic effect
    • Plouet J, Moro F, Bertagnolli S, Coldeboeuf N, Mazarguil H, et al. (1997) Extracellular cleavage of the vascular endothelial growth factor 189-amino acid form by urokinase is required for its mitogenic effect. J Biol Chem 272: 13390-13396.
    • (1997) J Biol Chem , vol.272 , pp. 13390-13396
    • Plouet, J.1    Moro, F.2    Bertagnolli, S.3    Coldeboeuf, N.4    Mazarguil, H.5
  • 24
    • 0037183997 scopus 로고    scopus 로고
    • Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165
    • Hashimoto G, Inoki I, Fujii Y, Aoki T, Ikeda E, et al. (2002) Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165. J Biol Chem 277: 36288-36295.
    • (2002) J Biol Chem , vol.277 , pp. 36288-36295
    • Hashimoto, G.1    Inoki, I.2    Fujii, Y.3    Aoki, T.4    Ikeda, E.5
  • 25
    • 0025318680 scopus 로고
    • Release of basic fibroblast growth factor-heparan sulfate complexes from endothelial cells by plasminogen activator-mediated proteolytic activity
    • Saksela O, Rifkin DB (1990) Release of basic fibroblast growth factor-heparan sulfate complexes from endothelial cells by plasminogen activator-mediated proteolytic activity. J Cell Biol 110: 767-775.
    • (1990) J Cell Biol , vol.110 , pp. 767-775
    • Saksela, O.1    Rifkin, D.B.2
  • 26
    • 1842416597 scopus 로고    scopus 로고
    • Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase
    • Gronski TJ, Jr., Martin RL, Kobayashi DK, Walsh BC, Holman MC, et al. (1997) Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase. J Biol Chem 272: 12189-12194.
    • (1997) J Biol Chem , vol.272 , pp. 12189-12194
    • Gronski Jr., T.J.1    Martin, R.L.2    Kobayashi, D.K.3    Walsh, B.C.4    Holman, M.C.5
  • 27
    • 33644977975 scopus 로고    scopus 로고
    • VEGF165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase
    • Robinson CJ, Mulloy B, Gallagher JT, Stringer SE (2006) VEGF165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by K5 lyase. J Biol Chem 281: 1731-1740.
    • (2006) J Biol Chem , vol.281 , pp. 1731-1740
    • Robinson, C.J.1    Mulloy, B.2    Gallagher, J.T.3    Stringer, S.E.4
  • 28
    • 0642272484 scopus 로고    scopus 로고
    • Cell-demanded release of VEGF from synthetic, biointeractive cell ingrowth matrices for vascularized tissue growth
    • Zisch AH, Lutolf MP, Ehrbar M, Raeber GP, Rizzi SC, et al. (2003) Cell-demanded release of VEGF from synthetic, biointeractive cell ingrowth matrices for vascularized tissue growth. FASEB J17: 2260-2262.
    • (2003) FASEB , vol.J17 , pp. 2260-2262
    • Zisch, A.H.1    Lutolf, M.P.2    Ehrbar, M.3    Raeber, G.P.4    Rizzi, S.C.5
  • 29
    • 2342623399 scopus 로고    scopus 로고
    • Cell-demanded liberation of VEGF121 from fibrin implants induces local and controlled blood vessel growth
    • Ehrbar M, Djonov VG, Schnell C, Tschanz SA, Martiny-Baron G, et al. (2004) Cell-demanded liberation of VEGF121 from fibrin implants induces local and controlled blood vessel growth. Circ Res 94: 1124-1132.
    • (2004) Circ Res , vol.94 , pp. 1124-1132
    • Ehrbar, M.1    Djonov, V.G.2    Schnell, C.3    Tschanz, S.A.4    Martiny-Baron, G.5
  • 30
    • 33747602354 scopus 로고    scopus 로고
    • Infiltrating neutrophils mediate the initial angiogenic switch in a mouse model of multistage carcinogenesis
    • Nozawa H, Chiu C, Hanahan D (2006) Infiltrating neutrophils mediate the initial angiogenic switch in a mouse model of multistage carcinogenesis. Proc Natl Acad Sci U S A 103: 12493-12498.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 12493-12498
    • Nozawa, H.1    Chiu, C.2    Hanahan, D.3
  • 31
    • 4944239035 scopus 로고    scopus 로고
    • An amino-bisphosphonate targets MMP-9-expressing macrophages and angiogenesis to impair cervical carcino-genesis
    • Giraudo E, Inoue M, Hanahan D (2004) An amino-bisphosphonate targets MMP-9-expressing macrophages and angiogenesis to impair cervical carcino-genesis. J Clin Invest 114: 623-633.
    • (2004) J Clin Invest , vol.114 , pp. 623-633
    • Giraudo, E.1    Inoue, M.2    Hanahan, D.3
  • 32
    • 50849090319 scopus 로고    scopus 로고
    • Macrophages define the invasive microenvironment in breast cancer
    • Pollard JW (2008) Macrophages define the invasive microenvironment in breast cancer. J Leukoc Biol 84: 623-630.
    • (2008) J Leukoc Biol , vol.84 , pp. 623-630
    • Pollard, J.W.1
  • 33
    • 40449120260 scopus 로고    scopus 로고
    • A new ELISA for use in a 3-ELISA system to assess concentrations of VEGF splice variants and VEGF(110) in ovarian cancer tumors
    • Gutierrez J, Konecny GE, Hong K, Burges A, Henry TD, et al. (2008) A new ELISA for use in a 3-ELISA system to assess concentrations of VEGF splice variants and VEGF(110) in ovarian cancer tumors. Clin Chem 54: 597-601.
    • (2008) Clin Chem , vol.54 , pp. 597-601
    • Gutierrez, J.1    Konecny, G.E.2    Hong, K.3    Burges, A.4    Henry, T.D.5
  • 34
    • 0037032431 scopus 로고    scopus 로고
    • Generationofanovel proteolysis resistant vascular endothelial growth factor165 variant by a site-directed mutation at the plasmin sensitive cleavage site
    • Lauer G, Sollberg S, Cole M, Krieg T, Eming SA (2002) Generationofanovel proteolysis resistant vascular endothelial growth factor165 variant by a site-directed mutation at the plasmin sensitive cleavage site. FEBS Lett 531: 309-313.
    • (2002) FEBS Lett , vol.531 , pp. 309-313
    • Lauer, G.1    Sollberg, S.2    Cole, M.3    Krieg, T.4    Eming, S.A.5
  • 36
    • 0033838376 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and related tissue inhibitors in the cyst fluids of ovarian mucinous neoplasms
    • Furuya M, Ishikura H, Kawarada Y, Ogawa Y, Sakuragi N, et al. (2000) Expression of matrix metalloproteinases and related tissue inhibitors in the cyst fluids of ovarian mucinous neoplasms. Gynecol Oncol 78: 106-112.
    • (2000) Gynecol Oncol , vol.78 , pp. 106-112
    • Furuya, M.1    Ishikura, H.2    Kawarada, Y.3    Ogawa, Y.4    Sakuragi, N.5
  • 37
    • 43149096265 scopus 로고    scopus 로고
    • Trypsin, elastase, plasmin and MMP-9 activity in the serum during the human ageing process
    • Paczek L, Michalska W, Bartlomiejczyk I (2008) Trypsin, elastase, plasmin and MMP-9 activity in the serum during the human ageing process. Age Ageing 37: 318-323.
    • (2008) Age Ageing , vol.37 , pp. 318-323
    • Paczek, L.1    Michalska, W.2    Bartlomiejczyk, I.3
  • 39
    • 1942501856 scopus 로고    scopus 로고
    • Increased matrix metalloproteinase-9 concentration and activity after stimulation with interleukin-17 in mouse airways
    • Prause O, Bozinovski S, Anderson GP, Linden A (2004) Increased matrix metalloproteinase-9 concentration and activity after stimulation with interleukin-17 in mouse airways. Thorax 59: 313-317.
    • (2004) Thorax , vol.59 , pp. 313-317
    • Prause, O.1    Bozinovski, S.2    Anderson, G.P.3    Linden, A.4
  • 40
    • 0036841677 scopus 로고    scopus 로고
    • Cardiac remodelling in end stage heart failure: Upregulation of matrix metalloproteinase (MMP) irrespective of the underlying disease, and evidence for a direct inhibitory effect of ACE inhibitors on MMP
    • Reinhardt D, Sigusch HH, Hensse J, Tyagi SC, Korfer R, et al. (2002) Cardiac remodelling in end stage heart failure: upregulation of matrix metalloproteinase (MMP) irrespective of the underlying disease, and evidence for a direct inhibitory effect of ACE inhibitors on MMP. Heart 88: 525-530.
    • (2002) Heart , vol.88 , pp. 525-530
    • Reinhardt, D.1    Sigusch, H.H.2    Hensse, J.3    Tyagi, S.C.4    Korfer, R.5
  • 41
    • 33748550328 scopus 로고    scopus 로고
    • Combined determination of plasma MMP2, MMP9, and TIMP1 improves the non-invasive detection of transitional cell carcinoma of the bladder
    • Staack A, Badendieck S, Schnorr D, Loening SA, Jung K (2006) Combined determination of plasma MMP2, MMP9, and TIMP1 improves the non-invasive detection of transitional cell carcinoma of the bladder. BMC Urol 6: 19.
    • (2006) BMC Urol , vol.6 , pp. 19
    • Staack, A.1    Badendieck, S.2    Schnorr, D.3    Loening, S.A.4    Jung, K.5
  • 42
    • 37249059009 scopus 로고    scopus 로고
    • Newly identified biologically active and proteolysis-resistant VEGF-A isoform VEGF111 is induced by genotoxic agents
    • Mineur P, Colige AC, Deroanne CF, Dubail J, Kesteloot F, et al. (2007) Newly identified biologically active and proteolysis-resistant VEGF-A isoform VEGF111 is induced by genotoxic agents. J Cell Biol 179: 1261-1273.
    • (2007) J Cell Biol , vol.179 , pp. 1261-1273
    • Mineur, P.1    Colige, A.C.2    Deroanne, C.F.3    Dubail, J.4    Kesteloot, F.5
  • 43
    • 38749138430 scopus 로고    scopus 로고
    • The role of actively released fibrin-conjugated VEGF for VEGF receptor 2 gene activation and the enhancement of angiogenesis
    • Ehrbar M, Zeisberger SM, Raeber GP, Hubbell JA, Schnell C, et al. (2008) The role of actively released fibrin-conjugated VEGF for VEGF receptor 2 gene activation and the enhancement of angiogenesis. Biomaterials 29: 1720-1729.
    • (2008) Biomaterials , vol.29 , pp. 1720-1729
    • Ehrbar, M.1    Zeisberger, S.M.2    Raeber, G.P.3    Hubbell, J.A.4    Schnell, C.5
  • 45
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu Q, Stamenkovic I (1999) Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev 13: 35-48.
    • (1999) Genes Dev , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 47
    • 0042330309 scopus 로고    scopus 로고
    • Inducible expression of tissue inhibitor of metalloproteinases-resistant matrix metalloproteinase-9 on the cell surface of neutrophils
    • Owen CA, Hu Z, Barrick B, Shapiro SD (2003) Inducible expression of tissue inhibitor of metalloproteinases-resistant matrix metalloproteinase-9 on the cell surface of neutrophils. Am J Respir Cell Mol Biol 29: 283-294.
    • (2003) Am J Respir Cell Mol Biol , vol.29 , pp. 283-294
    • Owen, C.A.1    Hu, Z.2    Barrick, B.3    Shapiro, S.D.4
  • 48
    • 2942536116 scopus 로고    scopus 로고
    • Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase
    • Owen CA, Hu Z, Lopez-Otin C, Shapiro SD (2004) Membrane-bound matrix metalloproteinase-8 on activated polymorphonuclear cells is a potent, tissue inhibitor of metalloproteinase-resistant collagenase and serpinase. J Immunol 172: 7791-7803.
    • (2004) J Immunol , vol.172 , pp. 7791-7803
    • Owen, C.A.1    Hu, Z.2    Lopez-Otin, C.3    Shapiro, S.D.4
  • 49
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I (2000) Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 14: 163-176.
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 50
    • 28444488632 scopus 로고    scopus 로고
    • Distinct modes of collagen type I proteolysis by matrix metalloproteinase (MMP) 2 and membrane type I MMP during the migration of a tip endothelial cell: Insights from a computational model
    • Karagiannis ED, Popel AS (2006) Distinct modes of collagen type I proteolysis by matrix metalloproteinase (MMP) 2 and membrane type I MMP during the migration of a tip endothelial cell: insights from a computational model. J Theor Biol 238: 124-145.
    • (2006) J Theor Biol , vol.238 , pp. 124-145
    • Karagiannis, E.D.1    Popel, A.S.2
  • 51
    • 0030954151 scopus 로고    scopus 로고
    • Localization and activation of type IV collagenase/gelatinase at endothelial focal contacts
    • Partridge CA, Phillips PG, Niedbala MJ, Jeffrey JJ (1997) Localization and activation of type IV collagenase/gelatinase at endothelial focal contacts. Am J Physiol 272: L813-822.
    • (1997) Am J Physiol , vol.272
    • Partridge, C.A.1    Phillips, P.G.2    Niedbala, M.J.3    Jeffrey, J.J.4
  • 52
    • 2342430205 scopus 로고    scopus 로고
    • Secreted MMP9 promotes angiogenesis more efficiently than constitutive active MMP9 bound to the tumor cell surface
    • Mira E, Lacalle RA, Buesa JM, de Buitrago GG, Jimenez-Baranda S, et al. (2004)Secreted MMP9 promotes angiogenesis more efficiently than constitutive active MMP9 bound to the tumor cell surface. J Cell Sci 117: 1847-1857.
    • (2004) J Cell Sci , vol.117 , pp. 1847-1857
    • Mira, E.1    Lacalle, R.A.2    Buesa, J.M.3    de Buitrago, G.G.4    Jimenez-Baranda, S.5
  • 53
    • 55949094110 scopus 로고    scopus 로고
    • A hybrid model for three-dimensional simulations of sprouting angiogenesis
    • Milde F, Bergdorf M, Koumoutsakos P (2008) A hybrid model for three-dimensional simulations of sprouting angiogenesis. Biophys J 95: 3146-3160.
    • (2008) Biophys J , vol.95 , pp. 3146-3160
    • Milde, F.1    Bergdorf, M.2    Koumoutsakos, P.3
  • 54
    • 0033582420 scopus 로고    scopus 로고
    • Heparan sulfate mediates bFGF transport through basement membrane by diffusion with rapid reversible binding
    • Dowd CJ, Cooney CL, Nugent MA (1999) Heparan sulfate mediates bFGF transport through basement membrane by diffusion with rapid reversible binding. J Biol Chem 274: 5236-5244.
    • (1999) J Biol Chem , vol.274 , pp. 5236-5244
    • Dowd, C.J.1    Cooney, C.L.2    Nugent, M.A.3
  • 55
    • 0034805462 scopus 로고    scopus 로고
    • Spatialrange of autocrine signaling: Modeling and computational analysis
    • Shvartsman SY, Wiley HS, Deen WM, Lauffenburger DA (2001) Spatialrange of autocrine signaling: modeling and computational analysis. Biophys J 81: 1854-1867.
    • (2001) Biophys J , vol.81 , pp. 1854-1867
    • Shvartsman, S.Y.1    Wiley, H.S.2    Deen, W.M.3    Lauffenburger, D.A.4
  • 56
    • 74049154719 scopus 로고    scopus 로고
    • Spatial restriction of FGF signaling by a matrix metalloprotease controls branching morphogenesis
    • Wang Q, Uhlirova M, Bohmann D (2010) Spatial restriction of FGF signaling by a matrix metalloprotease controls branching morphogenesis. Dev Cell 18: 157-164.
    • (2010) Dev Cell , vol.18 , pp. 157-164
    • Wang, Q.1    Uhlirova, M.2    Bohmann, D.3
  • 57
    • 44449123245 scopus 로고    scopus 로고
    • Spatial distribution of VEGF isoforms and chemotactic signals in the vicinity of a tumor
    • Small AR, Neagu A, Amyot F, Sackett D, Chernomordik V, et al. (2008) Spatial distribution of VEGF isoforms and chemotactic signals in the vicinity of a tumor. J Theor Biol 252: 593-607.
    • (2008) J Theor Biol , vol.252 , pp. 593-607
    • Small, A.R.1    Neagu, A.2    Amyot, F.3    Sackett, D.4    Chernomordik, V.5
  • 58
    • 4644236059 scopus 로고    scopus 로고
    • A theoretical model of type I collagen proteolysis by matrix metalloproteinase (MMP) 2 and membrane type 1 MMP in the presence of tissue inhibitor of metalloproteinase 2
    • Karagiannis ED, Popel AS (2004) A theoretical model of type I collagen proteolysis by matrix metalloproteinase (MMP) 2 and membrane type 1 MMP in the presence of tissue inhibitor of metalloproteinase 2. J Biol Chem 279: 39105-39114.
    • (2004) J Biol Chem , vol.279 , pp. 39105-39114
    • Karagiannis, E.D.1    Popel, A.S.2
  • 59
    • 38049136866 scopus 로고    scopus 로고
    • A biochemical model of matrix metalloproteinase 9 activation and inhibition
    • Vempati P, Karagiannis ED, Popel AS (2007) A biochemical model of matrix metalloproteinase 9 activation and inhibition. J Biol Chem 282: 37585-37596.
    • (2007) J Biol Chem , vol.282 , pp. 37585-37596
    • Vempati, P.1    Karagiannis, E.D.2    Popel, A.S.3
  • 60
    • 34249680152 scopus 로고    scopus 로고
    • Multi-scale computational models of pro-angiogenic treatments in peripheral arterial disease
    • MacGabhann F, JiJW, Popel AS (2007) Multi-scale computational models of pro-angiogenic treatments in peripheral arterial disease. Ann Biomed Eng 35: 982-994.
    • (2007) Ann Biomed Eng , vol.35 , pp. 982-994
    • Macgabhann, F.1    Ji, J.W.2    Popel, A.S.3
  • 61
    • 33846327237 scopus 로고    scopus 로고
    • Interactions of VEGF isoforms with VEGFR-1, VEGFR-2, and neuropilin in vivo: A computational model of human skeletal muscle
    • MacGabhann F, Popel AS (2007) Interactions of VEGF isoforms with VEGFR-1, VEGFR-2, and neuropilin in vivo: a computational model of human skeletal muscle. Am J Physiol Heart Circ Physiol 292: H459-H474.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Macgabhann, F.1    Popel, A.S.2
  • 62
    • 53549094683 scopus 로고    scopus 로고
    • A compartment model of VEGF distribution in blood, healthy and diseased tissues
    • Stefanini MO, Wu FT, MacGabhann F, Popel AS (2008) A compartment model of VEGF distribution in blood, healthy and diseased tissues. BMC Syst Biol 2: 77.
    • (2008) BMC Syst Biol , vol.2 , pp. 77
    • Stefanini, M.O.1    Wu, F.T.2    Macgabhann, F.3    Popel, A.S.4
  • 63
    • 74549170440 scopus 로고    scopus 로고
    • The presence of VEGF receptors on the luminal surface of endothelial cells affects VEGF distribution and VEGF signaling
    • Stefanini MO, Wu FT, MacGabhann F, Popel AS (2009) The presence of VEGF receptors on the luminal surface of endothelial cells affects VEGF distribution and VEGF signaling. PLoS Comput Biol 5: e1000622.
    • (2009) PLoS Comput Biol , vol.5
    • Stefanini, M.O.1    Wu, F.T.2    Macgabhann, F.3    Popel, A.S.4
  • 64
    • 57149102486 scopus 로고    scopus 로고
    • Systems biology of vascular endothelial growth factors
    • MacGabhann F, Popel AS (2008) Systems biology of vascular endothelial growth factors. Microcirculation 15: 715-738.
    • (2008) Microcirculation , vol.15 , pp. 715-738
    • Macgabhann, F.1    Popel, A.S.2
  • 65
    • 67649482465 scopus 로고    scopus 로고
    • Computational kinetic model of VEGF trapping by soluble VEGF receptor-1: Effects of transendothelial and lymphatic macromolecular transport
    • Wu FT, Stefanini MO, MacGabhann F, Kontos CD, Annex BH, et al. (2009) Computational kinetic model of VEGF trapping by soluble VEGF receptor-1: effects of transendothelial and lymphatic macromolecular transport. Physiol Genomics 38: 29-41.
    • (2009) Physiol Genomics , vol.38 , pp. 29-41
    • Wu, F.T.1    Stefanini, M.O.2    Macgabhann, F.3    Kontos, C.D.4    Annex, B.H.5
  • 66
    • 77952593669 scopus 로고    scopus 로고
    • A systems biology perspective on sVEGFR1: Its biological function, pathogenic role and therapeutic use
    • Wu FT, Stefanini MO, MacGabhann F, Kontos CD, Annex BH, et al. (2010) A systems biology perspective on sVEGFR1: its biological function, pathogenic role and therapeutic use. J Cell Mol Med 14: 528-552.
    • (2010) J Cell Mol Med , vol.14 , pp. 528-552
    • Wu, F.T.1    Stefanini, M.O.2    Macgabhann, F.3    Kontos, C.D.4    Annex, B.H.5
  • 67
    • 65249100178 scopus 로고    scopus 로고
    • A compartment model of VEGF distribution in humans in the presence of soluble VEGF receptor-1 acting as a ligand trap
    • Wu FT, Stefanini MO, MacGabhann F, Popel AS (2009) A compartment model of VEGF distribution in humans in the presence of soluble VEGF receptor-1 acting as a ligand trap. PLoS One 4: e5108.
    • (2009) PLoS One , vol.e5108 , pp. 4
    • Wu, F.T.1    Stefanini, M.O.2    Macgabhann, F.3    Popel, A.S.4
  • 68
    • 36849032983 scopus 로고    scopus 로고
    • Skeletal muscle VEGF gradients in peripheral arterial disease: Simulations of rest and exercise
    • Ji JW, MacGabhann F, Popel AS (2007) Skeletal muscle VEGF gradients in peripheral arterial disease: simulations of rest and exercise. Am J Physiol Heart Circ Physiol 293: H3740-3749.
    • (2007) Am J Physiol Heart Circ Physiol , vol.293
    • Ji, J.W.1    Macgabhann, F.2    Popel, A.S.3
  • 69
    • 0142151097 scopus 로고    scopus 로고
    • Abnormalities of basement membrane on blood vessels and endothelial sprouts in tumors
    • Baluk P, Morikawa S, Haskell A, Mancuso M, McDonald DM (2003) Abnormalities of basement membrane on blood vessels and endothelial sprouts in tumors. Am J Pathol 163: 1801-1815.
    • (2003) Am J Pathol , vol.163 , pp. 1801-1815
    • Baluk, P.1    Morikawa, S.2    Haskell, A.3    Mancuso, M.4    McDonald, D.M.5
  • 70
    • 43249122406 scopus 로고    scopus 로고
    • Laminin deposition is dispensable for vasculogenesis but regulates blood vessel diameter independent offlow
    • Jakobsson L, Domogatskaya A, Tryggvason K, Edgar D, Claesson-Welsh L (2008) Laminin deposition is dispensable for vasculogenesis but regulates blood vessel diameter independent offlow. FASEB J22: 1530-1539.
    • (2008) FASEB , vol.J22 , pp. 1530-1539
    • Jakobsson, L.1    Domogatskaya, A.2    Tryggvason, K.3    Edgar, D.4    Claesson-Welsh, L.5
  • 71
    • 0035544745 scopus 로고    scopus 로고
    • Available space and extracellular transport of macromolecules: Effects of pore size and connectedness
    • Yuan F, Krol A, Tong S (2001) Available space and extracellular transport of macromolecules: effects of pore size and connectedness. Ann Biomed Eng 29: 1150-1158.
    • (2001) Ann Biomed Eng , vol.29 , pp. 1150-1158
    • Yuan, F.1    Krol, A.2    Tong, S.3
  • 72
    • 0027315777 scopus 로고
    • Effect of cell arrangement and interstitial volume fraction on the diffusivity of monoclonal antibodies in tissue
    • el-Kareh AW, Braunstein SL, Secomb TW (1993) Effect of cell arrangement and interstitial volume fraction on the diffusivity of monoclonal antibodies in tissue. Biophys J64: 1638-1646.
    • (1993) Biophys , vol.J64 , pp. 1638-1646
    • El-Kareh, A.W.1    Braunstein, S.L.2    Secomb, T.W.3
  • 73
    • 34948896998 scopus 로고    scopus 로고
    • Where is VEGF in the body? A meta-analysis of VEGF distribution in cancer
    • Kut C, MacGabhann F, Popel AS (2007) Where is VEGF in the body? A meta-analysis of VEGF distribution in cancer. Br J Cancer 97: 978-985.
    • (2007) Br J Cancer , vol.97 , pp. 978-985
    • Kut, C.1    Macgabhann, F.2    Popel, A.S.3
  • 74
    • 0142091644 scopus 로고    scopus 로고
    • Comparison of the thickness ofbasement membranes in various tissues ofthe rat
    • Osawa T, Onodera M, Feng XY, Nozaka Y (2003) Comparison of the thickness ofbasement membranes in various tissues ofthe rat. J Electron Microsc (Tokyo) 52: 435-440.
    • (2003) J Electron Microsc (Tokyo) , vol.52 , pp. 435-440
    • Osawa, T.1    Onodera, M.2    Feng, X.Y.3    Nozaka, Y.4
  • 76
    • 28444449872 scopus 로고    scopus 로고
    • Effects of receptor clustering on ligand dissociation kinetics: Theory and simulations
    • Gopalakrishnan M, Forsten-Williams K, Nugent MA, Tauber UC (2005) Effects of receptor clustering on ligand dissociation kinetics: theory and simulations. Biophys J 89: 3686-3700.
    • (2005) Biophys J , vol.89 , pp. 3686-3700
    • Gopalakrishnan, M.1    Forsten-Williams, K.2    Nugent, M.A.3    Tauber, U.C.4
  • 78
    • 0023433628 scopus 로고
    • Flow through interstitium and other fibrous matrices
    • Levick JR (1987) Flow through interstitium and other fibrous matrices. Q J Exp Physiol 72: 409-437.
    • (1987) Q J Exp Physiol , vol.72 , pp. 409-437
    • Levick, J.R.1
  • 79
    • 0345737075 scopus 로고    scopus 로고
    • Model of competitive binding of vascular endothelial growth factor and placental growth factor to VEGF receptors on endothelial cells
    • MacGabhann F, Popel AS (2004) Model of competitive binding of vascular endothelial growth factor and placental growth factor to VEGF receptors on endothelial cells. Am J Physiol Heart Circ Physiol 286: H153-164.
    • (2004) Am J Physiol Heart Circ Physiol , vol.286
    • Macgabhann, F.1    Popel, A.S.2
  • 80
    • 19344372080 scopus 로고    scopus 로고
    • Differential binding of VEGF isoforms to VEGF receptor 2 in the presence of neuropilin-1: A computational model
    • MacGabhann F, Popel AS (2005) Differential binding of VEGF isoforms to VEGF receptor 2 in the presence of neuropilin-1: a computational model. Am J Physiol Heart Circ Physiol 288: H2851-2860.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Macgabhann, F.1    Popel, A.S.2
  • 81
    • 33645284986 scopus 로고    scopus 로고
    • Possible pathophysiological role ofvascular endothelial growth factor (VEGF) and matrix metalloproteinases (MMPs) in metastatic brain tumor-associated intracerebral hemorrhage
    • Jung S, Moon KS, Jung TY, Kim IY, Lee YH, et al. (2006) Possible pathophysiological role ofvascular endothelial growth factor (VEGF) and matrix metalloproteinases (MMPs) in metastatic brain tumor-associated intracerebral hemorrhage. J Neurooncol 76: 257-263.
    • (2006) J Neurooncol , vol.76 , pp. 257-263
    • Jung, S.1    Moon, K.S.2    Jung, T.Y.3    Kim, I.Y.4    Lee, Y.H.5
  • 82
    • 0035957277 scopus 로고    scopus 로고
    • Circulating levels of MMP-1, -2, -3, -9, and TIMP-1 are increased in POEMS syndrome
    • Michizono K, Umehara F, Hashiguchi T, Arimura K, Matsuura E, et al. (2001) Circulating levels of MMP-1, -2, -3, -9, and TIMP-1 are increased in POEMS syndrome. Neurology 56: 807-810.
    • (2001) Neurology , vol.56 , pp. 807-810
    • Michizono, K.1    Umehara, F.2    Hashiguchi, T.3    Arimura, K.4    Matsuura, E.5
  • 83
    • 0033532205 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion
    • Ramos-DeSimone N, Hahn-Dantona E, Sipley J, Nagase H, French DL, et al. (1999) Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem 274: 13066-13076.
    • (1999) J Biol Chem , vol.274 , pp. 13066-13076
    • Ramos-Desimone, N.1    Hahn-Dantona, E.2    Sipley, J.3    Nagase, H.4    French, D.L.5
  • 84
    • 0023035995 scopus 로고
    • Secretion of metalloprotei-nases by stimulated capillary endothelial cells. I. Production of procollagenase and prostromelysin exceeds expression of proteolytic activity
    • Herron GS, Werb Z, Dwyer K, Banda MJ (1986) Secretion of metalloprotei-nases by stimulated capillary endothelial cells. I. Production of procollagenase and prostromelysin exceeds expression of proteolytic activity. J Biol Chem 261: 2810-2813.
    • (1986) J Biol Chem , vol.261 , pp. 2810-2813
    • Herron, G.S.1    Werb, Z.2    Dwyer, K.3    Banda, M.J.4
  • 85
    • 0034672120 scopus 로고    scopus 로고
    • Type IV collagen induces matrix metalloproteinase 2 activation in HT1080 fibrosarcoma cells
    • Maquoi E, Frankenne F, Noel A, Krell HW, Grams F, et al. (2000) Type IV collagen induces matrix metalloproteinase 2 activation in HT1080 fibrosarcoma cells. Exp Cell Res 261: 348-359.
    • (2000) Exp Cell Res , vol.261 , pp. 348-359
    • Maquoi, E.1    Frankenne, F.2    Noel, A.3    Krell, H.W.4    Grams, F.5
  • 86
    • 0021278562 scopus 로고
    • Collagenase is a major gene product of induced rabbit synovial fibroblasts
    • Aggeler J, Frisch SM, Werb Z (1984) Collagenase is a major gene product of induced rabbit synovial fibroblasts. J Cell Biol 98: 1656-1661.
    • (1984) J Cell Biol , vol.98 , pp. 1656-1661
    • Aggeler, J.1    Frisch, S.M.2    Werb, Z.3
  • 87
    • 0020365610 scopus 로고
    • Plasminogen activator and collagenase production by cultured capillary endothelial cells
    • Gross JL, Moscatelli D, Jaffe EA, Rifkin DB (1982) Plasminogen activator and collagenase production by cultured capillary endothelial cells. J Cell Biol 95: 974-981.
    • (1982) J Cell Biol , vol.95 , pp. 974-981
    • Gross, J.L.1    Moscatelli, D.2    Jaffe, E.A.3    Rifkin, D.B.4
  • 88
    • 0032838247 scopus 로고    scopus 로고
    • Heparin and fragments modulate the expression of collagen-degrading enzymes (matrix metalloproteinases 1 and 2) by human gingival fibroblasts
    • Hornebeck W, Gogly B, Godeau G, Emonard H, Pellat B (1999) Heparin and fragments modulate the expression of collagen-degrading enzymes (matrix metalloproteinases 1 and 2) by human gingival fibroblasts. Ann N Y Acad Sci 878: 625-628.
    • (1999) Ann N Y Acad Sci , vol.878 , pp. 625-628
    • Hornebeck, W.1    Gogly, B.2    Godeau, G.3    Emonard, H.4    Pellat, B.5
  • 89
    • 0031057650 scopus 로고    scopus 로고
    • Fibronectin-fragment-induced cartilage chondrolysis is associated with release of catabolic cytokines
    • Homandberg GA, Hui F, Wen C, Purple C, Bewsey K, et al. (1997) Fibronectin-fragment-induced cartilage chondrolysis is associated with release of catabolic cytokines. Biochem J 321(Pt 3): 751-757.
    • (1997) Biochem J , vol.321 , Issue.Pt 3 , pp. 751-757
    • Homandberg, G.A.1    Hui, F.2    Wen, C.3    Purple, C.4    Bewsey, K.5
  • 90
    • 0030614869 scopus 로고    scopus 로고
    • VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix
    • Poltorak Z, Cohen T, Sivan R, Kandelis Y, Spira G, et al. (1997) VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix. J Biol Chem 272: 7151-7158.
    • (1997) J Biol Chem , vol.272 , pp. 7151-7158
    • Poltorak, Z.1    Cohen, T.2    Sivan, R.3    Kandelis, Y.4    Spira, G.5
  • 91
    • 0023687871 scopus 로고
    • Endothelial cell-derived heparan sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation
    • Saksela O, Moscatelli D, Sommer A, Rifkin DB (1988) Endothelial cell-derived heparan sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation. J Cell Biol 107: 743-751.
    • (1988) J Cell Biol , vol.107 , pp. 743-751
    • Saksela, O.1    Moscatelli, D.2    Sommer, A.3    Rifkin, D.B.4
  • 92
    • 38749149555 scopus 로고    scopus 로고
    • Overexpression of vascular endothelial growth factor 189 in breast cancer cells leads to delayed tumor uptake with dilated intratumoral vessels
    • Herve MA, Buteau-Lozano H, Vassy R, Bieche I, Velasco G, et al. (2008) Overexpression of vascular endothelial growth factor 189 in breast cancer cells leads to delayed tumor uptake with dilated intratumoral vessels. Am J Pathol 172: 167-178.
    • (2008) Am J Pathol , vol.172 , pp. 167-178
    • Herve, M.A.1    Buteau-Lozano, H.2    Vassy, R.3    Bieche, I.4    Velasco, G.5
  • 93
    • 0030047580 scopus 로고    scopus 로고
    • Hindered diffusion in agarose gels: Test ofeffective medium model
    • Johnson EM, Berk DA, Jain RK, Deen WM (1996) Hindered diffusion in agarose gels: test ofeffective medium model. Biophys J70: 1017-1023.
    • (1996) Biophys , vol.J70 , pp. 1017-1023
    • Johnson, E.M.1    Berk, D.A.2    Jain, R.K.3    Deen, W.M.4
  • 94
    • 1042291194 scopus 로고    scopus 로고
    • Macrophage matrix metalloproteinase-9 regulates angio-genesis in ischemic muscle
    • Bendeck MP (2004) Macrophage matrix metalloproteinase-9 regulates angio-genesis in ischemic muscle. Circ Res 94: 138-139.
    • (2004) Circ Res , vol.94 , pp. 138-139
    • Bendeck, M.P.1
  • 95
    • 0027444528 scopus 로고
    • Degradation of entactin by matrix metalloproteinases. Susceptibility to matrilysin and identification of cleavage sites
    • Sires UI, Griffin GL, Broekelmann TJ, Mecham RP, Murphy G, et al. (1993) Degradation of entactin by matrix metalloproteinases. Susceptibility to matrilysin and identification of cleavage sites. J Biol Chem 268: 2069-2074.
    • (1993) J Biol Chem , vol.268 , pp. 2069-2074
    • Sires, U.I.1    Griffin, G.L.2    Broekelmann, T.J.3    Mecham, R.P.4    Murphy, G.5
  • 96
    • 29544452734 scopus 로고    scopus 로고
    • Skeletal muscle ultrastructural and plasma biochemical signs of endothelium dysfunction induced by a high-altitude expedition (Pumori, 7161 m)
    • Magalhaes J, Ascensao A, Marques F, Soares J, Neuparth M, et al. (2005) Skeletal muscle ultrastructural and plasma biochemical signs of endothelium dysfunction induced by a high-altitude expedition (Pumori, 7161 m). Basic Appl Myol 15: 29-35.
    • (2005) Basic Appl Myol , vol.15 , pp. 29-35
    • Magalhaes, J.1    Ascensao, A.2    Marques, F.3    Soares, J.4    Neuparth, M.5
  • 97
    • 11144252286 scopus 로고    scopus 로고
    • Intracoronary administration of FGF-2: A computational model of myocardial deposition and retention
    • Filion RJ, Popel AS (2005) Intracoronary administration of FGF-2: a computational model of myocardial deposition and retention. Am J Physiol Heart Circ Physiol 288: H263-279.
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Filion, R.J.1    Popel, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.