메뉴 건너뛰기




Volumn 4, Issue 3, 2004, Pages 163-176

Fibrin mechanisms and functions in nervous system pathology

Author keywords

[No Author keywords available]

Indexed keywords

ALTEPLASE; ANTICOAGULANT AGENT; BASIC FIBROBLAST GROWTH FACTOR; BLOOD CLOTTING FACTOR; BLOOD CLOTTING INHIBITOR; CADHERIN; CD11B ANTIGEN; CD18 ANTIGEN; D DIMER; FIBRIN; FIBRIN DEGRADATION PRODUCT; FIBRINOGEN; FIBRINOGEN RECEPTOR; FIBRINOLYTIC AGENT; FIBROBLAST GROWTH FACTOR 2; FIBRONECTIN; GELSOLIN; INTERCELLULAR ADHESION MOLECULE 1; PLASMINOGEN; PROTEINASE; SOMATOMEDIN BINDING PROTEIN 3; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR; VASCULOTROPIN; VERY LATE ACTIVATION ANTIGEN 5;

EID: 3242690811     PISSN: 15340384     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (116)

References (166)
  • 2
    • 0037077134 scopus 로고    scopus 로고
    • Sensory nerves determine the pattern of arterial differentiation and blood vessel branching in the skin
    • Mukouyama, Y.S., Shin, D., Britsch, S., Taniguchi, M., and Anderson, D.J. Sensory nerves determine the pattern of arterial differentiation and blood vessel branching in the skin. Cell 109, 693-705 (2002).
    • (2002) Cell , vol.109 , pp. 693-705
    • Mukouyama, Y.S.1    Shin, D.2    Britsch, S.3    Taniguchi, M.4    Anderson, D.J.5
  • 4
    • 0037130466 scopus 로고    scopus 로고
    • Artemin is a vascular-derived neurotropic factor for developing sympathetic neurons
    • Honma, Y., Araki, T., Gianino, S., Bruce, A., Heuckeroth, R., Johnson, E., and Millbrandt, J. Artemin is a vascular-derived neurotropic factor for developing sympathetic neurons. Neuron 35, 267-282 (2002).
    • (2002) Neuron , vol.35 , pp. 267-282
    • Honma, Y.1    Araki, T.2    Gianino, S.3    Bruce, A.4    Heuckeroth, R.5    Johnson, E.6    Millbrandt, J.7
  • 5
    • 0036837873 scopus 로고    scopus 로고
    • Defective associations between blood vessels and brain parenchyma lead to cerebral hemorrhage in mice lacking av integrins
    • McCarty, J.H., Monahan-Earley, R.A., Brown, L.F. et al. Defective associations between blood vessels and brain parenchyma lead to cerebral hemorrhage in mice lacking av integrins. Mol. Cell. Biol. 22, 7667-7677 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7667-7677
    • McCarty, J.H.1    Monahan-Earley, R.A.2    Brown, L.F.3
  • 6
    • 0034597430 scopus 로고    scopus 로고
    • Vascular niche for adult hippocampal neurogenesis
    • Palmer, T.D., Willhoite, A.R., and Gage, F.H. Vascular niche for adult hippocampal neurogenesis. J. Comp. Neurol. 425, 479-494 (2000).
    • (2000) J. Comp. Neurol. , vol.425 , pp. 479-494
    • Palmer, T.D.1    Willhoite, A.R.2    Gage, F.H.3
  • 7
    • 0037071892 scopus 로고    scopus 로고
    • Coordinated interaction of neurogenesis and angiogenesis in the adult songbird brain
    • Louissaint, A., Jr., Rao, S., Leventhal, C., and Goldman, S.A. Coordinated interaction of neurogenesis and angiogenesis in the adult songbird brain. Neuron 34, 945-960 (2002).
    • (2002) Neuron , vol.34 , pp. 945-960
    • Louissaint Jr., A.1    Rao, S.2    Leventhal, C.3    Goldman, S.A.4
  • 9
    • 3242703082 scopus 로고    scopus 로고
    • Linear and nonlinear relationships between neuronal activity, oxygen metabolism, and hemodynamic responses
    • Sheth, S.A., Nemoto, M., Guiou, M.,Walker, M., Pouratian, N., and Toga, A.W. Linear and nonlinear relationships between neuronal activity, oxygen metabolism, and hemodynamic responses. Neuron 42, 347-355 (2004).
    • (2004) Neuron , vol.42 , pp. 347-355
    • Sheth, S.A.1    Nemoto, M.2    Guiou, M.3    Walker, M.4    Pouratian, N.5    Toga, A.W.6
  • 10
    • 0037131216 scopus 로고    scopus 로고
    • Shadows cast by retinal blood vessels mapped in primary visual cortex
    • Adams, D.L. and Horton, J.C. Shadows cast by retinal blood vessels mapped in primary visual cortex. Science 298, 572-576 (2002).
    • (2002) Science , vol.298 , pp. 572-576
    • Adams, D.L.1    Horton, J.C.2
  • 11
    • 84984763363 scopus 로고    scopus 로고
    • Mechanisms, challenges and opportunities in stroke
    • Lo, E.H., Dalkara, T., and Moskowitz, M.A. Mechanisms, challenges and opportunities in stroke. Nat. Rev. Neurosci. 4, 399-415 (2003).
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 399-415
    • Lo, E.H.1    Dalkara, T.2    Moskowitz, M.A.3
  • 12
    • 0035576934 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions in the blood-brain barrier
    • Huber, J.D., Egleton, R.D., and Davis, T.P. Molecular physiology and pathophysiology of tight junctions in the blood-brain barrier. Trends Neurosci. 24, 719-725 (2001).
    • (2001) Trends Neurosci. , vol.24 , pp. 719-725
    • Huber, J.D.1    Egleton, R.D.2    Davis, T.P.3
  • 13
    • 0036319335 scopus 로고    scopus 로고
    • Astrocyte-endothelial interactions and blood-brain barrier permeability
    • Abbott, N.J. Astrocyte-endothelial interactions and blood-brain barrier permeability. J. Anat. 200, 629-638 (2002).
    • (2002) J. Anat. , vol.200 , pp. 629-638
    • Abbott, N.J.1
  • 14
    • 0742321910 scopus 로고    scopus 로고
    • Triggers and mediators of hemorrhagic transformation in cerebral ischemia
    • Wang, X. and Lo, E.H. Triggers and mediators of hemorrhagic transformation in cerebral ischemia. Mol. Neurobiol. 28, 229-244 (2003).
    • (2003) Mol. Neurobiol. , vol.28 , pp. 229-244
    • Wang, X.1    Lo, E.H.2
  • 15
    • 0034989998 scopus 로고    scopus 로고
    • Crosstalk between components of the blood brain barrier and cells of the CNS in microglial activation in AIDS
    • Langford, D. and Masliah, E. Crosstalk between components of the blood brain barrier and cells of the CNS in microglial activation in AIDS. Brain Pathol. 11, 306-312 (2001).
    • (2001) Brain Pathol. , vol.11 , pp. 306-312
    • Langford, D.1    Masliah, E.2
  • 18
    • 0344961161 scopus 로고    scopus 로고
    • Blood-brain barrier disruption in multiple sclerosis
    • Minagar, A. and Alexander, J.S. Blood-brain barrier disruption in multiple sclerosis. Mult. Scler. 9, 540-549 (2003).
    • (2003) Mult. Scler. , vol.9 , pp. 540-549
    • Minagar, A.1    Alexander, J.S.2
  • 19
    • 0030560684 scopus 로고    scopus 로고
    • A quantitative spatial analysis of the blood-spinal cord barrier. I. Permeability changes after experimental spinal contusion injury
    • Popovich, P.G., Horner, P.J., Mullin, B.B., and Stokes, B.T. A quantitative spatial analysis of the blood-spinal cord barrier. I. Permeability changes after experimental spinal contusion injury. Exp. Neurol. 142, 258-275 (1996).
    • (1996) Exp. Neurol. , vol.142 , pp. 258-275
    • Popovich, P.G.1    Horner, P.J.2    Mullin, B.B.3    Stokes, B.T.4
  • 20
    • 0023067429 scopus 로고
    • Immunohistochemical demonstration of serum proteins in human cerebral gliomas
    • Seitz, R.J. and Wechsler, W: Immunohistochemical demonstration of serum proteins in human cerebral gliomas. Acta Neuropathol. (Berl.) 73, 145-152 (1987).
    • (1987) Acta Neuropathol. (Berl.) , vol.73 , pp. 145-152
    • Seitz, R.J.1    Wechsler, W.2
  • 21
    • 0034060928 scopus 로고    scopus 로고
    • Quantitative measurement of microvascular permeability in human brain tumors achieved using dynamic contrast-enhanced MR imaging: Correlation with histologic grade
    • Roberts, H.C., Roberts, T.P., Brasch, R.C., and Dillon, W.P. Quantitative measurement of microvascular permeability in human brain tumors achieved using dynamic contrast-enhanced MR imaging: Correlation with histologic grade. AJNR Am. J. Neuroradiol. 21, 891-899 (2000).
    • (2000) AJNR Am. J. Neuroradiol. , vol.21 , pp. 891-899
    • Roberts, H.C.1    Roberts, T.P.2    Brasch, R.C.3    Dillon, W.P.4
  • 22
    • 0037868085 scopus 로고    scopus 로고
    • Pathogenesis of bacterial meningitis: From bacteraemia to neuronal injury
    • Kim, K.S. Pathogenesis of bacterial meningitis: From bacteraemia to neuronal injury. Nat. Rev. Neurosci. 4, 376-385 (2003).
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 376-385
    • Kim, K.S.1
  • 23
    • 0141925659 scopus 로고    scopus 로고
    • Fibrinogen: Biochemistry, epidemiology and determinants
    • Kamath, S. and Lip, G.Y. Fibrinogen: Biochemistry, epidemiology and determinants. QJM 96, 711-729 (2003).
    • (2003) QJM , vol.96 , pp. 711-729
    • Kamath, S.1    Lip, G.Y.2
  • 24
    • 0032968080 scopus 로고    scopus 로고
    • Injury-induced gelatinase and thrombin-like activities in regenerating and nonregenerating nervous systems
    • Friedmann, I.,Faber-Elman, A., Yoles, E., and Schwartz, M. Injury-induced gelatinase and thrombin-like activities in regenerating and nonregenerating nervous systems. FASEB J. 13, 533-543 (1999).
    • (1999) FASEB J. , vol.13 , pp. 533-543
    • Friedmann, I.1    Faber-Elman, A.2    Yoles, E.3    Schwartz, M.4
  • 25
    • 0027278070 scopus 로고
    • Tissue factor contributes to microvascular defects after focal cerebral ischemia
    • Thomas, W.S., Mori, E., Copeland, B.R., Yu, J.Q., Morrissey, J.H., and del Zoppo, G.J. Tissue factor contributes to microvascular defects after focal cerebral ischemia. Stroke 24, 847-853 (1993).
    • (1993) Stroke , vol.24 , pp. 847-853
    • Thomas, W.S.1    Mori, E.2    Copeland, B.R.3    Yu, J.Q.4    Morrissey, J.H.5    del Zoppo, G.J.6
  • 26
    • 0036005958 scopus 로고    scopus 로고
    • Nervous system pathologies: The fibrin perspective
    • Akassoglou, K. and Strickland, S. Nervous system pathologies: The fibrin perspective. Biol. Chem. 383, 37-45 (2002).
    • (2002) Biol. Chem. , vol.383 , pp. 37-45
    • Akassoglou, K.1    Strickland, S.2
  • 27
    • 0034461642 scopus 로고    scopus 로고
    • Does inflammation contribute to thrombotic events?
    • Esmon, C.T. Does inflammation contribute to thrombotic events? Haemostasis 30, 34-40 (2000).
    • (2000) Haemostasis , vol.30 , pp. 34-40
    • Esmon, C.T.1
  • 29
    • 0022534483 scopus 로고
    • Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B
    • Senior, R.M., Skogen, W.F., Griffin, G.L., and Wilner, G.D. Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B. J. Clin. Invest. 77, 1014-1019 (1986).
    • (1986) J. Clin. Invest. , vol.77 , pp. 1014-1019
    • Senior, R.M.1    Skogen, W.F.2    Griffin, G.L.3    Wilner, G.D.4
  • 30
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • Spraggon, G., Everse, S.J., and Doolittle, R.F. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 389, 455-462 (1997).
    • (1997) Nature , vol.389 , pp. 455-462
    • Spraggon, G.1    Everse, S.J.2    Doolittle, R.F.3
  • 33
    • 0034687693 scopus 로고    scopus 로고
    • A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides
    • Yang, Z., Mochalkin, I., and Doolittle, R.F. A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides. Proc. Natl. Acad. Sci. U.S.A. 97, 14156-14161 (2000).
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14156-14161
    • Yang, Z.1    Mochalkin, I.2    Doolittle, R.F.3
  • 34
    • 0034969433 scopus 로고    scopus 로고
    • Elements of the fibrinolytic system
    • Lijnen, H.R. Elements of the fibrinolytic system. Ann. N.Y. Acad. Sci. 936, 226-236 (2001).
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 226-236
    • Lijnen, H.R.1
  • 35
    • 0034952378 scopus 로고    scopus 로고
    • Fibrin degradation products. A review of structures found in vitro and in vivo
    • Gaffney, P.J. Fibrin degradation products. A review of structures found in vitro and in vivo. Ann. N.Y. Acad. Sci. 936, 594-610 (2001).
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 594-610
    • Gaffney, P.J.1
  • 36
    • 0034969115 scopus 로고    scopus 로고
    • Fibrinogen and its degradation products as thrombotic risk factors
    • Lowe, G.D. and Rumley, A. Fibrinogen and its degradation products as thrombotic risk factors. Ann. N.Y. Acad. Sci. 936, 560-565 (2001).
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 560-565
    • Lowe, G.D.1    Rumley, A.2
  • 38
    • 0030584083 scopus 로고    scopus 로고
    • Loss of fibrinogen rescues mice from the pleiotropic effects of plasminogen deficiency
    • Bugge, T.H., Kombrinck, K.W., Flick, M.J., Daugherty, C.C., Danton, M.J., and Degen, J.L. Loss of fibrinogen rescues mice from the pleiotropic effects of plasminogen deficiency. Cell 87, 709-719 (1996).
    • (1996) Cell , vol.87 , pp. 709-719
    • Bugge, T.H.1    Kombrinck, K.W.2    Flick, M.J.3    Daugherty, C.C.4    Danton, M.J.5    Degen, J.L.6
  • 39
    • 0023915420 scopus 로고
    • The platelet membrane glycoprotein IIb-IIIa complex
    • Phillips, D.R., Charo, I.F., Parise, L.V., and Fitzgerald, L.A. The platelet membrane glycoprotein IIb-IIIa complex. Blood 71, 831-843 (1988).
    • (1988) Blood , vol.71 , pp. 831-843
    • Phillips, D.R.1    Charo, I.F.2    Parise, L.V.3    Fitzgerald, L.A.4
  • 40
    • 0034964396 scopus 로고    scopus 로고
    • Recognition of fibrinogen by leukocyte integrins
    • Ugarova, T.P. and Yakubenko, V.P. Recognition of fibrinogen by leukocyte integrins. Ann. N.Y. Acad. Sci. 936, 368-385 (2001).
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 368-385
    • Ugarova, T.P.1    Yakubenko, V.P.2
  • 41
    • 0034638830 scopus 로고    scopus 로고
    • 2 integrin clustering or activation in the control of apoptosis via regulation of Akt and ERK survival mechanisms
    • 2 integrin clustering or activation in the control of apoptosis via regulation of Akt and ERK survival mechanisms. J. Cell Biol. 151, 1305-1320 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 1305-1320
    • Whitlock, B.B.1    Gardai, S.2    Fadok, V.3    Bratton, D.4    Henson, P.M.5
  • 42
    • 0033129378 scopus 로고    scopus 로고
    • Transcriptional regulation of the interleukin-1β promoter via fibrinogen engagement of the CD18 integrin receptor
    • Perez, R.L., Ritzenthaler, J.D., and Roman, J. Transcriptional regulation of the interleukin-1β promoter via fibrinogen engagement of the CD18 integrin receptor. Am. J. Respir. Cell Mol. Biol. 20, 1059-1066 (1999).
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.20 , pp. 1059-1066
    • Perez, R.L.1    Ritzenthaler, J.D.2    Roman, J.3
  • 43
    • 0035164333 scopus 로고    scopus 로고
    • Analysis of the roles of ICAM-1 in neutrophil transmigration using a reconstituted mammalian cell expression model: Implication of ICAM-1 cytoplasmic domain and Rho-dependent signaling pathway
    • Sans, E., Delachanal, E., and Duperray, A. Analysis of the roles of ICAM-1 in neutrophil transmigration using a reconstituted mammalian cell expression model: Implication of ICAM-1 cytoplasmic domain and Rho-dependent signaling pathway. J. Immunol. 166, 544-551 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 544-551
    • Sans, E.1    Delachanal, E.2    Duperray, A.3
  • 44
    • 0036240189 scopus 로고    scopus 로고
    • Interactions of intercellular adhesion molecule-1 with fibrinogen
    • Tsakadze, N.L., Zhao, Z., and D'Souza, S.E. Interactions of intercellular adhesion molecule-1 with fibrinogen. Trends Cardiovasc. Med. 12, 101-108 (2002).
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 101-108
    • Tsakadze, N.L.1    Zhao, Z.2    D'Souza, S.E.3
  • 45
    • 0033865669 scopus 로고    scopus 로고
    • Fibrinogen interactions with ICAM-1 (CD54) regulate endothelial cell survival
    • Pluskota, E. and D'Souza, S.E. Fibrinogen interactions with ICAM-1 (CD54) regulate endothelial cell survival. Eur. J. Biochem. 267, 4693-4704 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4693-4704
    • Pluskota, E.1    D'Souza, S.E.2
  • 47
    • 0018185067 scopus 로고
    • Affinity of fibronectin to collagens of different genetic types and to fibrinogen
    • Engvall, E., Ruoslahti, E., and Miller, E.J. Affinity of fibronectin to collagens of different genetic types and to fibrinogen. J. Exp. Med. 147, 1584-1595 (1978).
    • (1978) J. Exp. Med. , vol.147 , pp. 1584-1595
    • Engvall, E.1    Ruoslahti, E.2    Miller, E.J.3
  • 48
    • 0018838451 scopus 로고
    • Fibroblast adhesion to fibrinogen and fibrin substrata: Requirement for cold-insoluble globulin (plasma fibronectin)
    • Grinnell, F., Feld, M. and Minter, D. Fibroblast adhesion to fibrinogen and fibrin substrata: Requirement for cold-insoluble globulin (plasma fibronectin). Cell 19, 517-525 (1980).
    • (1980) Cell , vol.19 , pp. 517-525
    • Grinnell, F.1    Feld, M.2    Minter, D.3
  • 49
    • 0023198290 scopus 로고
    • Quantitative measurement of plasma gelsolin and its incorporation into fibrin clots
    • Smith, D.B., Janmey, P.A., Herbert, T.J., and Lind, S.E. Quantitative measurement of plasma gelsolin and its incorporation into fibrin clots. J. Lab. Clin. Med. 110, 189-195 (1987).
    • (1987) J. Lab. Clin. Med. , vol.110 , pp. 189-195
    • Smith, D.B.1    Janmey, P.A.2    Herbert, T.J.3    Lind, S.E.4
  • 50
    • 0033569731 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein-3 binds fibrinogen and fibrin
    • Campbell, P.G., Durham, S.K., Hayes, J.D., Suwanichkul, A., and Powell, D.R. Insulin-like growth factor-binding protein-3 binds fibrinogen and fibrin. J. Biol. Chem. 274, 30215-30221 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30215-30221
    • Campbell, P.G.1    Durham, S.K.2    Hayes, J.D.3    Suwanichkul, A.4    Powell, D.R.5
  • 51
    • 0032571259 scopus 로고    scopus 로고
    • Binding of basic fibroblast growth factor to fibrinogen and fibrin
    • Sahni, A., Odrljin, T., and Francis, C.W. Binding of basic fibroblast growth factor to fibrinogen and fibrin. J. Biol. Chem. 273, 7554-7559 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 7554-7559
    • Sahni, A.1    Odrljin, T.2    Francis, C.W.3
  • 52
    • 0033591220 scopus 로고    scopus 로고
    • Potentiation of endothelial cell proliferation by fibrin(ogen)-bound fibroblast growth factor-2
    • Sahni, A., Sporn, L.A., and Francis, C.W. Potentiation of endothelial cell proliferation by fibrin(ogen)-bound fibroblast growth factor-2. J. Biol. Chem. 274, 14936-14941 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14936-14941
    • Sahni, A.1    Sporn, L.A.2    Francis, C.W.3
  • 53
    • 0034548802 scopus 로고    scopus 로고
    • Vascular endothelial growth factor binds to fibrinogen and fibrin and stimulates endothelial cell proliferation
    • Sahni, A. and Francis, C.W. Vascular endothelial growth factor binds to fibrinogen and fibrin and stimulates endothelial cell proliferation. Blood 96, 3772-3778 (2000).
    • (2000) Blood , vol.96 , pp. 3772-3778
    • Sahni, A.1    Francis, C.W.2
  • 54
    • 0035138368 scopus 로고    scopus 로고
    • Localization of protein kinase A and vitronectin in resting platelets and their translocation onto fibrin fibers during clot formation
    • Morgenstern, E., Gnad, U., Preissner, K.T., Dierichs, R., Belleli, A., Chestukhin, A., Schvartz, I., and Shaltiel, S. Localization of protein kinase A and vitronectin in resting platelets and their translocation onto fibrin fibers during clot formation. Eur. J. Cell Biol. 80, 87-98 (2001).
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 87-98
    • Morgenstern, E.1    Gnad, U.2    Preissner, K.T.3    Dierichs, R.4    Belleli, A.5    Chestukhin, A.6    Schvartz, I.7    Shaltiel, S.8
  • 56
    • 0033779403 scopus 로고    scopus 로고
    • A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance
    • Ringdahl, U., Svensson, H.G., Kotarsky, H., Gustafsson, M., Weineisen, M., and Sjobring, U. A role for the fibrinogen-binding regions of streptococcal M proteins in phagocytosis resistance. Mol. Microbiol. 37, 1318-1326 (2000).
    • (2000) Mol. Microbiol. , vol.37 , pp. 1318-1326
    • Ringdahl, U.1    Svensson, H.G.2    Kotarsky, H.3    Gustafsson, M.4    Weineisen, M.5    Sjobring, U.6
  • 57
    • 0034718896 scopus 로고    scopus 로고
    • Regenerating the damaged central nervous system
    • Horner, P.J. and Gage, F.H. Regenerating the damaged central nervous system. Nature 407, 963-970 (2000).
    • (2000) Nature , vol.407 , pp. 963-970
    • Horner, P.J.1    Gage, F.H.2
  • 58
    • 0742288565 scopus 로고    scopus 로고
    • Regeneration beyond the glial scar
    • Silver, J. and Miller, J.H. Regeneration beyond the glial scar. Nat. Rev. Neurosci. 5, 146-156 (2004).
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 146-156
    • Silver, J.1    Miller, J.H.2
  • 59
    • 0033200055 scopus 로고    scopus 로고
    • Schwann cells and their precursors emerge as major regulators of nerve development
    • Jessen, K.R. and Mirsky, R. Schwann cells and their precursors emerge as major regulators of nerve development. Trends Neurosci. 22, 402-410 (1999).
    • (1999) Trends Neurosci. , vol.22 , pp. 402-410
    • Jessen, K.R.1    Mirsky, R.2
  • 60
    • 0034465826 scopus 로고    scopus 로고
    • Developmental regulation in the Schwann cell lineage
    • Jessen, K.R. and Mirsky, R. Developmental regulation in the Schwann cell lineage. Adv. Exp. Med. Biol. 468, 3-12 (1999).
    • (1999) Adv. Exp. Med. Biol. , vol.468 , pp. 3-12
    • Jessen, K.R.1    Mirsky, R.2
  • 61
    • 0345599006 scopus 로고    scopus 로고
    • Laminin g1 is critical for Schwann cell differentiation, axon myelination, and regeneration in the peripheral nerve
    • Chen Z.L., and Strickland, S. Laminin g1 is critical for Schwann cell differentiation, axon myelination, and regeneration in the peripheral nerve. J. Cell Biol. 163, 889-899 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 889-899
    • Chen, Z.L.1    Strickland, S.2
  • 62
    • 0027968167 scopus 로고
    • Merosin promotes neurite growth and Schwann cell migration in vitro and nerve regeneration in vivo: Evidence using an antibody to merosin, ARM-1
    • Anton, E.S., Sandrock, A.W., Jr., and Matthew, W.D. Merosin promotes neurite growth and Schwann cell migration in vitro and nerve regeneration in vivo: Evidence using an antibody to merosin, ARM-1. Dev. Biol. 164, 133-146 (1994).
    • (1994) Dev. Biol. , vol.164 , pp. 133-146
    • Anton, E.S.1    Sandrock Jr., A.W.2    Matthew, W.D.3
  • 64
    • 18444368408 scopus 로고    scopus 로고
    • Conditional disruption of b1 integrin in Schwann cells impedes interactions with axons
    • Feltri, M.L., Porta, D.G., Previtali, S.C. et al. Conditional disruption of b1 integrin in Schwann cells impedes interactions with axons. J. Cell Biol. 156, 199-210 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 199-210
    • Feltri, M.L.1    Porta, D.G.2    Previtali, S.C.3
  • 65
    • 0034729210 scopus 로고    scopus 로고
    • Tissue plasminogen activator-mediated fibrinolysis protects against axonal degeneration and demyelination after sciatic nerve injury
    • Akassoglou, K., Kombrinck, K.W., Degen, J.L., and Strickland, S. Tissue plasminogen activator-mediated fibrinolysis protects against axonal degeneration and demyelination after sciatic nerve injury. J. Cell Biol. 149, 1157-1166 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 1157-1166
    • Akassoglou, K.1    Kombrinck, K.W.2    Degen, J.L.3    Strickland, S.4
  • 66
    • 0037075577 scopus 로고    scopus 로고
    • Fibrin inhibits peripheral nerve regeneration by arresting Schwann cell differentiation
    • Akassoglou, K., Yu, W.-M., Akpinar, P., and Strickland, S. Fibrin inhibits peripheral nerve regeneration by arresting Schwann cell differentiation. Neuron 33, 861-875 (2002).
    • (2002) Neuron , vol.33 , pp. 861-875
    • Akassoglou, K.1    Yu, W.-M.2    Akpinar, P.3    Strickland, S.4
  • 67
    • 0025284761 scopus 로고
    • A plasminogen activator is induced during goldfish optic nerve regeneration
    • Salles, F.J., Schechter, N., and Strickland, S. A plasminogen activator is induced during goldfish optic nerve regeneration. EMBO J. 9, 2471-2477 (1990).
    • (1990) EMBO J. , vol.9 , pp. 2471-2477
    • Salles, F.J.1    Schechter, N.2    Strickland, S.3
  • 68
    • 0035876289 scopus 로고    scopus 로고
    • Mice lacking tPA, uPA, or plasminogen genes showed delayed functional recovery after sciatic nerve crush
    • Siconolfi, L.B. and Seeds, N.W. Mice lacking tPA, uPA, or plasminogen genes showed delayed functional recovery after sciatic nerve crush. J. Neurosci. 21, 4348-4355 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 4348-4355
    • Siconolfi, L.B.1    Seeds, N.W.2
  • 70
    • 0037422271 scopus 로고    scopus 로고
    • Fibrin is a regulator of Schwann cell migration after sciatic nerve injury in mice
    • Akassoglou, K., Akpinar, P., Murray, S., and Strickland, S. Fibrin is a regulator of Schwann cell migration after sciatic nerve injury in mice. Neurosci. Lett. 338, 185-188 (2003).
    • (2003) Neurosci. Lett. , vol.338 , pp. 185-188
    • Akassoglou, K.1    Akpinar, P.2    Murray, S.3    Strickland, S.4
  • 71
    • 0029916769 scopus 로고    scopus 로고
    • Making of a Schwann
    • Kioussi, C. and Gruss, P. Making of a Schwann. Trends Genet. 12, 84-86 (1996).
    • (1996) Trends Genet. , vol.12 , pp. 84-86
    • Kioussi, C.1    Gruss, P.2
  • 72
    • 0033998677 scopus 로고    scopus 로고
    • Schwann cell extracellular matrix molecules and their receptors
    • Chernousov, M.A. and Carey, D.J. Schwann cell extracellular matrix molecules and their receptors. Histol. Histopathol. 15, 593-601 (2000).
    • (2000) Histol. Histopathol. , vol.15 , pp. 593-601
    • Chernousov, M.A.1    Carey, D.J.2
  • 74
    • 0344441399 scopus 로고    scopus 로고
    • 8 integrin is a Schwann cell receptor for fibrin
    • 8 integrin is a Schwann cell receptor for fibrin. Exp. Cell Res. 291, 514-524 (2003).
    • (2003) Exp. Cell Res. , vol.291 , pp. 514-524
    • Chernousov, M.A.1    Carey, D.J.2
  • 75
    • 0035096330 scopus 로고    scopus 로고
    • Heterogeneity of multiple sclerosis pathogenesis: Implications for diagnosis and therapy
    • Lassmann, H., Bruck, W., and Lucchinetti, C. Heterogeneity of multiple sclerosis pathogenesis: Implications for diagnosis and therapy. Trends Mol. Med. 7, 115-121. (2001).
    • (2001) Trends Mol. Med. , vol.7 , pp. 115-121
    • Lassmann, H.1    Bruck, W.2    Lucchinetti, C.3
  • 76
    • 0024990661 scopus 로고
    • Breakdown of the blood-brain barrier precedes symptoms and other MRI signs of new lesions in multiple sclerosis. Pathogenetic and clinical implications
    • Kermode, A.G., Thompson, A.J., Tofts, P., MacManus, D.G., Kendall, B.E., Kingsley, D.P., Moseley, I.F., Rudge, P., and McDonald, W.I. Breakdown of the blood-brain barrier precedes symptoms and other MRI signs of new lesions in multiple sclerosis. Pathogenetic and clinical implications. Brain 113, 1477-1489 (1990).
    • (1990) Brain , vol.113 , pp. 1477-1489
    • Kermode, A.G.1    Thompson, A.J.2    Tofts, P.3    MacManus, D.G.4    Kendall, B.E.5    Kingsley, D.P.6    Moseley, I.F.7    Rudge, P.8    McDonald, W.I.9
  • 77
    • 0000138505 scopus 로고
    • Histologisches detail zu der grauen degeneration von gehirn und ruckenmark
    • Rindfleisch, E. Histologisches detail zu der grauen degeneration von gehirn und ruckenmark. Archives of Pathological Anatomy and Physiology 26, 474-483 (1863).
    • (1863) Archives of Pathological Anatomy and Physiology , vol.26 , pp. 474-483
    • Rindfleisch, E.1
  • 78
    • 0029116712 scopus 로고
    • Evidence of persistent blood-brain barrier abnormalities in chronic- progressive multiple sclerosis
    • Claudio, L., Raine, C.S., and Brosnan, C.F. Evidence of persistent blood-brain barrier abnormalities in chronic- progressive multiple sclerosis. Acta Neuropathol. 90, 228-238 (1995).
    • (1995) Acta Neuropathol. , vol.90 , pp. 228-238
    • Claudio, L.1    Raine, C.S.2    Brosnan, C.F.3
  • 79
    • 0028330910 scopus 로고
    • Immunohistochemical study of vascular injury in acute multiple sclerosis
    • Wakefield, A.J., More, L.J., Difford, J., and McLaughlin, J.E. Immunohistochemical study of vascular injury in acute multiple sclerosis. J. Clin. Pathol. 47, 129-133 (1994).
    • (1994) J. Clin. Pathol. , vol.47 , pp. 129-133
    • Wakefield, A.J.1    More, L.J.2    Difford, J.3    McLaughlin, J.E.4
  • 80
    • 1842367972 scopus 로고    scopus 로고
    • The application of multifactorial cluster analysis in the staging of plaques in early multiple sclerosis. Identification and characterization of the primary demyelinating lesion
    • Gay, F.W., Drye, T.J., Dick, G.W., and Esiri, M.M. The application of multifactorial cluster analysis in the staging of plaques in early multiple sclerosis. Identification and characterization of the primary demyelinating lesion. Brain 120, 1461-1483 (1997).
    • (1997) Brain , vol.120 , pp. 1461-1483
    • Gay, F.W.1    Drye, T.J.2    Dick, G.W.3    Esiri, M.M.4
  • 81
    • 0034774402 scopus 로고    scopus 로고
    • Plasminogen activators in multiple sclerosis lesions: Implications for the inflammatory response and axonal damage
    • Gveric, D., Hanemaaijer, R., Newcombe, J., van Lent, N.A., Sier, C.F., and Cuzner, M.L. Plasminogen activators in multiple sclerosis lesions: Implications for the inflammatory response and axonal damage. Brain 124, 1978-1988 (2001).
    • (2001) Brain , vol.124 , pp. 1978-1988
    • Gveric, D.1    Hanemaaijer, R.2    Newcombe, J.3    van Lent, N.A.4    Sier, C.F.5    Cuzner, M.L.6
  • 82
    • 0141926694 scopus 로고    scopus 로고
    • Tight junctional abnormality in multiple sclerosis white matter affects all calibres of vessel and is associated with blood-brain barrier leakage and active demyelination
    • Kirk, J., Plumb, J., Mirakhur, M., and McQuaid, S. Tight junctional abnormality in multiple sclerosis white matter affects all calibres of vessel and is associated with blood-brain barrier leakage and active demyelination. J. Pathol. 201, 319-327 (2003).
    • (2003) J. Pathol. , vol.201 , pp. 319-327
    • Kirk, J.1    Plumb, J.2    Mirakhur, M.3    McQuaid, S.4
  • 83
    • 0034284153 scopus 로고    scopus 로고
    • Serine proteases and brain damage - Is there a link?
    • Gingrich, M.B. and Traynelis, S.F. Serine proteases and brain damage - is there a link? Trends Neurosci. 23, 399-407 (2000).
    • (2000) Trends Neurosci. , vol.23 , pp. 399-407
    • Gingrich, M.B.1    Traynelis, S.F.2
  • 84
    • 0036549939 scopus 로고    scopus 로고
    • Tissue plasminogen activator as a modulator of neuronal survival and function
    • Tsirka, S.E. Tissue plasminogen activator as a modulator of neuronal survival and function. Biochem. Soc. Trans. 3, 222-225 (2002).
    • (2002) Biochem. Soc. Trans. , vol.3 , pp. 222-225
    • Tsirka, S.E.1
  • 85
    • 0036081376 scopus 로고    scopus 로고
    • Tissue plasminogen activator and seizures: A clot-buster's secret life
    • Pawlak, R. and Strickland, S. Tissue plasminogen activator and seizures: A clot-buster's secret life. J. Clin. Invest. 109, 1529-1531 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 1529-1531
    • Pawlak, R.1    Strickland, S.2
  • 86
    • 0642279043 scopus 로고    scopus 로고
    • The possible role of tissue-type plasminogen activator (tPA) and tPA blockers in the pathogenesis and treatment of Alzheimer's disease
    • Melchor, J.P., Pawlak, R., Chen, Z., and Strickland, S. The possible role of tissue-type plasminogen activator (tPA) and tPA blockers in the pathogenesis and treatment of Alzheimer's disease. J. Mol. Neurosci. 20, 287-289 (2003).
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 287-289
    • Melchor, J.P.1    Pawlak, R.2    Chen, Z.3    Strickland, S.4
  • 88
    • 0842289222 scopus 로고    scopus 로고
    • tPA and proteolysis in the neurovascular unit
    • Lo, E.H., Broderick, J.P. and Moskowitz, M.A. tPA and proteolysis in the neurovascular unit. Stroke 35, 354-356 (2004).
    • (2004) Stroke , vol.35 , pp. 354-356
    • Lo, E.H.1    Broderick, J.P.2    Moskowitz, M.A.3
  • 89
    • 0030055419 scopus 로고    scopus 로고
    • Cerebrospinal fluid activity of tissue plasminogen activator in patients with neurological diseases
    • Akenami, F.O., Siren, V., Koskiniemi, M., Siimes, M.A., Teravainen, H., and Vaheri, A. Cerebrospinal fluid activity of tissue plasminogen activator in patients with neurological diseases. J. Clin. Pathol. 49, 577-580 (1996).
    • (1996) J. Clin. Pathol. , vol.49 , pp. 577-580
    • Akenami, F.O.1    Siren, V.2    Koskiniemi, M.3    Siimes, M.A.4    Teravainen, H.5    Vaheri, A.6
  • 90
    • 0036545522 scopus 로고    scopus 로고
    • Tissue plasminogen activator as a key effector in neurobiology and neuropathology
    • Teesalu, T., Kulla, A., Asser, T., Koskiniemi, M., and Vaheri, A. Tissue plasminogen activator as a key effector in neurobiology and neuropathology. Biochem. Soc. Trans. 30, 183-189 (2002).
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 183-189
    • Teesalu, T.1    Kulla, A.2    Asser, T.3    Koskiniemi, M.4    Vaheri, A.5
  • 91
    • 0033137097 scopus 로고    scopus 로고
    • Tissue plasminogen activator gene expression in multiple sclerosis brain tissue
    • Akenami, F.O., Siren, V., Wessman, M., Koskiniemi, M., and Vaheri, A. Tissue plasminogen activator gene expression in multiple sclerosis brain tissue. J. Neurol. Sci. 165, 71-76 (1999).
    • (1999) J. Neurol. Sci. , vol.165 , pp. 71-76
    • Akenami, F.O.1    Siren, V.2    Wessman, M.3    Koskiniemi, M.4    Vaheri, A.5
  • 92
    • 0038157213 scopus 로고    scopus 로고
    • Impaired fibrinolysis in multiple sclerosis: A role for tissue plasminogen activator inhibitors
    • Gveric, D., Herrera, B., Petzold, A., Lawrence, D.A., and Cuzner, M.L. Impaired fibrinolysis in multiple sclerosis: A role for tissue plasminogen activator inhibitors. Brain. 126, 1-9 (2003).
    • (2003) Brain , vol.126 , pp. 1-9
    • Gveric, D.1    Herrera, B.2    Petzold, A.3    Lawrence, D.A.4    Cuzner, M.L.5
  • 93
    • 0033249811 scopus 로고    scopus 로고
    • Elevated plasma level of plasminogen activator inhibitor-1 (PAI-1) in patients with relapsing-remitting multiple sclerosis
    • Onodera, H., Nakashima, I., Fujihara, K., Nagata, T., and Itoyama, Y. Elevated plasma level of plasminogen activator inhibitor-1 (PAI-1) in patients with relapsing-remitting multiple sclerosis. Tohoku J. Exp. Med. 189, 259-265 (1999).
    • (1999) Tohoku J. Exp. Med. , vol.189 , pp. 259-265
    • Onodera, H.1    Nakashima, I.2    Fujihara, K.3    Nagata, T.4    Itoyama, Y.5
  • 94
    • 0031050864 scopus 로고    scopus 로고
    • Cerebrospinal fluid plasminogen activator inhibitor-1 in patients with neurological disease
    • Akenami, F.O., Koskiniemi, M., Farkkila, M., and Vaheri, A. Cerebrospinal fluid plasminogen activator inhibitor-1 in patients with neurological disease. J Clin. Pathol. 50, 157-160 (1997).
    • (1997) J. Clin. Pathol. , vol.50 , pp. 157-160
    • Akenami, F.O.1    Koskiniemi, M.2    Farkkila, M.3    Vaheri, A.4
  • 95
    • 0023874876 scopus 로고
    • The immunopathology of acute experimental allergic encephalomyelitis. V. A light microscopic and ultrastructural immunohistochemical analysis of fibronectin and fibrinogen
    • Sobel, R.A., Schneeberger, E.E., and Colvin, R.B. The immunopathology of acute experimental allergic encephalomyelitis. V. A light microscopic and ultrastructural immunohistochemical analysis of fibronectin and fibrinogen. Am. J. Pathol. 131, 547-558 (1988).
    • (1988) Am. J. Pathol. , vol.131 , pp. 547-558
    • Sobel, R.A.1    Schneeberger, E.E.2    Colvin, R.B.3
  • 96
    • 0019421942 scopus 로고
    • Experimental allergic encephalomyelitis. Exudate and cellular infiltrates in the spinal cord of Lewis rats
    • Ackermann, H.P., Ulrich, J., and Heitz, P.U. Experimental allergic encephalomyelitis. Exudate and cellular infiltrates in the spinal cord of Lewis rats. Acta Neuropathol. (Berl) 54, 149-152 (1981).
    • (1981) Acta Neuropathol. (Berl) , vol.54 , pp. 149-152
    • Ackermann, H.P.1    Ulrich, J.2    Heitz, P.U.3
  • 97
    • 0018976135 scopus 로고
    • Neuropathology of experimental allergic encephalomyelitis in inbred strains of mice
    • Raine, C.S., Barnett, L.B., Brown, A., Behar, T., and McFarlin, D.E. Neuropathology of experimental allergic encephalomyelitis in inbred strains of mice. Lab. Invest. 43, 150-157 (1980).
    • (1980) Lab. Invest. , vol.43 , pp. 150-157
    • Raine, C.S.1    Barnett, L.B.2    Brown, A.3    Behar, T.4    McFarlin, D.E.5
  • 98
    • 0017106754 scopus 로고
    • Experimental allergic encephalomyelitis: Role of fibrin deposition in immunopathogenesis of inflammation in rats
    • Paterson, P.Y. Experimental allergic encephalomyelitis: role of fibrin deposition in immunopathogenesis of inflammation in rats. Fed. Proc. 35, 2428-2434 (1976).
    • (1976) Fed. Proc. , vol.35 , pp. 2428-2434
    • Paterson, P.Y.1
  • 99
    • 0030561019 scopus 로고    scopus 로고
    • Suppression of cell-transferred experimental autoimmune encephalomyelitis in defibrinated Lewis rats
    • Inoue, A., Koh, C.S., Shimada, K., Yanagisawa, N., and Yoshimura, K. Suppression of cell-transferred experimental autoimmune encephalomyelitis in defibrinated Lewis rats. J. Neuroimmunol. 71, 131-137 (1996).
    • (1996) J. Neuroimmunol. , vol.71 , pp. 131-137
    • Inoue, A.1    Koh, C.S.2    Shimada, K.3    Yanagisawa, N.4    Yoshimura, K.5
  • 100
    • 0035184313 scopus 로고    scopus 로고
    • Coordinated induction of extracellular proteolysis systems during experimental autoimmune encephalomyelitis in mice
    • Teesalu, T., Hinkkanen, A.E. and Vaheri, A. Coordinated induction of extracellular proteolysis systems during experimental autoimmune encephalomyelitis in mice. Am. J. Pathol. 159, 2227-2237 (2001).
    • (2001) Am. J. Pathol. , vol.159 , pp. 2227-2237
    • Teesalu, T.1    Hinkkanen, A.E.2    Vaheri, A.3
  • 101
    • 0037115099 scopus 로고    scopus 로고
    • Involvement of tissue plasminogen activator in onset and effector phases of experimental allergic encephalomyelitis
    • Lu, W., Bhasin, M., and Tsirka, S.E. Involvement of tissue plasminogen activator in onset and effector phases of experimental allergic encephalomyelitis. J. Neurosci. 22, 10781-10789 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 10781-10789
    • Lu, W.1    Bhasin, M.2    Tsirka, S.E.3
  • 102
    • 0019997718 scopus 로고
    • Observations on the effects of protease inhibitors on the suppression of experimental allergic encephalomyelitis
    • Smith, M.E. and L.A. Amaducci, Observations on the effects of protease inhibitors on the suppression of experimental allergic encephalomyelitis. Neurochem. Res. 7, 541-554 (1982).
    • (1982) Neurochem. Res. , vol.7 , pp. 541-554
    • Smith, M.E.1    Amaducci, L.A.2
  • 103
    • 0018879480 scopus 로고
    • Proteinase inhibitors suppress the development of experimental allergic encephalomyelitis
    • Brosnan, C.F., Cammer, W., Norton, W.T., and Bloom, B.R. Proteinase inhibitors suppress the development of experimental allergic encephalomyelitis. Nature 285, 235-237 (1980).
    • (1980) Nature , vol.285 , pp. 235-237
    • Brosnan, C.F.1    Cammer, W.2    Norton, W.T.3    Bloom, B.R.4
  • 104
    • 0025332729 scopus 로고
    • Neurovascular fibrinolytic activity in normal Lewis rats and rats with cell-transferred experimental allergic encephalomyelitis
    • Koh, C.S., Kwaan, H.C., and Paterson, P.Y. Neurovascular fibrinolytic activity in normal Lewis rats and rats with cell-transferred experimental allergic encephalomyelitis. J. Neuroimmunol. 28, 189-200 (1990).
    • (1990) J. Neuroimmunol. , vol.28 , pp. 189-200
    • Koh, C.S.1    Kwaan, H.C.2    Paterson, P.Y.3
  • 105
    • 0022177307 scopus 로고
    • The clotting system: Gatekeeper of cerebrovascular permeability and monitor of clinical manifestations of neuroautoimmune disease
    • Paterson, P.Y., Gausas, J., Koh, C.S., and Kwaan, H.C. The clotting system: Gatekeeper of cerebrovascular permeability and monitor of clinical manifestations of neuroautoimmune disease. Trans. Am. Clin. Climatol. Assoc. 97, 149-157 (1985).
    • (1985) Trans. Am. Clin. Climatol. Assoc. , vol.97 , pp. 149-157
    • Paterson, P.Y.1    Gausas, J.2    Koh, C.S.3    Kwaan, H.C.4
  • 106
    • 0023157207 scopus 로고
    • Role of the clotting system in the pathogenesis of neuroimmunologic disease
    • Paterson, P.Y., Koh, C.S., and Kwaan, H.C. Role of the clotting system in the pathogenesis of neuroimmunologic disease. Fed. Proc. 46, 91-96 (1987).
    • (1987) Fed. Proc. , vol.46 , pp. 91-96
    • Paterson, P.Y.1    Koh, C.S.2    Kwaan, H.C.3
  • 107
    • 3242678753 scopus 로고
    • Role of the clotting-fibrinolysis system in the pathogenesis of experimental allergic encephalomyelitis
    • Koh, C. Role of the clotting-fibrinolysis system in the pathogenesis of experimental allergic encephalomyelitis in Neuroimmunological Diseases(A. Igata ed) pp 169-174 (1988).
    • (1988) Neuroimmunological Diseases(A. Igata Ed) , pp. 169-174
    • Koh, C.1
  • 108
    • 0019801232 scopus 로고
    • Fibrinolytic activity of plaques and white matter in multiple sclerosis
    • Hirsch, H.E., Blanco, C.E., and Parks, M.E. Fibrinolytic activity of plaques and white matter in multiple sclerosis. J. Neuropathol. Exp. Neurol. 40, 271-280 (1981).
    • (1981) J. Neuropathol. Exp. Neurol. , vol.40 , pp. 271-280
    • Hirsch, H.E.1    Blanco, C.E.2    Parks, M.E.3
  • 109
    • 0035128996 scopus 로고    scopus 로고
    • Genetic models for CNS inflammation
    • Owens, T., Wekerle, H., and Antel, J. Genetic models for CNS inflammation. Nat. Med. 7, 161-166 (2001).
    • (2001) Nat. Med. , vol.7 , pp. 161-166
    • Owens, T.1    Wekerle, H.2    Antel, J.3
  • 110
    • 0034652416 scopus 로고    scopus 로고
    • Brain-immune connection: Immunoregulatory properties of CNS-resident cells
    • Becher, B., Prat, A., and Antel, J.P. Brain-immune connection: immunoregulatory properties of CNS-resident cells. Glia 29, 293-304 (2000).
    • (2000) Glia , vol.29 , pp. 293-304
    • Becher, B.1    Prat, A.2    Antel, J.P.3
  • 111
    • 0032722822 scopus 로고    scopus 로고
    • Multiple sclerosis and central nervous system demyelination
    • Pouly, S. and Antel, J.P. Multiple sclerosis and central nervous system demyelination. J. Autoimmun. 13, 297-306 (1999).
    • (1999) J. Autoimmun. , vol.13 , pp. 297-306
    • Pouly, S.1    Antel, J.P.2
  • 112
    • 0031659763 scopus 로고    scopus 로고
    • Oligodendrocyte apoptosis and primary demyelination induced by local TNF/p55TNF receptor signaling in the central nervous system of transgenic mice: Models for multiple sclerosis with primary oligodendrogliopathy
    • Akassoglou, K., Bauer, J., Kassiotis, G., Pasparakis, M., Lassmann, H., Kollias, G., and Probert, L. Oligodendrocyte apoptosis and primary demyelination induced by local TNF/p55TNF receptor signaling in the central nervous system of transgenic mice: Models for multiple sclerosis with primary oligodendrogliopathy. Am. J. Pathol. 153, 801-813 (1998).
    • (1998) Am. J. Pathol. , vol.153 , pp. 801-813
    • Akassoglou, K.1    Bauer, J.2    Kassiotis, G.3    Pasparakis, M.4    Lassmann, H.5    Kollias, G.6    Probert, L.7
  • 113
    • 0033775139 scopus 로고    scopus 로고
    • TNFR1 signalling is critical for the development of demyelination and the limitation of T-cell responses during immune-mediated CNS disease
    • Probert, L., Eugster, H.P., Akassoglou, K., Bauer, J., Frei, K., Lassmann, H., and Fontana, A. TNFR1 signalling is critical for the development of demyelination and the limitation of T-cell responses during immune-mediated CNS disease. Brain 123, 2005-2019 (2000).
    • (2000) Brain , vol.123 , pp. 2005-2019
    • Probert, L.1    Eugster, H.P.2    Akassoglou, K.3    Bauer, J.4    Frei, K.5    Lassmann, H.6    Fontana, A.7
  • 114
    • 0030056764 scopus 로고    scopus 로고
    • Distinct patterns of multiple sclerosis pathology indicates heterogeneity on pathogenesis
    • Lucchinetti, C.F., Bruck, W., Rodriguez, M., and Lassmann, H. Distinct patterns of multiple sclerosis pathology indicates heterogeneity on pathogenesis. Brain Pathol. 6, 259-274 (1996).
    • (1996) Brain Pathol. , vol.6 , pp. 259-274
    • Lucchinetti, C.F.1    Bruck, W.2    Rodriguez, M.3    Lassmann, H.4
  • 115
    • 1642281535 scopus 로고    scopus 로고
    • Relapsing and remitting multiple sclerosis: Pathology of the newly forming lesion
    • Barnett, M.H. and Prineas, J.W. Relapsing and remitting multiple sclerosis: pathology of the newly forming lesion. Ann. Neurol. 55, 458-468 (2004).
    • (2004) Ann. Neurol. , vol.55 , pp. 458-468
    • Barnett, M.H.1    Prineas, J.W.2
  • 117
    • 0035148983 scopus 로고    scopus 로고
    • Glial expression of tumor necrosis factor in transgenic animals: How do these models reflect the "normal situation"?
    • Probert, L. and Akassoglou, K. Glial expression of tumor necrosis factor in transgenic animals: How do these models reflect the "normal situation"? Glia 36, 212-219 (2001).
    • (2001) Glia , vol.36 , pp. 212-219
    • Probert, L.1    Akassoglou, K.2
  • 118
    • 2342570412 scopus 로고    scopus 로고
    • Fibrin depletion decreases inflammation and delays the onset of demyelination in a tumor necrosis factor transgenic mouse model for multiple sclerosis
    • Akassoglou, K., Adams, R.A., Bauer, J., Mercado, P., Tseveleki, V., Lassmann, H., Probert, L., and Strickland, S. Fibrin depletion decreases inflammation and delays the onset of demyelination in a tumor necrosis factor transgenic mouse model for multiple sclerosis. Proc. Natl. Acad. Sci. U S A 101, 6698-6703 (2004).
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6698-6703
    • Akassoglou, K.1    Adams, R.A.2    Bauer, J.3    Mercado, P.4    Tseveleki, V.5    Lassmann, H.6    Probert, L.7    Strickland, S.8
  • 119
    • 0342906187 scopus 로고    scopus 로고
    • Heterogeneity of multiple sclerosis lesions: Implications for the pathogenesis of demyelination
    • Lucchinetti, C., Bruck, W., Parisi, J., Scheithauer, B., Rodriguez, M., and Lassmann, H. Heterogeneity of multiple sclerosis lesions: Implications for the pathogenesis of demyelination. Ann. Neurol. 47, 707-717 (2000).
    • (2000) Ann. Neurol. , vol.47 , pp. 707-717
    • Lucchinetti, C.1    Bruck, W.2    Parisi, J.3    Scheithauer, B.4    Rodriguez, M.5    Lassmann, H.6
  • 120
    • 0032726065 scopus 로고    scopus 로고
    • Regulation of leukocyte-endothelium interaction by fibrinogen
    • Altieri, D.C. Regulation of leukocyte-endothelium interaction by fibrinogen. Thromb. Haemost. 82, 781-786 (1999).
    • (1999) Thromb. Haemost. , vol.82 , pp. 781-786
    • Altieri, D.C.1
  • 121
    • 0028814602 scopus 로고
    • Fibrin enhances the expression of IL-1 beta by human peripheral blood mononuclear cells. Implications in pulmonary inflammation
    • Perez, R.L. and Roman, J. Fibrin enhances the expression of IL-1 beta by human peripheral blood mononuclear cells. Implications in pulmonary inflammation. J. Immunol. 154, 1879-1887 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 1879-1887
    • Perez, R.L.1    Roman, J.2
  • 122
    • 0027212363 scopus 로고
    • Integrin regulation of leukocyte inflammatory functions. CD11b/CD18 enhancement of the tumor necrosis factor-alpha responses of monocytes
    • Fan, S.T and Edgington, T.S. Integrin regulation of leukocyte inflammatory functions. CD11b/CD18 enhancement of the tumor necrosis factor-alpha responses of monocytes. J. Immunol. 150, 2972-2980 (1993).
    • (1993) J. Immunol. , vol.150 , pp. 2972-2980
    • Fan, S.T.1    Edgington, T.S.2
  • 123
    • 0035451118 scopus 로고    scopus 로고
    • Fibrinogen stimulates macrophage chemokine secretion through toll-like receptor 4
    • Smiley, S.T, King, J.A., and Hancock, W.W. Fibrinogen stimulates macrophage chemokine secretion through toll-like receptor 4. J. Immunol. 167, 2887-2894 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 2887-2894
    • Smiley, S.T.1    King, J.A.2    Hancock, W.W.3
  • 124
    • 0041589180 scopus 로고    scopus 로고
    • Neuropathology of multiple sclerosis-new concepts
    • Kornek, B. and Lassmann, H. Neuropathology of multiple sclerosis-new concepts. Brain Res. Bull. 61, 321-326 (2003).
    • (2003) Brain Res. Bull. , vol.61 , pp. 321-326
    • Kornek, B.1    Lassmann, H.2
  • 125
    • 0027363435 scopus 로고
    • Neurovascular permeability and fibrin deposition in the central neuraxis of Lewis rats with cell-transferred experimental allergic encephalomyelitis in relationship to clinical and histopathological features of the disease
    • Koh, C.S., Gausas, J., and Paterson, P.Y. Neurovascular permeability and fibrin deposition in the central neuraxis of Lewis rats with cell-transferred experimental allergic encephalomyelitis in relationship to clinical and histopathological features of the disease. J. Neuroimmunol. 47, 141-145 (1993).
    • (1993) J. Neuroimmunol. , vol.47 , pp. 141-145
    • Koh, C.S.1    Gausas, J.2    Paterson, P.Y.3
  • 126
    • 0025726977 scopus 로고
    • Proteins of the complement system and acute phase reactants in sera of patients with spinal cord injury
    • Rebhun, J., Madorsky, J.G., and Glovsky, M.M. Proteins of the complement system and acute phase reactants in sera of patients with spinal cord injury. Ann. Allergy 66, 335-338 (1991).
    • (1991) Ann. Allergy , vol.66 , pp. 335-338
    • Rebhun, J.1    Madorsky, J.G.2    Glovsky, M.M.3
  • 127
    • 0034030862 scopus 로고    scopus 로고
    • Sniffing out new approaches to spinal cord repair
    • Raisman, G. Sniffing out new approaches to spinal cord repair. Nat. Med. 6, 382-383 (2000).
    • (2000) Nat. Med. , vol.6 , pp. 382-383
    • Raisman, G.1
  • 128
    • 0037263651 scopus 로고    scopus 로고
    • Decreased neural damage after spinal cord injury in tPA-deficient mice
    • Abe, Y., Nakamura, H., Yoshino, O., Oya, T., and Kimura, T. Decreased neural damage after spinal cord injury in tPA-deficient mice. J. Neurotrauma 20, 43-57 (2003).
    • (2003) J. Neurotrauma , vol.20 , pp. 43-57
    • Abe, Y.1    Nakamura, H.2    Yoshino, O.3    Oya, T.4    Kimura, T.5
  • 129
    • 0031045064 scopus 로고    scopus 로고
    • Endothelial fibrinolytic reactivity and the risk of deep venous thrombosis after spinal cord injury
    • Boudaoud, L., Roussi, J., Lortat-Jacob, S., Bussel, B., Dizien, O., and Drouet, L. Endothelial fibrinolytic reactivity and the risk of deep venous thrombosis after spinal cord injury. Spinal Cord 35, 151-157 (1997).
    • (1997) Spinal Cord , vol.35 , pp. 151-157
    • Boudaoud, L.1    Roussi, J.2    Lortat-Jacob, S.3    Bussel, B.4    Dizien, O.5    Drouet, L.6
  • 130
    • 0347364820 scopus 로고    scopus 로고
    • Diagnosis, prevalence, and management of thromboembolism in patients with spinal cord injury
    • Green, D. Diagnosis, prevalence, and management of thromboembolism in patients with spinal cord injury. J. Spinal Cord. Med. 26, 329-334 (2003).
    • (2003) J. Spinal Cord. Med. , vol.26 , pp. 329-334
    • Green, D.1
  • 131
    • 2342614850 scopus 로고    scopus 로고
    • Neurovascular regulation in the normal brain and in Alzheimer's disease
    • Iadecola, C. Neurovascular regulation in the normal brain and in Alzheimer's disease. Nat. Rev. Neurosci. 5, 347-360 (2004).
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 347-360
    • Iadecola, C.1
  • 132
    • 0033391684 scopus 로고    scopus 로고
    • The blood-brain barrier and cerebrovascular pathology in Alzheimer's disease
    • Kalaria, R.N. The blood-brain barrier and cerebrovascular pathology in Alzheimer's disease. Ann. N. Y. Acad. Sci. 893, 113-125 (1999).
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 113-125
    • Kalaria, R.N.1
  • 133
    • 0029670094 scopus 로고    scopus 로고
    • Beta-Amyloid-mediated vasoactivity and vascular endothelial damage
    • Thomas, T., Thomas, G., McLendon, C., Sutton, T., and Mullan, M. beta-Amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380, 168-171 (1996).
    • (1996) Nature , vol.380 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 134
    • 0029824524 scopus 로고    scopus 로고
    • Modulation of fibrin assembly and polymerization by the β-amyloid of Alzheimer's disease
    • Merkle, D.L., Cheng, C.H., Castellino, F.J., and Chibber, B.A. Modulation of fibrin assembly and polymerization by the β -amyloid of Alzheimer's disease. Blood Coagul. Fibrinolysis, 7, 650-658 (1996).
    • (1996) Blood Coagul. Fibrinolysis , vol.7 , pp. 650-658
    • Merkle, D.L.1    Cheng, C.H.2    Castellino, F.J.3    Chibber, B.A.4
  • 136
    • 0141641077 scopus 로고    scopus 로고
    • The tissue plasminogen activator-plasminogen proteolytic cascade accelerates amyloid-β (Abeta) degradation and inhibits Abeta-induced neurodegeneration
    • Melchor, J.P., Pawlak, R., and Strickland, S. The tissue plasminogen activator-plasminogen proteolytic cascade accelerates amyloid-β (Abeta) degradation and inhibits Abeta-induced neurodegeneration. J Neurosci. 23, 8867-8871 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 8867-8871
    • Melchor, J.P.1    Pawlak, R.2    Strickland, S.3
  • 137
    • 0346749451 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan
    • Larsen, P.H., Wells, J.E., Stallcup, W.B., Opdenakker, G., and Yong, V.W. Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan. J. Neurosci. 23, 11127-11135 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 11127-11135
    • Larsen, P.H.1    Wells, J.E.2    Stallcup, W.B.3    Opdenakker, G.4    Yong, V.W.5
  • 138
    • 0029088484 scopus 로고
    • Excitotoxin-induced neuronal degeneration and seizure are mediated by tissue plasminogen activator
    • Tsirka, S.E., Gualandris, A., Amaral, D.G., and Strickland, S. Excitotoxin-induced neuronal degeneration and seizure are mediated by tissue plasminogen activator. Nature 377, 340-344 (1995).
    • (1995) Nature , vol.377 , pp. 340-344
    • Tsirka, S.E.1    Gualandris, A.2    Amaral, D.G.3    Strickland, S.4
  • 139
    • 0031951510 scopus 로고    scopus 로고
    • Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice
    • Wang, Y.F., Tsirka, S.E., Strickland, S., Stieg, P.E., Soriano, S.G., and Lipton, S.A. Tissue plasminogen activator (tPA) increases neuronal damage after focal cerebral ischemia in wild-type and tPA-deficient mice. Nat. Med. 4, 228-231 (1998).
    • (1998) Nat. Med. , vol.4 , pp. 228-231
    • Wang, Y.F.1    Tsirka, S.E.2    Strickland, S.3    Stieg, P.E.4    Soriano, S.G.5    Lipton, S.A.6
  • 140
    • 0036330667 scopus 로고    scopus 로고
    • Rapid breakdown of microvascular barriers and subsequent hemorrhagic transformation after delayed recombinant tissue plasminogen activator treatment in a rat embolic stroke model
    • Dijkhuizen, R.M., Asahi, M., Wu, O., Rosen, B.R., and Lo, E.H. Rapid breakdown of microvascular barriers and subsequent hemorrhagic transformation after delayed recombinant tissue plasminogen activator treatment in a rat embolic stroke model. Stroke 33, 2100-2104 (2002).
    • (2002) Stroke , vol.33 , pp. 2100-2104
    • Dijkhuizen, R.M.1    Asahi, M.2    Wu, O.3    Rosen, B.R.4    Lo, E.H.5
  • 141
    • 0028089844 scopus 로고
    • Blood -brain barrier abnormalities in longstanding multiple sclerosis lesions. An immunohistochemical study
    • Kwon, E.E. and Prineas, J.W. Blood -brain barrier abnormalities in longstanding multiple sclerosis lesions. An immunohistochemical study. J. Neuropathol. Exp. Neurol. 53, 625-636 (1994).
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 625-636
    • Kwon, E.E.1    Prineas, J.W.2
  • 142
    • 0026503083 scopus 로고
    • Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Agkistrodon rhodostoma
    • Burkhart, W., Smith, G.F., Su, J.L., Parikh, I., and LeVine, H. Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Agkistrodon rhodostoma. FEBS Lett. 297, 297-301 (1992).
    • (1992) FEBS Lett. , vol.297 , pp. 297-301
    • Burkhart, W.1    Smith, G.F.2    Su, J.L.3    Parikh, I.4    LeVine, H.5
  • 143
    • 0018136199 scopus 로고
    • The effects of ancrod, the coagulating enzyme from the venom of Malayan pit viper (A. rhodostoma) on prothrombin and fibrinogen metabolism and fibrinopeptide A release in man
    • Bell, W.R., Shapiro, S.S., Martinez, J., and Nossel, H.L. The effects of ancrod, the coagulating enzyme from the venom of Malayan pit viper (A. rhodostoma) on prothrombin and fibrinogen metabolism and fibrinopeptide A release in man. J. Lab. Clin. Med. 91, 592-604 (1978).
    • (1978) J. Lab. Clin. Med. , vol.91 , pp. 592-604
    • Bell, W.R.1    Shapiro, S.S.2    Martinez, J.3    Nossel, H.L.4
  • 144
    • 0034729698 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix assembly by activated Ras in transformed cells
    • Brenner, K.A., Corbett, S.A., and Schwarzbauer, J.E. Regulation of fibronectin matrix assembly by activated Ras in transformed cells. Oncogene 19, 3156-3163 (2000).
    • (2000) Oncogene , vol.19 , pp. 3156-3163
    • Brenner, K.A.1    Corbett, S.A.2    Schwarzbauer, J.E.3
  • 145
    • 0026061695 scopus 로고
    • The effects of cAMP on differentiation of cultured Schwann cells: Progression from an early phenotype (04+) to a myelin phenotype (P0+, GFAP-, N-CAM-, NGF-receptor-) depends on growth inhibition
    • Morgan, L., Jessen, K.R., and Mirsky, R. The effects of cAMP on differentiation of cultured Schwann cells: progression from an early phenotype (04+) to a myelin phenotype (P0+, GFAP-, N-CAM-, NGF-receptor-) depends on growth inhibition. J. Cell Biol. 112, 457-467 (1991).
    • (1991) J. Cell Biol. , vol.112 , pp. 457-467
    • Morgan, L.1    Jessen, K.R.2    Mirsky, R.3
  • 146
    • 0003703970 scopus 로고    scopus 로고
    • The Parthenon Publishing Group Inc, New York, NY
    • Poser, C.M., An Atlas of Multiple Sclerosis. The Parthenon Publishing Group Inc, New York, NY, 1998: p.60.
    • (1998) an Atlas of Multiple Sclerosis , pp. 60
    • Poser, C.M.1
  • 148
    • 0038297125 scopus 로고    scopus 로고
    • Fibrinogen-CD11b/CD18 interaction activates the NF-κB pathway and delays apoptosis in human neutrophils
    • Rubel, C., Gomez, S., Fernandez, G.C., Isturiz, M.A., Caamano, J., and Palermo, M.S. Fibrinogen-CD11b/CD18 interaction activates the NF-κB pathway and delays apoptosis in human neutrophils. Eur. J. Immunol. 33, 1429-1438 (2003).
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1429-1438
    • Rubel, C.1    Gomez, S.2    Fernandez, G.C.3    Isturiz, M.A.4    Caamano, J.5    Palermo, M.S.6
  • 149
    • 0036533481 scopus 로고    scopus 로고
    • Soluble fibrinogen modulates neutrophil functionality through the activation of an extracellular signal-regulated kinase-dependent pathway
    • Rubel, C., Fernandez, G.C., Rosa, F.A., Gomez, S., Bompadre, M.B., Coso, O.A., Isturiz, M.A., and Palermo, M.S. Soluble fibrinogen modulates neutrophil functionality through the activation of an extracellular signal-regulated kinase-dependent pathway. J. Immunol. 168, 3527-3535 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 3527-3535
    • Rubel, C.1    Fernandez, G.C.2    Rosa, F.A.3    Gomez, S.4    Bompadre, M.B.5    Coso, O.A.6    Isturiz, M.A.7    Palermo, M.S.8
  • 150
    • 0024109978 scopus 로고
    • Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen
    • Altieri, D.C., Bader, R., Mannucci, P.M., and Edgington, T.S. Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen. J. Cell Biol. 107, 1893-1900 (1988).
    • (1988) J. Cell Biol. , vol.107 , pp. 1893-1900
    • Altieri, D.C.1    Bader, R.2    Mannucci, P.M.3    Edgington, T.S.4
  • 152
    • 0035927074 scopus 로고    scopus 로고
    • Integrin aMb2-mediated cell migration to fibrinogen and its recognition peptides
    • Forsyth, C.B, Solovjov, D.A., Ugarova, T.P., and Plow, E.F. Integrin aMb2-mediated cell migration to fibrinogen and its recognition peptides. J. Exp. Med. 193, 1123-1133 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 1123-1133
    • Forsyth, C.B.1    Solovjov, D.A.2    Ugarova, T.P.3    Plow, E.F.4
  • 153
    • 0030952228 scopus 로고    scopus 로고
    • Thrombopoietin enhances the aIIbb3-dependent adhesion of megakaryocytic cells to fibrinogen or fibronectin through PI 3 kinase
    • Zauli, G., Bassini, A., Vitale, M., Gibellini, D., Celeghini, C., Caramelli, E., Pierpaoli, S., Guidotti, L., and Capitani, S. Thrombopoietin enhances the aIIbb3-dependent adhesion of megakaryocytic cells to fibrinogen or fibronectin through PI 3 kinase. Blood 89, 883-895 (1997).
    • (1997) Blood , vol.89 , pp. 883-895
    • Zauli, G.1    Bassini, A.2    Vitale, M.3    Gibellini, D.4    Celeghini, C.5    Caramelli, E.6    Pierpaoli, S.7    Guidotti, L.8    Capitani, S.9
  • 154
    • 0005306564 scopus 로고
    • Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor
    • Cheresh, D.A. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc. Natl. Acad. Sci. U.S.A. 84, 6471-6475 (1987).
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6471-6475
    • Cheresh, D.A.1
  • 155
  • 156
    • 0035164333 scopus 로고    scopus 로고
    • Analysis of the roles of ICAM-1 in neutrophil transmigration using a reconstituted mammalian cell expression model: Implication of ICAM-1 cytoplasmic domain and Rho-dependent signaling pathway
    • Sans, E., Delachanal, E., and Duperray, A. Analysis of the roles of ICAM-1 in neutrophil transmigration using a reconstituted mammalian cell expression model: Implication of ICAM-1 cytoplasmic domain and Rho-dependent signaling pathway. J. Immunol. 166, 544-551 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 544-551
    • Sans, E.1    Delachanal, E.2    Duperray, A.3
  • 157
    • 0028897412 scopus 로고
    • Structural recognition of a novel fibrinogen gamma chain sequence (117-133) by intercellular adhesion molecule-1 mediates leukocyte-endothelium interaction
    • Altieri, D.C., Duperray, A., Plescia, J., Thornton, G.B., and Languino, L.R. Structural recognition of a novel fibrinogen gamma chain sequence (117-133) by intercellular adhesion molecule-1 mediates leukocyte-endothelium interaction. J. Biol. Chem. 270, 696-699 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 696-699
    • Altieri, D.C.1    Duperray, A.2    Plescia, J.3    Thornton, G.B.4    Languino, L.R.5
  • 158
    • 0031017065 scopus 로고    scopus 로고
    • Molecular identification of a novel fibrinogen binding site on the first domain of ICAM-1 regulating leukocyte-endothelium bridging
    • Duperray, A., Languino, L.R., Plescia, J., McDowall, A., Hogg, N., Craig, A.G., Berendt, A.R., and Altieri, D.C. Molecular identification of a novel fibrinogen binding site on the first domain of ICAM-1 regulating leukocyte-endothelium bridging. J. Biol. Chem. 272, 435-441 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 435-441
    • Duperray, A.1    Languino, L.R.2    Plescia, J.3    McDowall, A.4    Hogg, N.5    Craig, A.G.6    Berendt, A.R.7    Altieri, D.C.8
  • 159
    • 0027318675 scopus 로고
    • Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway
    • Languino, L.R., Plescia, J., Duperray, A., Brian, A.A., Plow, E.F., Geltosky, J.E., and Altieri, D.C. Fibrinogen mediates leukocyte adhesion to vascular endothelium through an ICAM-1-dependent pathway. Cell 73, 1423-1434 (1993).
    • (1993) Cell , vol.73 , pp. 1423-1434
    • Languino, L.R.1    Plescia, J.2    Duperray, A.3    Brian, A.A.4    Plow, E.F.5    Geltosky, J.E.6    Altieri, D.C.7
  • 160
    • 0028957672 scopus 로고
    • Regulation of leukocyte-endothelium interaction and leukocyte transendothelial migration by intercellular adhesion molecule 1-fibrinogen recognition
    • Languino, L.R., Duperray, A., Joganic, K.J., Fornaro, M., Thornton, G.B., and Altieri, D.C. Regulation of leukocyte-endothelium interaction and leukocyte transendothelial migration by intercellular adhesion molecule 1-fibrinogen recognition. Proc. Natl. Acad. Sci. U.S.A. 92, 1505-1509 (1995).
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1505-1509
    • Languino, L.R.1    Duperray, A.2    Joganic, K.J.3    Fornaro, M.4    Thornton, G.B.5    Altieri, D.C.6
  • 162
    • 0029133834 scopus 로고
    • Cell proliferation on fibrin: Modulation by fibrinopeptide cleavage
    • Sporn, L.A., Bunce, L.A., and Francis, C.W. Cell proliferation on fibrin: Modulation by fibrinopeptide cleavage. Blood 86, 1802-1810 (1995).
    • (1995) Blood , vol.86 , pp. 1802-1810
    • Sporn, L.A.1    Bunce, L.A.2    Francis, C.W.3
  • 164
    • 0032514899 scopus 로고    scopus 로고
    • Endothelial cell VE-cadherin functions as a receptor for the b15-42 sequence of fibrin
    • Bach, T.L., Barsigian, C., Yaen, C.H., and Martinez, J. Endothelial cell VE-cadherin functions as a receptor for the b15-42 sequence of fibrin. J. Biol. Chem. 273, 30719-30728 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 30719-30728
    • Bach, T.L.1    Barsigian, C.2    Yaen, C.H.3    Martinez, J.4
  • 165
    • 0018631259 scopus 로고
    • The binding of thrombin by fibrin
    • Liu, C.Y., Nossel, H.L., and Kaplan, K.L. The binding of thrombin by fibrin. J. Biol. Chem. 254, 10421-10425 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 10421-10425
    • Liu, C.Y.1    Nossel, H.L.2    Kaplan, K.L.3
  • 166
    • 0021046716 scopus 로고
    • Latent tissue plasminogen activator produced by human endothelial cells in culture: Evidence for an enzyme-inhibitor complex
    • Levin, E.G. Latent tissue plasminogen activator produced by human endothelial cells in culture: Evidence for an enzyme-inhibitor complex. Proc. Natl. Acad. Sci. U.S.A. 80, 6804-6808 (1983).
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 6804-6808
    • Levin, E.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.