메뉴 건너뛰기




Volumn 15, Issue 12, 2009, Pages 1385-1400

The extracellular matrix of blood vessels

Author keywords

Angiogenesis; Blood vessel; Endothelial cells; Extracellular matrix; Vascular smooth muscle cells

Indexed keywords

ANGIOPOIETIN; BASIC FIBROBLAST GROWTH FACTOR; COLLAGEN TYPE 4; ELASTIN; FIBRILLIN 1; FIBULIN 5; LAMININ; MATRIX METALLOPROTEINASE; PERLECAN; PLATELET DERIVED GROWTH FACTOR; PROTEIN LYSINE 6 OXIDASE; SYNDECAN; THROMBOSPONDIN; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; VASCULOTROPIN; VON WILLEBRAND FACTOR;

EID: 65649147889     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161209787846757     Document Type: Review
Times cited : (137)

References (201)
  • 2
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: Structure, assembly and role in tumor angiogenesis
    • Kalluri R. Basement membranes: structure, assembly and role in tumor angiogenesis. Nat Rev Cancer 2003; 3: 422-33.
    • (2003) Nat Rev Cancer , vol.3 , pp. 422-433
    • Kalluri, R.1
  • 3
    • 34848889281 scopus 로고    scopus 로고
    • Structure and function of basement membranes
    • LeBleu VS, MacDonald B, Kalluri R. Structure and function of basement membranes. Exp Biol Med 2007; 232: 1121-9.
    • (2007) Exp Biol Med , vol.232 , pp. 1121-1129
    • LeBleu, V.S.1    MacDonald, B.2    Kalluri, R.3
  • 4
    • 23144436642 scopus 로고    scopus 로고
    • Basement membrane proteoglycans: From cellar to ceiling
    • Iozzo RV. Basement membrane proteoglycans: from cellar to ceiling. Nat Rev Mol Cell Biol 2005; 6: 646-56.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 646-656
    • Iozzo, R.V.1
  • 5
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases, and potentials for therapy
    • Prockop DJ, Kivirikko KI. Collagens: molecular biology, diseases, and potentials for therapy. Annu Rev Biochem 1995; 64: 403-34.
    • (1995) Annu Rev Biochem , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 6
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J, Kivirikko K. Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends in Genetics 2004; 20: 33-43.
    • (2004) Trends in Genetics , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.2
  • 8
    • 1442333284 scopus 로고    scopus 로고
    • Atherosclerosis and extracellular matrix
    • Katsuda S, Kaji T. Atherosclerosis and extracellular matrix. J Atheroscler Throm 2003; 10: 267-74.
    • (2003) J Atheroscler Throm , vol.10 , pp. 267-274
    • Katsuda, S.1    Kaji, T.2
  • 9
    • 0037212317 scopus 로고    scopus 로고
    • Vascular collagens: Spotlight on the role of type VIII collagen in atherogenesis
    • Plenz GA, Deng MC, Robenek K, Völker W. Vascular collagens: spotlight on the role of type VIII collagen in atherogenesis. Atherosclerosis 2003; 166: 1-11.
    • (2003) Atherosclerosis , vol.166 , pp. 1-11
    • Plenz, G.A.1    Deng, M.C.2    Robenek, K.3    Völker, W.4
  • 10
    • 0028639246 scopus 로고
    • Basement membrane (type IV) collagen
    • Kühn K. Basement membrane (type IV) collagen. Matrix Biol 1994; 14: 439-45.
    • (1994) Matrix Biol , vol.14 , pp. 439-445
    • Kühn, K.1
  • 12
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensible for initiation of its assembly during early development
    • Pöschl E, Schlötzer-Schrehardt U, Brachvogel B, Saito K, Ninmiya Y, Mayer U. Collagen IV is essential for basement membrane stability but dispensible for initiation of its assembly during early development. Development 2003; 131: 1619-28.
    • (2003) Development , vol.131 , pp. 1619-1628
    • Pöschl, E.1    Schlötzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninmiya, Y.5    Mayer, U.6
  • 13
    • 18144404148 scopus 로고    scopus 로고
    • Physiological role of collagen XVIII and endostatin
    • Marneros AG, Olson BR. Physiological role of collagen XVIII and endostatin. FASEB J 2005; 19: 716-28.
    • (2005) FASEB J , vol.19 , pp. 716-728
    • Marneros, A.G.1    Olson, B.R.2
  • 14
    • 0032962217 scopus 로고    scopus 로고
    • Mutation analysis and molecular genetics of epidermolysis bullosa
    • Pulkkinen L, Uitto J. Mutation analysis and molecular genetics of epidermolysis bullosa. Matrix Biol 1999; 18: 29-42.
    • (1999) Matrix Biol , vol.18 , pp. 29-42
    • Pulkkinen, L.1    Uitto, J.2
  • 15
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, et al. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol 1999; 144: 151-60.
    • (1999) J Cell Biol , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6
  • 16
    • 0031661502 scopus 로고    scopus 로고
    • The role of laminins in basement membrane function
    • Aumailley M, Smyth N. The role of laminins in basement membrane function. J Anat 1998; 193: 1-21.
    • (1998) J Anat , vol.193 , pp. 1-21
    • Aumailley, M.1    Smyth, N.2
  • 17
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato H, Yurchenco PD. Form and function: the laminin family of heterotrimers. Dev Dyn 2000; 218: 213-34.
    • (2000) Dev Dyn , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 19
    • 0034333146 scopus 로고    scopus 로고
    • Integrins as receptors for laminins
    • Belkin AM, Stepp MA. Integrins as receptors for laminins. Microsc Res techn 2000; 51: 280-301.
    • (2000) Microsc Res techn , vol.51 , pp. 280-301
    • Belkin, A.M.1    Stepp, M.A.2
  • 20
    • 0033612299 scopus 로고    scopus 로고
    • Dystroglycan versatility
    • Hemler ME. Dystroglycan versatility. Cell 1999; 97: 543-6.
    • (1999) Cell , vol.97 , pp. 543-546
    • Hemler, M.E.1
  • 21
    • 21244438355 scopus 로고    scopus 로고
    • Expression and functions of laminins in the embryonic and mature vasculature
    • Hallmann R, Horn N, Selg M, Wendler O, Pausch F, Sorokin LM. Expression and functions of laminins in the embryonic and mature vasculature. Physiol Rev 2005; 85: 979-1000.
    • (2005) Physiol Rev , vol.85 , pp. 979-1000
    • Hallmann, R.1    Horn, N.2    Selg, M.3    Wendler, O.4    Pausch, F.5    Sorokin, L.M.6
  • 22
    • 4344655934 scopus 로고    scopus 로고
    • Beauvais DM, Rapraeger AC. Syndecans in tumor cell adhesion and signaling. Reprod Biol Endocrinol 2004; 2:
    • Beauvais DM, Rapraeger AC. Syndecans in tumor cell adhesion and signaling. Reprod Biol Endocrinol 2004; 2:
  • 23
  • 24
    • 0027263329 scopus 로고
    • Nidogen mediates the formation of ternary complexes of basement membrane components
    • Aumailley M, Battaglia C, Mayer U, Nischt R, Timpl R, Fox J. Nidogen mediates the formation of ternary complexes of basement membrane components. Kidney Int 1993; 43: 7-12.
    • (1993) Kidney Int , vol.43 , pp. 7-12
    • Aumailley, M.1    Battaglia, C.2    Mayer, U.3    Nischt, R.4    Timpl, R.5    Fox, J.6
  • 26
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: A new basement membrane protein with diverse binding properties
    • Kohfeldt E, Sasaki T, Gohring W, Timpl R. Nidogen-2: a new basement membrane protein with diverse binding properties. J Mol Biol 1998; 282: 99-109.
    • (1998) J Mol Biol , vol.282 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Gohring, W.3    Timpl, R.4
  • 27
    • 0036405396 scopus 로고    scopus 로고
    • Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens
    • Salmavirta K, Talts JS, Olsson M, Sasaki T, Timpl R, Ekblom P. Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens. Exp Cell Res 2002; 279: 188-201.
    • (2002) Exp Cell Res , vol.279 , pp. 188-201
    • Salmavirta, K.1    Talts, J.S.2    Olsson, M.3    Sasaki, T.4    Timpl, R.5    Ekblom, P.6
  • 28
    • 22544456862 scopus 로고    scopus 로고
    • Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice
    • Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkopati S, et al. Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol Cell Biol 2005; 25: 6846-56.
    • (2005) Mol Cell Biol , vol.25 , pp. 6846-6856
    • Bader, B.L.1    Smyth, N.2    Nedbal, S.3    Miosge, N.4    Baranowsky, A.5    Mokkopati, S.6
  • 29
    • 42949109152 scopus 로고    scopus 로고
    • Novel interactions of perlecan: Unraveling perlecan's role in angiogenesis
    • Bix G, Iozzo RV. Novel interactions of perlecan: unraveling perlecan's role in angiogenesis. Microsc Res Tech 2008; 71: 339-48.
    • (2008) Microsc Res Tech , vol.71 , pp. 339-348
    • Bix, G.1    Iozzo, R.V.2
  • 30
    • 34548749193 scopus 로고    scopus 로고
    • Perlecan - a multifunctional extracellular proteoglycan scaffold
    • Farach-Carson MC, Carson DD. Perlecan - a multifunctional extracellular proteoglycan scaffold. Glycobiol 2007; 17: 897-905.
    • (2007) Glycobiol , vol.17 , pp. 897-905
    • Farach-Carson, M.C.1    Carson, D.D.2
  • 31
    • 33750886289 scopus 로고    scopus 로고
    • Perlecan: How does one molcule do so many things ?
    • Knox SM, Whitelock JM. Perlecan: how does one molcule do so many things ? Cell Mol Life Sci 2006; 63: 2435-45.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2435-2445
    • Knox, S.M.1    Whitelock, J.M.2
  • 32
    • 4043063680 scopus 로고    scopus 로고
    • The role of perlecan in arterial injury and angiogenesis
    • Segev A, Nili N, Strauss BH. The role of perlecan in arterial injury and angiogenesis. Cardivasc Res 2004; 63: 603-10.
    • (2004) Cardivasc Res , vol.63 , pp. 603-610
    • Segev, A.1    Nili, N.2    Strauss, B.H.3
  • 33
    • 3142682314 scopus 로고    scopus 로고
    • Impaired angiogenesis, delayed wound healing and retarded tumor growth in perlecan heparan sulfate-deficient mice
    • Zhou Z, Wang J, Cao R, Morita H, Soininen R, Chan KM, et al. Impaired angiogenesis, delayed wound healing and retarded tumor growth in perlecan heparan sulfate-deficient mice. Cancer Res 2004; 64: 4699-702.
    • (2004) Cancer Res , vol.64 , pp. 4699-4702
    • Zhou, Z.1    Wang, J.2    Cao, R.3    Morita, H.4    Soininen, R.5    Chan, K.M.6
  • 34
    • 38349140682 scopus 로고    scopus 로고
    • Integrin α2β1 is the required receptor for endorepellin angiostatic activity
    • Woodall BP, Nyström A, Iozzo RA, Eble JA, Niland S, Krieg T, et al. Integrin α2β1 is the required receptor for endorepellin angiostatic activity. J Biol Chem 2008; 283: 2335-43.
    • (2008) J Biol Chem , vol.283 , pp. 2335-2343
    • Woodall, B.P.1    Nyström, A.2    Iozzo, R.A.3    Eble, J.A.4    Niland, S.5    Krieg, T.6
  • 36
    • 0034715896 scopus 로고    scopus 로고
    • Insights into extracellular matrix functions from mutant mouse models
    • Gustafsson E, Fassler R. Insights into extracellular matrix functions from mutant mouse models. Exp Cell Res 2000; 261: 52-68.
    • (2000) Exp Cell Res , vol.261 , pp. 52-68
    • Gustafsson, E.1    Fassler, R.2
  • 37
    • 0036160658 scopus 로고    scopus 로고
    • Dyssegmental dysplasia, Silverman-Handmaker type: Unexpected role of perlecan in cartilage development
    • Arilawa-Hirasawa E-, Wilcox WR, Yamada Y. Dyssegmental dysplasia, Silverman-Handmaker type: unexpected role of perlecan in cartilage development. Am J Med Genet 2001; 106: 254-7.
    • (2001) Am J Med Genet , vol.106 , pp. 254-257
    • Arilawa-Hirasawa, E.1    Wilcox, W.R.2    Yamada, Y.3
  • 39
    • 0035022957 scopus 로고    scopus 로고
    • SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury
    • Bradshaw AD, Sage EH. SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury. J Clin Invest 2001; 107: 1049-54.
    • (2001) J Clin Invest , vol.107 , pp. 1049-1054
    • Bradshaw, A.D.1    Sage, E.H.2
  • 40
    • 33846895981 scopus 로고    scopus 로고
    • Role of SPARC - matricellular protein in pathophysiology and tissue injury healing. Implications for gastritis and gastric ulcers
    • Phan E, Ahluwalia A, Tamawaski AS. Role of SPARC - matricellular protein in pathophysiology and tissue injury healing. Implications for gastritis and gastric ulcers. Med Sci Monit 2007; 13: RA25-30.
    • (2007) Med Sci Monit , vol.13
    • Phan, E.1    Ahluwalia, A.2    Tamawaski, A.S.3
  • 41
    • 1942532093 scopus 로고    scopus 로고
    • Molecules in focus: The thrombospondins
    • Adams JC, Lawler J. Molecules in focus: The thrombospondins. Int J Biochem Cell Biol 2004; 36: 961-8.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 961-968
    • Adams, J.C.1    Lawler, J.2
  • 42
    • 34250022258 scopus 로고    scopus 로고
    • Osteopontin and cardiovascular system
    • Okamoto H. Osteopontin and cardiovascular system. Mol Cell Biochem 2007; 300: 1-7.
    • (2007) Mol Cell Biochem , vol.300 , pp. 1-7
    • Okamoto, H.1
  • 43
    • 33645579919 scopus 로고    scopus 로고
    • Plasma von Willebrand factor, thrombosis, and the endothelium: The first 30 years
    • Blann AD. Plasma von Willebrand factor, thrombosis, and the endothelium: the first 30 years. Thromb Haemost 2006; 95: 49-55.
    • (2006) Thromb Haemost , vol.95 , pp. 49-55
    • Blann, A.D.1
  • 44
    • 0141498240 scopus 로고    scopus 로고
    • Willebrand factor, platelets and endothelial cell interactions
    • Ruggeri ZM. Von Willebrand factor, platelets and endothelial cell interactions. J Thromb Haemost 2003; 1: 1335-42.
    • (2003) J Thromb Haemost , vol.1 , pp. 1335-1342
    • Von, R.Z.M.1
  • 45
    • 0025243601 scopus 로고
    • Cell biology of the von Willebrand factor
    • Wagner DD. Cell biology of the von Willebrand factor. Annu Rev Cell Biol 1990; 6: 217-46.
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 217-246
    • Wagner, D.D.1
  • 46
    • 0029858896 scopus 로고    scopus 로고
    • Shear-dependent changes in the three-dimensional structure of human von Willebrand factor
    • Siedlecki CA, Lestini BJ, Kottke-Marchant KK. Shear-dependent changes in the three-dimensional structure of human von Willebrand factor. Blood 1996; 88: 2939-50.
    • (1996) Blood , vol.88 , pp. 2939-2950
    • Siedlecki, C.A.1    Lestini, B.J.2    Kottke-Marchant, K.K.3
  • 48
    • 33746330507 scopus 로고    scopus 로고
    • Von Willebrand factor and thrombosis
    • Franchini M, Lippi G. Von Willebrand factor and thrombosis. Ann Haematol 2006; 85: 415-23.
    • (2006) Ann Haematol , vol.85 , pp. 415-423
    • Franchini, M.1    Lippi, G.2
  • 49
    • 33745683637 scopus 로고    scopus 로고
    • The molecular biology of thrombotic microangiopathy
    • Tsai H-M. The molecular biology of thrombotic microangiopathy. Kidney Intern 2006; 70: 16-23.
    • (2006) Kidney Intern , vol.70 , pp. 16-23
    • Tsai, H.-M.1
  • 50
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • Nieswandt B, Watson SP. Platelet-collagen interaction: is GPVI the central receptor? Blood 2003; 102: 449-61.
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 51
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002; 110: 673-87.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 53
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with Arg-Gly-Asp ligand
    • Xiong J-P, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman S, et al. Crystal structure of the extracellular segment of integrin αVβ3 in complex with Arg-Gly-Asp ligand. Science 2002; 296: 151-5.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.6
  • 55
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti F, Ruoslahti E. Integrin signaling. Science 1999; 285: 1028-32.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.1    Ruoslahti, E.2
  • 56
    • 39849104321 scopus 로고    scopus 로고
    • Endothelial adherens and tight junctions in vascular homeostasis, inflammation and angiogenesis
    • Wallez Y, Huber P. Endothelial adherens and tight junctions in vascular homeostasis, inflammation and angiogenesis. Biochem Biophys Acta 2008; 1778: 794-809.
    • (2008) Biochem Biophys Acta , vol.1778 , pp. 794-809
    • Wallez, Y.1    Huber, P.2
  • 57
    • 34547858139 scopus 로고    scopus 로고
    • Endothelial immunogenicity - a matter of matrix microarchitecture
    • Methe H, Hess S, Edelman ER. Endothelial immunogenicity - a matter of matrix microarchitecture. Thromb Haemost 2007; 98: 278-82.
    • (2007) Thromb Haemost , vol.98 , pp. 278-282
    • Methe, H.1    Hess, S.2    Edelman, E.R.3
  • 58
    • 0030989435 scopus 로고    scopus 로고
    • Inducible nitrice oxide and prostacyclin productions are differently controlled by extracellular matrix and cell density in human vascular endothelial cells
    • Orpana A, Ranta V, Mikkola T, Viinikka L, Ylikorkala O. Inducible nitrice oxide and prostacyclin productions are differently controlled by extracellular matrix and cell density in human vascular endothelial cells. J Cell Biochem 1997; 64: 538-46.
    • (1997) J Cell Biochem , vol.64 , pp. 538-546
    • Orpana, A.1    Ranta, V.2    Mikkola, T.3    Viinikka, L.4    Ylikorkala, O.5
  • 59
    • 33846246406 scopus 로고    scopus 로고
    • Alexopoulou AN, Multhaupt HA, Couchman JR. Syndecans in wound healing, inflammation and vascular biology. Int J Biochem Cell Biol 2007; 39: 505-28.
    • Alexopoulou AN, Multhaupt HA, Couchman JR. Syndecans in wound healing, inflammation and vascular biology. Int J Biochem Cell Biol 2007; 39: 505-28.
  • 61
    • 4744368711 scopus 로고    scopus 로고
    • Inhibition by the soluble syndecan-1 ectodomains delays wound repair in mice overexpressing syndecan-1
    • Elenius V, Gotte M, Reizes O, Elenius K, Bernfield M. Inhibition by the soluble syndecan-1 ectodomains delays wound repair in mice overexpressing syndecan-1. J Biol Chem 2004; 279: 41928-35.
    • (2004) J Biol Chem , vol.279 , pp. 41928-41935
    • Elenius, V.1    Gotte, M.2    Reizes, O.3    Elenius, K.4    Bernfield, M.5
  • 62
    • 1442356942 scopus 로고    scopus 로고
    • Syndecan-2 is essential for angiogenic sprouting during zebrafish development
    • Chen E, Hermanson S, Ekker SC. Syndecan-2 is essential for angiogenic sprouting during zebrafish development. Blood 2004; 103: 1710-9.
    • (2004) Blood , vol.103 , pp. 1710-1719
    • Chen, E.1    Hermanson, S.2    Ekker, S.C.3
  • 64
    • 34447300158 scopus 로고    scopus 로고
    • Adhesion and signaling molecules controlling the transmigration of leukocytes through endothelium
    • Vestweber D. Adhesion and signaling molecules controlling the transmigration of leukocytes through endothelium. Immunol Rev 2007; 218: 178-96.
    • (2007) Immunol Rev , vol.218 , pp. 178-196
    • Vestweber, D.1
  • 65
    • 33745029732 scopus 로고    scopus 로고
    • Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils
    • Wang S, Voisin M-B, Larbi KY, Dangerfield J, Scheiermann C, Tran M, et al. Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils. J Exp Med 2006; 6: 1519-32.
    • (2006) J Exp Med , vol.6 , pp. 1519-1532
    • Wang, S.1    Voisin, M.-B.2    Larbi, K.Y.3    Dangerfield, J.4    Scheiermann, C.5    Tran, M.6
  • 66
    • 0035947768 scopus 로고    scopus 로고
    • Endothelial cell laminin isoforms, laminin 8 and 10, play decisive roles in T cell recruitment across the blood-brain barrier in experimental autoimmune encephalomyelitis
    • Sixt M, Engelhardt B, Pausch F, Hallmann R, Wendler O, Sorokin LM. Endothelial cell laminin isoforms, laminin 8 and 10, play decisive roles in T cell recruitment across the blood-brain barrier in experimental autoimmune encephalomyelitis. J Cell Biol 2001; 153: 933-45.
    • (2001) J Cell Biol , vol.153 , pp. 933-945
    • Sixt, M.1    Engelhardt, B.2    Pausch, F.3    Hallmann, R.4    Wendler, O.5    Sorokin, L.M.6
  • 67
    • 44749086106 scopus 로고    scopus 로고
    • Blood vessels of human islets of Langerhans are surrounded by a double basement membrane
    • Virtanen I, Banerjee M, Palgi I, Korsgren O, Lukinius A, Thornell L-E, et al. Blood vessels of human islets of Langerhans are surrounded by a double basement membrane. Diabetologia 2008; 51: 1181-91.
    • (2008) Diabetologia , vol.51 , pp. 1181-1191
    • Virtanen, I.1    Banerjee, M.2    Palgi, I.3    Korsgren, O.4    Lukinius, A.5    Thornell, L.-E.6
  • 68
    • 0033519298 scopus 로고
    • Characterization and expression of the laminin γ3 chain: A novel, non-basement membrane-associated, laminin chain
    • Koch M, Olson PF, Albus A, Jin W, Hunter DD, Brunken WJ, et al. Characterization and expression of the laminin γ3 chain: a novel, non-basement membrane-associated, laminin chain. J Cell Biol 1991; 145: 605-17.
    • (1991) J Cell Biol , vol.145 , pp. 605-617
    • Koch, M.1    Olson, P.F.2    Albus, A.3    Jin, W.4    Hunter, D.D.5    Brunken, W.J.6
  • 69
    • 33747417084 scopus 로고    scopus 로고
    • Integrin-matrix interactions in the cerebral microvasculature
    • Del Zoppo GJ, Milner R. Integrin-matrix interactions in the cerebral microvasculature. Arterioscler Thromb Vasc Biol 2006; 26: 1966-75.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1966-1975
    • Del Zoppo, G.J.1    Milner, R.2
  • 70
    • 0242456170 scopus 로고    scopus 로고
    • Axis of evil: Molecular mechanisms of cancer metastasis
    • Bogenrieder T, Herlyn M. Axis of evil: molecular mechanisms of cancer metastasis. Oncogene 2003; 22: 6524-36.
    • (2003) Oncogene , vol.22 , pp. 6524-6536
    • Bogenrieder, T.1    Herlyn, M.2
  • 72
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood JD, Cheresh DA. Role of integrins in cell invasion and migration. Nat Rev Cancer 2002; 2: 91-100.
    • (2002) Nat Rev Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 74
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 2006; 69: 562-73.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 76
    • 19544367266 scopus 로고    scopus 로고
    • Snake venoms and coagulopathy
    • White J. Snake venoms and coagulopathy. Toxicon 2005; 45: 951-67.
    • (2005) Toxicon , vol.45 , pp. 951-967
    • White, J.1
  • 77
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage
    • Gutiérrez JM, Rucavado A, Escalante T, Díaz C. Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 2005; 45: 997-1011.
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutiérrez, J.M.1    Rucavado, A.2    Escalante, T.3    Díaz, C.4
  • 78
    • 19544386458 scopus 로고    scopus 로고
    • Snake venom probes of platelet adhesion receptors and their ligands
    • Wijeyewickrema L, Berndt MC, Andrews RK. Snake venom probes of platelet adhesion receptors and their ligands. Toxicon 2005; 45: 1051-61.
    • (2005) Toxicon , vol.45 , pp. 1051-1061
    • Wijeyewickrema, L.1    Berndt, M.C.2    Andrews, R.K.3
  • 81
    • 33746943302 scopus 로고    scopus 로고
    • Elastic fibres in health and disease
    • Kielty CM. Elastic fibres in health and disease. Expert Rev Mol Med 2006; 8: 1-23.
    • (2006) Expert Rev Mol Med , vol.8 , pp. 1-23
    • Kielty, C.M.1
  • 82
    • 33744906744 scopus 로고    scopus 로고
    • Elastin biosynthesis: The missing link in tissue-engineered blood vessels
    • Pastel A, Fine B, Sandig M, Mequanint K. Elastin biosynthesis: the missing link in tissue-engineered blood vessels. Cardiovasc Res 2006; 71: 40-9.
    • (2006) Cardiovasc Res , vol.71 , pp. 40-49
    • Pastel, A.1    Fine, B.2    Sandig, M.3    Mequanint, K.4
  • 83
    • 0037213012 scopus 로고    scopus 로고
    • Extracellular matrix in vascular morphogenesis and disease: Structure versus signal
    • Brooke BS, Karnik SK, Li DY. Extracellular matrix in vascular morphogenesis and disease: structure versus signal. Trends Cell Biol 2003; 13: 51-6.
    • (2003) Trends Cell Biol , vol.13 , pp. 51-56
    • Brooke, B.S.1    Karnik, S.K.2    Li, D.Y.3
  • 84
  • 87
    • 0030804005 scopus 로고    scopus 로고
    • Elastin point mutations cause an obstructive vascular disease, supravalvular aortic stenosis
    • Li DY. Elastin point mutations cause an obstructive vascular disease, supravalvular aortic stenosis. Hum Mol Gen 1997; 6: 1021-8.
    • (1997) Hum Mol Gen , vol.6 , pp. 1021-1028
    • Li, D.Y.1
  • 88
    • 0033552883 scopus 로고    scopus 로고
    • Atherosclerosis - an inflammatory disease
    • Ross R. Atherosclerosis - an inflammatory disease. N Engl J Med 1999; 340: 115-26.
    • (1999) N Engl J Med , vol.340 , pp. 115-126
    • Ross, R.1
  • 89
  • 90
    • 44349128895 scopus 로고    scopus 로고
    • Biogenesis of extracellular microfibrils: Multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly
    • Hubmacher D, El-Hallous EI, Nelea V, Kaartinen MT, Lee ER, Reinhardt DR. Biogenesis of extracellular microfibrils: multimerization of the fibrillin-1 C terminus into bead-like structures enables self-assembly Proc Natl Acad Sci USA 2008; 105: 6548-53.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6548-6553
    • Hubmacher, D.1    El-Hallous, E.I.2    Nelea, V.3    Kaartinen, M.T.4    Lee, E.R.5    Reinhardt, D.R.6
  • 92
    • 14844302670 scopus 로고    scopus 로고
    • Latent TGF-beta binding proteins: Orchestrators of TGF-beta availability
    • Rifkin DB. Latent TGF-beta binding proteins: orchestrators of TGF-beta availability. J Biol Chem 2005; 280: 7409-12.
    • (2005) J Biol Chem , vol.280 , pp. 7409-7412
    • Rifkin, D.B.1
  • 93
    • 0037686257 scopus 로고    scopus 로고
    • Fibulins: A versatile family of extracellular matrix proteins
    • Timpl R, Sasaki T, Kostka G, Chu M-L. Fibulins: a versatile family of extracellular matrix proteins. Nat Rev Mol Cell Biol 2003; 4: 479-89.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 479-489
    • Timpl, R.1    Sasaki, T.2    Kostka, G.3    Chu, M.-L.4
  • 94
    • 0032703916 scopus 로고    scopus 로고
    • Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4
    • Giltay R, Timpl R, Kostka G. Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4. Matrix Biol 1999; 18: 469-80.
    • (1999) Matrix Biol , vol.18 , pp. 469-480
    • Giltay, R.1    Timpl, R.2    Kostka, G.3
  • 97
    • 0034802720 scopus 로고    scopus 로고
    • Perinatal lethality and endothelial cell abnormalities in several vessel components of fibulin-1 deficient mice
    • Kostka G, Giltay R, Bloch W, Addicks K, Timpl R, Fassler R, et al. Perinatal lethality and endothelial cell abnormalities in several vessel components of fibulin-1 deficient mice Mol Cell Biol 2001; 21: 7025-34.
    • (2001) Mol Cell Biol , vol.21 , pp. 7025-7034
    • Kostka, G.1    Giltay, R.2    Bloch, W.3    Addicks, K.4    Timpl, R.5    Fassler, R.6
  • 98
    • 33947721238 scopus 로고    scopus 로고
    • Fibulin-5/DANCE has an elastogenic organizer activity that is abrogated by proteolytic cleavage in vivo
    • Hirai M, Ohbayashi T, Horiguchi M, Okawa K, Hagiwara A, Chien KR, et al. Fibulin-5/DANCE has an elastogenic organizer activity that is abrogated by proteolytic cleavage in vivo. J Cell Biol 2007; 176: 1061-71.
    • (2007) J Cell Biol , vol.176 , pp. 1061-1071
    • Hirai, M.1    Ohbayashi, T.2    Horiguchi, M.3    Okawa, K.4    Hagiwara, A.5    Chien, K.R.6
  • 100
    • 0020691997 scopus 로고
    • Germline integration of Moloney murine leukemia virus at the Mov13 locus leads to recessive lethal mutation and early embryonic death
    • Jaenisch R, Harbers K, Schnieke A, Löhler J, Chumakov I, Jähner D, et al. Germline integration of Moloney murine leukemia virus at the Mov13 locus leads to recessive lethal mutation and early embryonic death. Cell 1983; 32: 209-16.
    • (1983) Cell , vol.32 , pp. 209-216
    • Jaenisch, R.1    Harbers, K.2    Schnieke, A.3    Löhler, J.4    Chumakov, I.5    Jähner, D.6
  • 101
    • 0037686614 scopus 로고    scopus 로고
    • Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils
    • Kassner A, Hansen U, Miosge N, Reinhardt DP, Aigner T, Bruckner-Tuderman L, et al. Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils. Matrix Biol 2003; 22: 131-43.
    • (2003) Matrix Biol , vol.22 , pp. 131-143
    • Kassner, A.1    Hansen, U.2    Miosge, N.3    Reinhardt, D.P.4    Aigner, T.5    Bruckner-Tuderman, L.6
  • 102
    • 0344848632 scopus 로고    scopus 로고
    • Collagen XVI is expressed by human dermal fibroblasts and keratinocytes and is associated with the microfibrillar apparatus in the upper papillary dermis
    • Grässel S, Unsöld C, Schäcke H, Bruckner-Tuderman L, Bruckner P. Collagen XVI is expressed by human dermal fibroblasts and keratinocytes and is associated with the microfibrillar apparatus in the upper papillary dermis. Matrix Biol 1999; 18: 211-330.
    • (1999) Matrix Biol , vol.18 , pp. 211-330
    • Grässel, S.1    Unsöld, C.2    Schäcke, H.3    Bruckner-Tuderman, L.4    Bruckner, P.5
  • 103
    • 33748744382 scopus 로고    scopus 로고
    • Collagen XVI harbors an integrin α1β1 recognition site in its C-terminal domains
    • Eble JA, Kassner A, Niland S, Mörgelin M, Grifka J, Grässel S. Collagen XVI harbors an integrin α1β1 recognition site in its C-terminal domains. J Biol Chem 2006; 281: 25745-56.
    • (2006) J Biol Chem , vol.281 , pp. 25745-25756
    • Eble, J.A.1    Kassner, A.2    Niland, S.3    Mörgelin, M.4    Grifka, J.5    Grässel, S.6
  • 104
    • 0035216201 scopus 로고    scopus 로고
    • Adhesion receptors of vascular smooth muscle cells and their functions
    • Moiseeva EP. Adhesion receptors of vascular smooth muscle cells and their functions. Cadiovasc Res 2001; 52: 372-86.
    • (2001) Cadiovasc Res , vol.52 , pp. 372-386
    • Moiseeva, E.P.1
  • 105
    • 0032408807 scopus 로고    scopus 로고
    • Microfibrils from the arterial subendothelium
    • Fauvel-Lafève F. Microfibrils from the arterial subendothelium. Int Rev Cytol 1999; 188: 1-40.
    • (1999) Int Rev Cytol , vol.188 , pp. 1-40
    • Fauvel-Lafève, F.1
  • 106
    • 0033988834 scopus 로고    scopus 로고
    • Extracellular matrix of human aortic media: An ultrastructural histochemical and immunhistochemical study of the adult aortic media
    • Dingemans KP, Teeling P, Lagendijk JH, Becker AE. Extracellular matrix of human aortic media: an ultrastructural histochemical and immunhistochemical study of the adult aortic media. Anat Rec 2000; 258: 1-14.
    • (2000) Anat Rec , vol.258 , pp. 1-14
    • Dingemans, K.P.1    Teeling, P.2    Lagendijk, J.H.3    Becker, A.E.4
  • 107
    • 24944559356 scopus 로고    scopus 로고
    • Collagen VI related muscle disorders
    • Lampe AK, Bushby KMD. Collagen VI related muscle disorders. J Med Genet 2005; 42: 673-85.
    • (2005) J Med Genet , vol.42 , pp. 673-685
    • Lampe, A.K.1    Bushby, K.M.D.2
  • 108
    • 0030977355 scopus 로고    scopus 로고
    • Phenotypic modulation of smooth muscle cells after arterial injury is associated with changes in the distribution of laminin and fibronectin
    • Thyberg J, Blomgren K, Roy J, Tran PK, Hedin U. Phenotypic modulation of smooth muscle cells after arterial injury is associated with changes in the distribution of laminin and fibronectin. J Histochem Cytochem 1997; 45: 837-47.
    • (1997) J Histochem Cytochem , vol.45 , pp. 837-847
    • Thyberg, J.1    Blomgren, K.2    Roy, J.3    Tran, P.K.4    Hedin, U.5
  • 109
    • 9744274523 scopus 로고    scopus 로고
    • The spatial and temporal expression patterns of integrins α9β1 and one of its ligands, the EIIIA segment of fibronectin, in cutaneous wound healing
    • Singh P, Reimer CL, Peters JH, Stepp MA, Hynes RO, Van de Winter L. The spatial and temporal expression patterns of integrins α9β1 and one of its ligands, the EIIIA segment of fibronectin, in cutaneous wound healing. J Invest Dermatol 2004; 123: 1176-81.
    • (2004) J Invest Dermatol , vol.123 , pp. 1176-1181
    • Singh, P.1    Reimer, C.L.2    Peters, J.H.3    Stepp, M.A.4    Hynes, R.O.5    Van de Winter, L.6
  • 110
    • 38649107709 scopus 로고    scopus 로고
    • Pericytes: Gatekeepers in tumour cell metastasis?
    • Gerhardt H, Semb H. Pericytes: gatekeepers in tumour cell metastasis? J Mol Med 2008; 86: 135-44.
    • (2008) J Mol Med , vol.86 , pp. 135-144
    • Gerhardt, H.1    Semb, H.2
  • 111
    • 33847344251 scopus 로고    scopus 로고
    • Review of the pericyte during angiogenesis and its role in cancer and diabetic retinopathy
    • Hall AP. Review of the pericyte during angiogenesis and its role in cancer and diabetic retinopathy. Toxicol Pathol 2006; 34: 763-75.
    • (2006) Toxicol Pathol , vol.34 , pp. 763-775
    • Hall, A.P.1
  • 112
    • 34249689753 scopus 로고    scopus 로고
    • Molecular regulation of angiogenesis and lymphangiogenesis
    • Adams RH, Alitalo K. Molecular regulation of angiogenesis and lymphangiogenesis. Nat Mol Cell Biol 2007; 8: 464-78.
    • (2007) Nat Mol Cell Biol , vol.8 , pp. 464-478
    • Adams, R.H.1    Alitalo, K.2
  • 113
    • 2442681602 scopus 로고    scopus 로고
    • Proteoglycans in atherosclerosis and restenosis: Key roles for versican
    • Wight TN, Merrilees MJ. Proteoglycans in atherosclerosis and restenosis: key roles for versican. Circ Res 2004; 94: 1158-67.
    • (2004) Circ Res , vol.94 , pp. 1158-1167
    • Wight, T.N.1    Merrilees, M.J.2
  • 114
    • 0037040276 scopus 로고    scopus 로고
    • Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks
    • Isogai Z, Aspberg A, Keene DR, Ono RN, Reinhardt DR, Sakai LY. Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks. J Biol Chem 2002; 277: 4565-72.
    • (2002) J Biol Chem , vol.277 , pp. 4565-4572
    • Isogai, Z.1    Aspberg, A.2    Keene, D.R.3    Ono, R.N.4    Reinhardt, D.R.5    Sakai, L.Y.6
  • 115
    • 0033575208 scopus 로고    scopus 로고
    • Fibulin-1 is a ligand for the C-type lectin domains of aggregan and versican
    • Aspberg A, Adam S, Kostka G, Timpl R, Heinegard D. Fibulin-1 is a ligand for the C-type lectin domains of aggregan and versican. J Biol Chem 1999; 274: 20444-9.
    • (1999) J Biol Chem , vol.274 , pp. 20444-20449
    • Aspberg, A.1    Adam, S.2    Kostka, G.3    Timpl, R.4    Heinegard, D.5
  • 116
    • 0035847046 scopus 로고    scopus 로고
    • The proteoglycans aggregan and versican form networks with fibulin-2 through their lectin domain binding
    • Olin AI, Mörgelin M, Sasaki T, Timpl R, Heinegard D, Aspberg A. The proteoglycans aggregan and versican form networks with fibulin-2 through their lectin domain binding. J Biol Chem 2001; 276: 1253-61.
    • (2001) J Biol Chem , vol.276 , pp. 1253-1261
    • Olin, A.I.1    Mörgelin, M.2    Sasaki, T.3    Timpl, R.4    Heinegard, D.5    Aspberg, A.6
  • 117
    • 27244432621 scopus 로고    scopus 로고
    • The interaction of versican with its binding partners
    • Wu YJ, La Pierre DP, Wu J, Yee AJ, Yang BB. The interaction of versican with its binding partners. Cell Res 2005; 15: 483-94.
    • (2005) Cell Res , vol.15 , pp. 483-494
    • Wu, Y.J.1    La Pierre, D.P.2    Wu, J.3    Yee, A.J.4    Yang, B.B.5
  • 118
    • 0038376002 scopus 로고    scopus 로고
    • Molecular regulation of vessel maturation
    • Jain RK. Molecular regulation of vessel maturation. Nat Med 2003; 9: 685-93.
    • (2003) Nat Med , vol.9 , pp. 685-693
    • Jain, R.K.1
  • 120
    • 19944402914 scopus 로고    scopus 로고
    • Endothelial cell regulation of matrix metalloproteinases
    • Haas TL. Endothelial cell regulation of matrix metalloproteinases. Can J Physiol Pharmacol 2005; 83: 1-7.
    • (2005) Can J Physiol Pharmacol , vol.83 , pp. 1-7
    • Haas, T.L.1
  • 121
    • 41949136223 scopus 로고    scopus 로고
    • Endothelial-stromal interactions in angiogenesis
    • Hughes CCW. Endothelial-stromal interactions in angiogenesis. Curr Opin Hematol 2008; 15: 204-9.
    • (2008) Curr Opin Hematol , vol.15 , pp. 204-209
    • Hughes, C.C.W.1
  • 122
    • 1342300684 scopus 로고    scopus 로고
    • Matrix metalloproteinases and matrikines in angiogenesis
    • Bellon G, Martiny L, Robinet A. Matrix metalloproteinases and matrikines in angiogenesis. Crit Rev Oncol Hematol 2004; 49: 203-20.
    • (2004) Crit Rev Oncol Hematol , vol.49 , pp. 203-220
    • Bellon, G.1    Martiny, L.2    Robinet, A.3
  • 124
    • 33644683263 scopus 로고    scopus 로고
    • Endothelial extracellular matrix: Biosynthesis, remodeling, and functions during vascular morphogenesis and neovessel stabilization
    • Davis GE, Senger DR. Endothelial extracellular matrix: biosynthesis, remodeling, and functions during vascular morphogenesis and neovessel stabilization. Circ Res 2005; 97: 1093-107.
    • (2005) Circ Res , vol.97 , pp. 1093-1107
    • Davis, G.E.1    Senger, D.R.2
  • 125
    • 10744223801 scopus 로고    scopus 로고
    • Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin
    • Hamano Y, Zeisberg M, Sugimoto H, Lively JC, Maeshima Y, Yang C, et al. Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin. Cancer Cell 2003; 3: 589-601.
    • (2003) Cancer Cell , vol.3 , pp. 589-601
    • Hamano, Y.1    Zeisberg, M.2    Sugimoto, H.3    Lively, J.C.4    Maeshima, Y.5    Yang, C.6
  • 126
    • 34250702237 scopus 로고    scopus 로고
    • Cell-matrix adhesion in vascular development
    • Hynes RO. Cell-matrix adhesion in vascular development. J Thromb Haemost 2007; 5: 32-40.
    • (2007) J Thromb Haemost , vol.5 , pp. 32-40
    • Hynes, R.O.1
  • 127
    • 0035793037 scopus 로고    scopus 로고
    • Disruption of matrix metalloproteinase 2 binding to integrin αvβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo
    • Silletti S, Kessler T, Goldberg J, Boger DL, Cheresh DA. Disruption of matrix metalloproteinase 2 binding to integrin αvβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc Natl Acad Sci USA 2001; 98: 119-24.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 119-124
    • Silletti, S.1    Kessler, T.2    Goldberg, J.3    Boger, D.L.4    Cheresh, D.A.5
  • 128
    • 36949016403 scopus 로고    scopus 로고
    • Type I collagen and collagen mimetics as angiogenesis promoting superpolymers
    • Twardowski T, Fertala A, Orgel JP, San Antonio JD. Type I collagen and collagen mimetics as angiogenesis promoting superpolymers. Curr Pharm Des 2007; 13: 3608-21.
    • (2007) Curr Pharm Des , vol.13 , pp. 3608-3621
    • Twardowski, T.1    Fertala, A.2    Orgel, J.P.3    San Antonio, J.D.4
  • 129
    • 34247872986 scopus 로고    scopus 로고
    • The extracellular matrix and blood vessel formation: Not just a scaffold
    • Rhodes JM, Simons M. The extracellular matrix and blood vessel formation: not just a scaffold. J Cell Mol Med 2007; 11: 176-205.
    • (2007) J Cell Mol Med , vol.11 , pp. 176-205
    • Rhodes, J.M.1    Simons, M.2
  • 130
    • 0037414766 scopus 로고    scopus 로고
    • Collagen I initiates endothelial cell morphogenesis by inducing actin polymerization through suppression of cyclic AMP and protein kinase A
    • Whelan MC, Senger DR, Sage EH. Collagen I initiates endothelial cell morphogenesis by inducing actin polymerization through suppression of cyclic AMP and protein kinase A. J Biol Chem 2003; 278: 37895-901.
    • (2003) J Biol Chem , vol.278 , pp. 37895-37901
    • Whelan, M.C.1    Senger, D.R.2    Sage, E.H.3
  • 132
    • 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, Fujisawa H, et al. Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. Genes Dev 2002; 16: 2684-98.
    • (2002) Genes Dev , vol.16 , pp. 2684-2698
    • Ruhrberg, C.1    Gerhardt, H.2    Golding, M.3    Watson, R.4    Ioannidou, S.5    Fujisawa, H.6
  • 133
    • 33847046849 scopus 로고    scopus 로고
    • Dll4 signalling through Notch1 regulates formation of tip cells during angiogenesis
    • Hellström M, Phng LK, Hofmann JJ, Wallgard E, Coultas L, Lindblom P, et al. Dll4 signalling through Notch1 regulates formation of tip cells during angiogenesis. Nature 2007; 445: 776-80.
    • (2007) Nature , vol.445 , pp. 776-780
    • Hellström, M.1    Phng, L.K.2    Hofmann, J.J.3    Wallgard, E.4    Coultas, L.5    Lindblom, P.6
  • 134
    • 34249744576 scopus 로고    scopus 로고
    • Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells
    • Yana I, Sagara H, Takaki S, Takatsu K, Nakamura K, Nakao K, et al. Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells. J Cell Sci 2007; 120: 1607-14.
    • (2007) J Cell Sci , vol.120 , pp. 1607-1614
    • Yana, I.1    Sagara, H.2    Takaki, S.3    Takatsu, K.4    Nakamura, K.5    Nakao, K.6
  • 136
    • 0036829020 scopus 로고    scopus 로고
    • Molecular basis of endothelial cell morphogenesis in three-dimensional collagen matrices
    • Davis GE, Bayless KJ, Mavila A. Molecular basis of endothelial cell morphogenesis in three-dimensional collagen matrices. Anat Rec 2002; 268: 252-75.
    • (2002) Anat Rec , vol.268 , pp. 252-275
    • Davis, G.E.1    Bayless, K.J.2    Mavila, A.3
  • 137
    • 0029967619 scopus 로고    scopus 로고
    • An α2β1 integrin-dependent pinocytic mechanism involving vacuole formation and coalescence regulates capillary lumen and tube formation in three-dimensional collagen matrix
    • Davis GE, Camarillo CW. An α2β1 integrin-dependent pinocytic mechanism involving vacuole formation and coalescence regulates capillary lumen and tube formation in three-dimensional collagen matrix. Exp Cell Res 1996; 224: 39-51.
    • (1996) Exp Cell Res , vol.224 , pp. 39-51
    • Davis, G.E.1    Camarillo, C.W.2
  • 139
    • 0005170476 scopus 로고    scopus 로고
    • An integrin and Rho GTPase-dependent pinocytic vacuole mechanism controls capillary lumen formation in collagen and fibrin matrices
    • Davis GE, Bayless KJ. An integrin and Rho GTPase-dependent pinocytic vacuole mechanism controls capillary lumen formation in collagen and fibrin matrices. Microcirculation 2003; 10: 27-44.
    • (2003) Microcirculation , vol.10 , pp. 27-44
    • Davis, G.E.1    Bayless, K.J.2
  • 140
    • 33748799968 scopus 로고    scopus 로고
    • Molecular balance of capillary tube formation versus regression in wound repair: Role of matrix metalloproteinases and their inhibitors
    • Davis GE, Saunders WB. Molecular balance of capillary tube formation versus regression in wound repair: role of matrix metalloproteinases and their inhibitors. J Investig Dermatol Symp Proc 2006; 2006: 44-56.
    • (2006) J Investig Dermatol Symp Proc 2006 , pp. 44-56
    • Davis, G.E.1    Saunders, W.B.2
  • 141
    • 85164057334 scopus 로고    scopus 로고
    • Miner JH. Laminins and their roles in mammals. Microsc Res Tech 2008; 71: 349-56.
    • Miner JH. Laminins and their roles in mammals. Microsc Res Tech 2008; 71: 349-56.
  • 142
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco PD, Amenta PS, Patton BL. Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol 2004; 22: 1677-85.
    • (2004) Matrix Biol , vol.22 , pp. 1677-1685
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 144
    • 11844254414 scopus 로고    scopus 로고
    • Normalization of tumor vasculature: An emerging concept in antiangiogenic therapy
    • Jain RK. Normalization of tumor vasculature: an emerging concept in antiangiogenic therapy. Science 2005; 307: 58-62.
    • (2005) Science , vol.307 , pp. 58-62
    • Jain, R.K.1
  • 145
    • 0031834239 scopus 로고    scopus 로고
    • A plasticity window for blood vessel remodelling is defined by pericyte coverage of the preformed endothelial network and is regulated by PDGF-B and VEGF
    • Benjamin LE, Hemo I, Keshet E. A plasticity window for blood vessel remodelling is defined by pericyte coverage of the preformed endothelial network and is regulated by PDGF-B and VEGF. Development 1998; 125: 1591-8.
    • (1998) Development , vol.125 , pp. 1591-1598
    • Benjamin, L.E.1    Hemo, I.2    Keshet, E.3
  • 147
    • 0034730784 scopus 로고    scopus 로고
    • Angiopoietin-1 is an antipermeability and anti-inflammatory agent in vitro and targets cell junctions
    • Gamble JR, Drew J, Trezise L, Underwood A, Parsons M, Kasminkas L, et al. Angiopoietin-1 is an antipermeability and anti-inflammatory agent in vitro and targets cell junctions. Circ Res 2000; 87: 603-7.
    • (2000) Circ Res , vol.87 , pp. 603-607
    • Gamble, J.R.1    Drew, J.2    Trezise, L.3    Underwood, A.4    Parsons, M.5    Kasminkas, L.6
  • 148
    • 0034036689 scopus 로고    scopus 로고
    • Angiopoietin-1 protects the adult vasculature against plasma leakage
    • Thurston G, Rudge JS, Ioffe E, Zhou H, Ross L, Croll SD, et al. Angiopoietin-1 protects the adult vasculature against plasma leakage. Nat Med 2000; 6: 460-3.
    • (2000) Nat Med , vol.6 , pp. 460-463
    • Thurston, G.1    Rudge, J.S.2    Ioffe, E.3    Zhou, H.4    Ross, L.5    Croll, S.D.6
  • 149
    • 0033601357 scopus 로고    scopus 로고
    • Leakage-resistant blood vessels in mice transgenically overexpressing angiopoietin-1
    • Thurston G, Suri C, Smith K, McClain J, Sato TN, Yancopoulos GD, et al. Leakage-resistant blood vessels in mice transgenically overexpressing angiopoietin-1. Science 1999; 286: 2511-4.
    • (1999) Science , vol.286 , pp. 2511-2514
    • Thurston, G.1    Suri, C.2    Smith, K.3    McClain, J.4    Sato, T.N.5    Yancopoulos, G.D.6
  • 150
    • 0042125242 scopus 로고    scopus 로고
    • Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall
    • Lindblom P, Gerhardt H, Liebner S, Abramsson A, Enge M, Hellstrom M, et al. Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall. Genes Dev 2003; 17: 1835-40.
    • (2003) Genes Dev , vol.17 , pp. 1835-1840
    • Lindblom, P.1    Gerhardt, H.2    Liebner, S.3    Abramsson, A.4    Enge, M.5    Hellstrom, M.6
  • 151
    • 33846955819 scopus 로고    scopus 로고
    • Defective N-sulfation of heparan sulfate proteoglycans limits PDGF-BB binding and pericyte recruitment in vascular development
    • Abramsson A, Kurup S, Busse M, Yamada S, Lindblom P, Schallmeiner E, et al. Defective N-sulfation of heparan sulfate proteoglycans limits PDGF-BB binding and pericyte recruitment in vascular development. Genes Dev 2007; 21: 316-31.
    • (2007) Genes Dev , vol.21 , pp. 316-331
    • Abramsson, A.1    Kurup, S.2    Busse, M.3    Yamada, S.4    Lindblom, P.5    Schallmeiner, E.6
  • 152
    • 33745433579 scopus 로고    scopus 로고
    • Heparan sulphate requirement in platelet-derived growth factor B-mediated pericyte recruitment
    • Kurup S, Abramsson A, Li JP, Lindahl U, Kjellen L, Betsholtz C, et al. Heparan sulphate requirement in platelet-derived growth factor B-mediated pericyte recruitment. Biochem Soc Trans 2006; 34: 454-5.
    • (2006) Biochem Soc Trans , vol.34 , pp. 454-455
    • Kurup, S.1    Abramsson, A.2    Li, J.P.3    Lindahl, U.4    Kjellen, L.5    Betsholtz, C.6
  • 153
    • 17444393268 scopus 로고    scopus 로고
    • An MT1-MMP-PDGF receptor-β axis regulates mural cell investment of the microvasculature
    • Lehti K, Allen E, Birkedal-Hansen H, Holmbeck K, Miyake Y, Chun TH, et al. An MT1-MMP-PDGF receptor-β axis regulates mural cell investment of the microvasculature. Genes Dev 2005; 19: 979-91.
    • (2005) Genes Dev , vol.19 , pp. 979-991
    • Lehti, K.1    Allen, E.2    Birkedal-Hansen, H.3    Holmbeck, K.4    Miyake, Y.5    Chun, T.H.6
  • 154
    • 28744431719 scopus 로고    scopus 로고
    • Endothelial survival factors and spatial completion, but not pericyte coverage of retinal capillaries determine vessel plasticity
    • Hoffmann J, Feng Y, vom Hagen F, Hillenbrand A, Lin J, Erber R, et al. Endothelial survival factors and spatial completion, but not pericyte coverage of retinal capillaries determine vessel plasticity. FASEB J 2005; 19: 2035-6.
    • (2005) FASEB J , vol.19 , pp. 2035-2036
    • Hoffmann, J.1    Feng, Y.2    vom Hagen, F.3    Hillenbrand, A.4    Lin, J.5    Erber, R.6
  • 155
    • 14644440555 scopus 로고    scopus 로고
    • Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis
    • Hicklin DJ, Ellis LM. Role of the vascular endothelial growth factor pathway in tumor growth and angiogenesis. J Clin Oncol 2005; 23: 1011-27.
    • (2005) J Clin Oncol , vol.23 , pp. 1011-1027
    • Hicklin, D.J.1    Ellis, L.M.2
  • 156
    • 33947390863 scopus 로고    scopus 로고
    • Alternative splicing in angiogenesis: The vascular endothelial growth factor paradigm
    • Ladomery MR, Harper SJ, Bates DO. Alternative splicing in angiogenesis: the vascular endothelial growth factor paradigm. Cancer Lett 2007; 249: 133-42.
    • (2007) Cancer Lett , vol.249 , pp. 133-142
    • Ladomery, M.R.1    Harper, S.J.2    Bates, D.O.3
  • 157
    • 33344474964 scopus 로고    scopus 로고
    • Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis
    • Shibuya M, Claesson-Welsh L. Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis. Exp Cell Res 2006; 312: 549-60.
    • (2006) Exp Cell Res , vol.312 , pp. 549-560
    • Shibuya, M.1    Claesson-Welsh, L.2
  • 158
    • 43249114710 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-dependent and - independent regulation of angiogenesis
    • Shibuya M. Vascular endothelial growth factor-dependent and - independent regulation of angiogenesis. BMB Rep 2008; 41: 278-86.
    • (2008) BMB Rep , vol.41 , pp. 278-286
    • Shibuya, M.1
  • 159
    • 17744396472 scopus 로고    scopus 로고
    • Signalling via vascular endothelial growth factor receptor-3 is sufficient for lymphangiogenesis in transgenic mice
    • Veikkola T, Jussila L, Makinen T, Karpanen T, Jeltsch M, Petrova TV, et al. Signalling via vascular endothelial growth factor receptor-3 is sufficient for lymphangiogenesis in transgenic mice. EMBO J 2001; 20: 1223-31.
    • (2001) EMBO J , vol.20 , pp. 1223-1231
    • Veikkola, T.1    Jussila, L.2    Makinen, T.3    Karpanen, T.4    Jeltsch, M.5    Petrova, T.V.6
  • 162
    • 0031572281 scopus 로고    scopus 로고
    • Developmental regulation of the laminin alpha5 chain suggests a role in epithelial and endothelial cell maturation
    • Sorokin LM, Pausch F, Frieser M, Kroger S, Ohage E, Deutzmann R. Developmental regulation of the laminin alpha5 chain suggests a role in epithelial and endothelial cell maturation. Dev Biol 1997; 189: 285-300.
    • (1997) Dev Biol , vol.189 , pp. 285-300
    • Sorokin, L.M.1    Pausch, F.2    Frieser, M.3    Kroger, S.4    Ohage, E.5    Deutzmann, R.6
  • 163
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao Y, Schwarzbauer JE. Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol 2005; 24: 389-99.
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 164
  • 165
    • 0029862310 scopus 로고    scopus 로고
    • Fibronectin isoform distribution in the mouse. I. The alternatively spliced EIIIB, EIIIA, and V segments show widespread codistribution in the developing mouse embryo
    • Peters JH, Hynes RO. Fibronectin isoform distribution in the mouse. I. The alternatively spliced EIIIB, EIIIA, and V segments show widespread codistribution in the developing mouse embryo. Cell Adhes Commun 1996; 4: 103-25.
    • (1996) Cell Adhes Commun , vol.4 , pp. 103-125
    • Peters, J.H.1    Hynes, R.O.2
  • 167
    • 0034715943 scopus 로고    scopus 로고
    • Adhesion modulation by antiadhesive molecules of the extracellular matrix
    • Ohrend G, Chiquet-Ehrismann R. Adhesion modulation by antiadhesive molecules of the extracellular matrix. Exp Cell Res 2000; 261: 104-10.
    • (2000) Exp Cell Res , vol.261 , pp. 104-110
    • Ohrend, G.1    Chiquet-Ehrismann, R.2
  • 168
    • 33646271127 scopus 로고    scopus 로고
    • Vascular tenascin-C regulates cardiac endothelial phenotype and neovascularization
    • Ballard VI, Sharma A, Duigan I, Holm JM, Chin A, Choi R, et al. Vascular tenascin-C regulates cardiac endothelial phenotype and neovascularization. FASEB J 2006; 20: 717-9.
    • (2006) FASEB J , vol.20 , pp. 717-719
    • Ballard, V.I.1    Sharma, A.2    Duigan, I.3    Holm, J.M.4    Chin, A.5    Choi, R.6
  • 169
    • 1842454323 scopus 로고    scopus 로고
    • Interaction between cell and extracellular matrix in heart disease: Multiple roles of tenascin-C in tissue remodeling
    • Imanaka-Yoshida K, Hiroe M, Yoshida T. Interaction between cell and extracellular matrix in heart disease: multiple roles of tenascin-C in tissue remodeling. Histol Histopathol 2004; 19: 517-24.
    • (2004) Histol Histopathol , vol.19 , pp. 517-524
    • Imanaka-Yoshida, K.1    Hiroe, M.2    Yoshida, T.3
  • 171
    • 4444353257 scopus 로고    scopus 로고
    • Tumor progression: The effects of thrombospondin-1 and -2
    • Lawler J, Detmar M. Tumor progression: the effects of thrombospondin-1 and -2. Int J Biochem Cell Biol 2004; 36: 1038-45.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1038-1045
    • Lawler, J.1    Detmar, M.2
  • 172
    • 34548821303 scopus 로고    scopus 로고
    • Thrombospondin-based antiangiogenic therapy
    • Zhang X, Lawler J. Thrombospondin-based antiangiogenic therapy. Microvasc Res 2007; 74: 90-9.
    • (2007) Microvasc Res , vol.74 , pp. 90-99
    • Zhang, X.1    Lawler, J.2
  • 173
    • 20144379162 scopus 로고    scopus 로고
    • Endogenous inhibitors of angiogenesis
    • Nyberg P, Xie L, Kalluri R. Endogenous inhibitors of angiogenesis. Cancer Res 2005; 65: 3967-79.
    • (2005) Cancer Res , vol.65 , pp. 3967-3979
    • Nyberg, P.1    Xie, L.2    Kalluri, R.3
  • 174
    • 0031454617 scopus 로고    scopus 로고
    • Endostatin: An endogenous inhibitor of angiogenesis and tumor growth
    • O'Reilly MS, Boehm T, Sing Y, Fukai N, Vasios G, Lane WS, et al. Endostatin: an endogenous inhibitor of angiogenesis and tumor growth. Cell 1997; 88: 277-85.
    • (1997) Cell , vol.88 , pp. 277-285
    • O'Reilly, M.S.1    Boehm, T.2    Sing, Y.3    Fukai, N.4    Vasios, G.5    Lane, W.S.6
  • 175
    • 0141621070 scopus 로고    scopus 로고
    • Endostatin associates with lipid rafts and induces reorganization of the actin cytoskeleton via down-regulation of RhoA activity
    • Wickström SA, Alitalo K, Keski-Oja J. Endostatin associates with lipid rafts and induces reorganization of the actin cytoskeleton via down-regulation of RhoA activity. J Biol Chem 2003; 278: 37895-901.
    • (2003) J Biol Chem , vol.278 , pp. 37895-37901
    • Wickström, S.A.1    Alitalo, K.2    Keski-Oja, J.3
  • 176
    • 47349107672 scopus 로고    scopus 로고
    • Research advances of endostatin and its short internal fragments
    • Xu HL, Tan HN, Wang FS, Tang W. Research advances of endostatin and its short internal fragments. Curr Protein Pept Sci 2008; 9: 275-83.
    • (2008) Curr Protein Pept Sci , vol.9 , pp. 275-283
    • Xu, H.L.1    Tan, H.N.2    Wang, F.S.3    Tang, W.4
  • 178
    • 0037423391 scopus 로고    scopus 로고
    • Mongiat M, Sweeney SM, San Antonio JD, Fu J, Iozzo RV. Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J Biol Chem 2003; 278: 4238-49.
    • Mongiat M, Sweeney SM, San Antonio JD, Fu J, Iozzo RV. Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J Biol Chem 2003; 278: 4238-49.
  • 179
    • 3142736457 scopus 로고    scopus 로고
    • Bix G, Fu J, Gonzalez EM, Macro L, Barker A, Campbell S, et al. Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin. J Cell Biol 2004; 166: 97-109.
    • Bix G, Fu J, Gonzalez EM, Macro L, Barker A, Campbell S, et al. Endorepellin causes endothelial cell disassembly of actin cytoskeleton and focal adhesions through alpha2beta1 integrin. J Cell Biol 2004; 166: 97-109.
  • 180
    • 35748947260 scopus 로고    scopus 로고
    • Type IV collagen-derived angiogenesis inhibitors
    • Mundel TM, Kalluri R. Type IV collagen-derived angiogenesis inhibitors. Microvasc Res 2007; 74: 85-9.
    • (2007) Microvasc Res , vol.74 , pp. 85-89
    • Mundel, T.M.1    Kalluri, R.2
  • 181
    • 0034677760 scopus 로고    scopus 로고
    • New functions for non-collagenous domains of human collagen type IV. Novel integrin ligands inhibiting angiogenesis and tumor growth in vivo
    • Petitclerc E, Boutaud A, Prestayko A, Xu J, Sado Y, Ninomiya Y, et al. New functions for non-collagenous domains of human collagen type IV. Novel integrin ligands inhibiting angiogenesis and tumor growth in vivo. J Biol Chem 2000; 275: 8051-61.
    • (2000) J Biol Chem , vol.275 , pp. 8051-8061
    • Petitclerc, E.1    Boutaud, A.2    Prestayko, A.3    Xu, J.4    Sado, Y.5    Ninomiya, Y.6
  • 184
    • 20144374161 scopus 로고    scopus 로고
    • Canstatin acts on endothelial and tumor cells via mitochondrial damage initiated through interaction with alphavbeta3 and alphavbeta5 integrins
    • Magnon C, Galaup A, Mullan B, Rouffiac V, Bouquet C, Bidart JM, et al. Canstatin acts on endothelial and tumor cells via mitochondrial damage initiated through interaction with alphavbeta3 and alphavbeta5 integrins. Cancer Res 2005; 65: 4353-61.
    • (2005) Cancer Res , vol.65 , pp. 4353-4361
    • Magnon, C.1    Galaup, A.2    Mullan, B.3    Rouffiac, V.4    Bouquet, C.5    Bidart, J.M.6
  • 186
    • 57149143771 scopus 로고    scopus 로고
    • Inhibition of tumor angiogenesis by tumstatin: Insights into signaling mechanisms and implications in cancer regression
    • in press
    • Sudhakar A, Boosani CS. Inhibition of tumor angiogenesis by tumstatin: insights into signaling mechanisms and implications in cancer regression. Pharm Res 2008; in press:
    • (2008) Pharm Res
    • Sudhakar, A.1    Boosani, C.S.2
  • 187
    • 0035940970 scopus 로고    scopus 로고
    • NC1 domain of human type VIII collagen (α1) inhibits bovine endothelial cell proliferation and causes cell apoptosis
    • Xu R, Yao ZY, Xin L, Zhang Q, Li TP, Gan RB, et al. NC1 domain of human type VIII collagen (α1) inhibits bovine endothelial cell proliferation and causes cell apoptosis. Biochem Biophys Res Commun 2001; 289: 264-8.
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 264-268
    • Xu, R.1    Yao, Z.Y.2    Xin, L.3    Zhang, Q.4    Li, T.P.5    Gan, R.B.6
  • 188
    • 0026652898 scopus 로고
    • A fibronectin self-assembly site involved in fibronectin matrix assembly: Reconstruction in a synthetic peptide
    • Morla A, Ruoslahti E. A fibronectin self-assembly site involved in fibronectin matrix assembly: reconstruction in a synthetic peptide. J Cell Biol 1992; 118: 421-9.
    • (1992) J Cell Biol , vol.118 , pp. 421-429
    • Morla, A.1    Ruoslahti, E.2
  • 189
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla A, Zhang Z, Ruoslahti E. Superfibronectin is a functionally distinct form of fibronectin. Nature 1994; 367: 193-6.
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 190
    • 0035895247 scopus 로고    scopus 로고
    • A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis
    • Yi M, Ruoslahti E. A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis. Proc Natl Acad Sci USA 2001; 98: 620-4.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 620-624
    • Yi, M.1    Ruoslahti, E.2
  • 191
    • 28244461501 scopus 로고    scopus 로고
    • Domain unfolding plays a role in superfibronectin formation
    • Ohashi T, Erickson HP. Domain unfolding plays a role in superfibronectin formation. J Biol Chem 2005; 280: 39143-51.
    • (2005) J Biol Chem , vol.280 , pp. 39143-39151
    • Ohashi, T.1    Erickson, H.P.2
  • 192
    • 11244261710 scopus 로고    scopus 로고
    • Ambesi A, Klein RM, Pumiglia KM, McKeown-Longo PJ. Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells. Cancer Res 2005; 65: 148-56.
    • Ambesi A, Klein RM, Pumiglia KM, McKeown-Longo PJ. Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells. Cancer Res 2005; 65: 148-56.
  • 193
    • 2342431195 scopus 로고    scopus 로고
    • Angiostatin and anti-angiogenic therapy in human disease
    • Wahl ML, Moser TL, Pizzo SV. Angiostatin and anti-angiogenic therapy in human disease. Recent Prog Horm Res 2004; 59: 73-104.
    • (2004) Recent Prog Horm Res , vol.59 , pp. 73-104
    • Wahl, M.L.1    Moser, T.L.2    Pizzo, S.V.3
  • 196
    • 15244345997 scopus 로고    scopus 로고
    • Maquart FX, Bellon G, Pasco S, Monboisse JC. Matrikines in the regulation of extracellular matrix degradation. Biochimie 2005; 87: 353-60.
    • Maquart FX, Bellon G, Pasco S, Monboisse JC. Matrikines in the regulation of extracellular matrix degradation. Biochimie 2005; 87: 353-60.
  • 197
    • 0035895883 scopus 로고    scopus 로고
    • Conformational dependence of collagenase (matrix metalloproteinase-1) up-regulation by elastin peptides in cultured fibroblasts
    • Brassart B, Fuchs P, Huet E, Alix AJ, Wallach J, Tamburro AM, et al. Conformational dependence of collagenase (matrix metalloproteinase-1) up-regulation by elastin peptides in cultured fibroblasts. J Biol Chem 2001; 276: 5222-7227.
    • (2001) J Biol Chem , vol.276 , pp. 5222-7227
    • Brassart, B.1    Fuchs, P.2    Huet, E.3    Alix, A.J.4    Wallach, J.5    Tamburro, A.M.6
  • 198
    • 33845416458 scopus 로고    scopus 로고
    • Human leukocyte elastase hydrolysis of peptides derived from human elastin exon 24
    • Lombard C, Arzel L, Bouchu D, Wallach J, Saulnier J. Human leukocyte elastase hydrolysis of peptides derived from human elastin exon 24. Biochimie 2006; 88: 1915-21.
    • (2006) Biochimie , vol.88 , pp. 1915-1921
    • Lombard, C.1    Arzel, L.2    Bouchu, D.3    Wallach, J.4    Saulnier, J.5
  • 200
    • 14044271602 scopus 로고    scopus 로고
    • Elastin-derived peptides enhance angiogenesis by promoting endothelial cell migration and tubulogenesis through upregulation of MT1-MMP
    • Robinet A, Fahem A, Cauchard JH, Huet E, Vincent L, Lorimier S, et al. Elastin-derived peptides enhance angiogenesis by promoting endothelial cell migration and tubulogenesis through upregulation of MT1-MMP. J Cell Sci 2005; 118: 343-56.
    • (2005) J Cell Sci , vol.118 , pp. 343-356
    • Robinet, A.1    Fahem, A.2    Cauchard, J.H.3    Huet, E.4    Vincent, L.5    Lorimier, S.6
  • 201
    • 33846168055 scopus 로고    scopus 로고
    • Targeted in vivo imaging of angiogenesis: Present status and perspectives
    • Choe YS, Lee KH. Targeted in vivo imaging of angiogenesis: present status and perspectives. Curr Pharm Des 2007; 13: 17-31.
    • (2007) Curr Pharm Des , vol.13 , pp. 17-31
    • Choe, Y.S.1    Lee, K.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.