메뉴 건너뛰기




Volumn 13, Issue 15, 1999, Pages 2214-2224

Incorporation of heparin-binding peptides into fibrin gels enhances neurite extension: An example of designer matrices in tissue engineering

Author keywords

Antithrombin III; Neural cell adhesion molecule; Platelet factor 4; Regeneration

Indexed keywords

ANTITHROMBIN III; BLOOD CLOTTING FACTOR 13A; FIBRIN; HEPARIN; HEPARIN BINDING PROTEIN; NERVE CELL ADHESION MOLECULE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; THROMBOCYTE FACTOR 4;

EID: 0032764946     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.13.15.2214     Document Type: Article
Times cited : (175)

References (48)
  • 1
    • 84974774282 scopus 로고
    • Nerve regeneration problems in a clinical perspective
    • Lundborg, G. (1990) Nerve regeneration problems in a clinical perspective. Restor. Neurol. Neurosci. 1, 297-302
    • (1990) Restor. Neurol. Neurosci. , vol.1 , pp. 297-302
    • Lundborg, G.1
  • 2
    • 0023522672 scopus 로고
    • Exogenous matrix precursors promote functional nerve regeneration across a 15 mm gap within a silicone chamber in the rat
    • Williams, L. R., Danielson, N., Müller, H., and Varon, S. (1987) Exogenous matrix precursors promote functional nerve regeneration across a 15 mm gap within a silicone chamber in the rat. J. Comp. Neurol. 264, 284-290
    • (1987) J. Comp. Neurol. , vol.264 , pp. 284-290
    • Williams, L.R.1    Danielson, N.2    Müller, H.3    Varon, S.4
  • 3
    • 0023610426 scopus 로고
    • Exogenous fibrin matrix precursors stimulate the temporal progress of nerve regeneration within a silicone chamber
    • William, L. R. (1987) Exogenous fibrin matrix precursors stimulate the temporal progress of nerve regeneration within a silicone chamber. Neurochem. Res. 12, 851-860
    • (1987) Neurochem. Res. , vol.12 , pp. 851-860
    • William, L.R.1
  • 4
    • 0025116502 scopus 로고
    • The morphology of regenerating peripheral nerves is modulated by the surface microgeometry of polymeric guidance channels
    • Aebischer, P., Guenard, V., and Valentini, R. F. (1990) The morphology of regenerating peripheral nerves is modulated by the surface microgeometry of polymeric guidance channels. Brain Res. 531, 211-218
    • (1990) Brain Res. , vol.531 , pp. 211-218
    • Aebischer, P.1    Guenard, V.2    Valentini, R.F.3
  • 5
    • 0023518505 scopus 로고
    • A pentapeptide from the laminin B1 chain mediates cell adhesion and bind the 67,000 da laminin receptor
    • Graf, J., Ogle, R. C., Robey, F. A., Sasaki, M., Martin, G. R., Yamada, Y., and Kleinman, H. R. (1987) A pentapeptide from the laminin B1 chain mediates cell adhesion and bind the 67,000 Da laminin receptor. Biochemistry 26, 6896-6900
    • (1987) Biochemistry , vol.26 , pp. 6896-6900
    • Graf, J.1    Ogle, R.C.2    Robey, F.A.3    Sasaki, M.4    Martin, G.R.5    Yamada, Y.6    Kleinman, H.R.7
  • 6
    • 0023666132 scopus 로고
    • Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor binding
    • Graf, J., Iwamoto, Y., Sasaki, M., Martin, G. R., Kleinman, H. R., Robey, F. A., and Yamada, Y. (1987) Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis, and receptor binding. Cell 48, 989-996
    • (1987) Cell , vol.48 , pp. 989-996
    • Graf, J.1    Iwamoto, Y.2    Sasaki, M.3    Martin, G.R.4    Kleinman, H.R.5    Robey, F.A.6    Yamada, Y.7
  • 7
    • 0024356683 scopus 로고
    • Identification of a second active site in laminin for promotion of cell adhesion and migration and inhibition of in vivo melanoma lung colonization
    • Kleinman, H. K., Graf, J., Iwamoto, I., Sasaki, M., Schasteen, C. S., Yamada, Y., Martin, G. R., and Robey, F. A. (1989) Identification of a second active site in laminin for promotion of cell adhesion and migration and inhibition of in vivo melanoma lung colonization. Arch. Biochem. Biophys. 272, 39-45
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 39-45
    • Kleinman, H.K.1    Graf, J.2    Iwamoto, I.3    Sasaki, M.4    Schasteen, C.S.5    Yamada, Y.6    Martin, G.R.7    Robey, F.A.8
  • 8
    • 0027481027 scopus 로고
    • Covalently immobilized laminin peptide Tyr-Ile-Gly-Ser-Arg (YIGSR) supports cell spreading and colocalization of the 67 kD laminin receptor with α-actinin and vinculin
    • Massia, S. P., Rao, S. S., and Hubbell, J. A. (1993) Covalently immobilized laminin peptide Tyr-Ile-Gly-Ser-Arg (YIGSR) supports cell spreading and colocalization of the 67 kD laminin receptor with α-actinin and vinculin. J. Biol. Chem. 268, 8053-8059
    • (1993) J. Biol. Chem. , vol.268 , pp. 8053-8059
    • Massia, S.P.1    Rao, S.S.2    Hubbell, J.A.3
  • 9
    • 0025259095 scopus 로고
    • Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site exposed in fragment PI
    • Aumailley, M., Gerl, M., Sonnenberg, A., Dutzmann, R., and Timpl, R. (1990) Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site exposed in fragment PI. FEBS Lett. 262, 82-86
    • (1990) FEBS Lett. , vol.262 , pp. 82-86
    • Aumailley, M.1    Gerl, M.2    Sonnenberg, A.3    Dutzmann, R.4    Timpl, R.5
  • 11
    • 0025159429 scopus 로고
    • α2β1 integrins from different cell types show different cell binding specificities
    • Kirchhofer, D., Languino, L. R., Ruslahti, E., and Peirschbacher, M. D. (1990) α2β1 integrins from different cell types show different cell binding specificities. J. Biol. Chem. 265, 615-618
    • (1990) J. Biol. Chem. , vol.265 , pp. 615-618
    • Kirchhofer, D.1    Languino, L.R.2    Ruslahti, E.3    Peirschbacher, M.D.4
  • 12
    • 0024443667 scopus 로고
    • A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth
    • Tashiro, K., Sephel, G. C., Weeks, B., Sasaki, M., Martin, G. R., Kleinman, H. K., and Yamada, Y. (1989) A synthetic peptide containing the IKVAV sequence from the A chain of laminin mediates cell attachment, migration, and neurite outgrowth. J. Biol. Chem. 264, 16174-16182
    • (1989) J. Biol. Chem. , vol.264 , pp. 16174-16182
    • Tashiro, K.1    Sephel, G.C.2    Weeks, B.3    Sasaki, M.4    Martin, G.R.5    Kleinman, H.K.6    Yamada, Y.7
  • 13
    • 0024562011 scopus 로고
    • Identification of a neurite-outgrowth promoting domain using synthetic peptides
    • Liesi, P., Narvanen, A., Soos, J., Sariola, H., and Snounou, G. (1989) Identification of a neurite-outgrowth promoting domain using synthetic peptides. FEBS Lett. 244, 141-148
    • (1989) FEBS Lett. , vol.244 , pp. 141-148
    • Liesi, P.1    Narvanen, A.2    Soos, J.3    Sariola, H.4    Snounou, G.5
  • 14
    • 0025238409 scopus 로고
    • Identification of a cadherin cell adhesion recognition sequence
    • Blaschuk, O. W., Sullivan, R., David, S., and Pouliot, Y. (1990) Identification of a cadherin cell adhesion recognition sequence. Dev. Biol. 139, 227-229
    • (1990) Dev. Biol. , vol.139 , pp. 227-229
    • Blaschuk, O.W.1    Sullivan, R.2    David, S.3    Pouliot, Y.4
  • 15
    • 0343237235 scopus 로고
    • The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival
    • Edgar, D., Timpl, R., and Thoenen, H. (1984) The heparin-binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival. EMBO J. 3, 1463-1468
    • (1984) EMBO J. , vol.3 , pp. 1463-1468
    • Edgar, D.1    Timpl, R.2    Thoenen, H.3
  • 16
    • 0021963316 scopus 로고
    • Neuron-specific interactions with two neurite-promoting fragments of fibronectin
    • Rogers, S. L., McCarthy, J. B., Palm, S. L., Furcht, L. T., and Letourneau, P. C. (1985) Neuron-specific interactions with two neurite-promoting fragments of fibronectin. J. Neurosci. 5, 369-378
    • (1985) J. Neurosci. , vol.5 , pp. 369-378
    • Rogers, S.L.1    McCarthy, J.B.2    Palm, S.L.3    Furcht, L.T.4    Letourneau, P.C.5
  • 17
    • 0023184076 scopus 로고
    • A heparin binding site in antithrombin III. Identification, purification, and amino acid sequence
    • Smith, J. W., and Knauer, D. J. (1987) A heparin binding site in antithrombin III. Identification, purification, and amino acid sequence. J. Biol. Chem. 262, 11964-11972
    • (1987) J. Biol. Chem. , vol.262 , pp. 11964-11972
    • Smith, J.W.1    Knauer, D.J.2
  • 18
    • 0027257980 scopus 로고
    • Mode of interaction between platelet factor 4 and heparin
    • Maccarana, M., and Lindahl, U. (1993) Mode of interaction between platelet factor 4 and heparin. Glycobiology 3, 271-277
    • (1993) Glycobiology , vol.3 , pp. 271-277
    • Maccarana, M.1    Lindahl, U.2
  • 19
    • 0022569856 scopus 로고
    • A heparin-binding domain from N-CAM is involved in neural cell-substratum adhesion
    • Cole, G. J., and Glaser, L. (1986) A heparin-binding domain from N-CAM is involved in neural cell-substratum adhesion. J. Cell Biol. 102, 403-412
    • (1986) J. Cell Biol. , vol.102 , pp. 403-412
    • Cole, G.J.1    Glaser, L.2
  • 20
    • 0029999681 scopus 로고    scopus 로고
    • Midkine, a heparin-binding growth/ differentiation factor, exhibits nerve cell adhesion and guidance activity for neurite outgrowth in vitro
    • Kaneda, N., Talukder, A. H., Nishiyama, H., Koizumi, S., and Muramatsu, T. (1996) Midkine, a heparin-binding growth/ differentiation factor, exhibits nerve cell adhesion and guidance activity for neurite outgrowth in vitro. J. Biochem. (Tokyo) 119, 1150-1156
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 1150-1156
    • Kaneda, N.1    Talukder, A.H.2    Nishiyama, H.3    Koizumi, S.4    Muramatsu, T.5
  • 21
    • 0028342466 scopus 로고
    • Expression of HB-GAM (heparin-binding growth-associated molecules) in the pathways of developing axonal processes in vivo and neurite outgrowth in vitro induced by HB-GAM
    • Rauvala, H., Vanhala, A., Castren, E., Nolo, R., Raulo, E., Merenmies, J., and Panula, P. (1994) Expression of HB-GAM (heparin-binding growth-associated molecules) in the pathways of developing axonal processes in vivo and neurite outgrowth in vitro induced by HB-GAM. Brain Res. Dev. Brain Res. 79, 157-176
    • (1994) Brain Res. Dev. Brain Res. , vol.79 , pp. 157-176
    • Rauvala, H.1    Vanhala, A.2    Castren, E.3    Nolo, R.4    Raulo, E.5    Merenmies, J.6    Panula, P.7
  • 22
    • 0024466788 scopus 로고
    • Molecular mechanisms of avian neural crest cell migration on fibronectin and laminin
    • Perris, R., Paulsson, M., and Bronner-Fraser, M. (1989) Molecular mechanisms of avian neural crest cell migration on fibronectin and laminin. Dev. Biol. 136, 222-238
    • (1989) Dev. Biol. , vol.136 , pp. 222-238
    • Perris, R.1    Paulsson, M.2    Bronner-Fraser, M.3
  • 23
    • 0024401983 scopus 로고
    • Laminin neural activity and binding proteins
    • Sephel, G. C., Burrous, B. A., and Kleinman, H. K. (1989) Laminin neural activity and binding proteins. Dev. Neurosci. 11, 313-331
    • (1989) Dev. Neurosci. , vol.11 , pp. 313-331
    • Sephel, G.C.1    Burrous, B.A.2    Kleinman, H.K.3
  • 24
    • 0026448194 scopus 로고
    • The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans
    • Kallapur, S. G., and Akeson, R. A. (1992) The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans. J. Neurosci. Res. 33, 538-548
    • (1992) J. Neurosci. Res. , vol.33 , pp. 538-548
    • Kallapur, S.G.1    Akeson, R.A.2
  • 25
    • 0029662171 scopus 로고    scopus 로고
    • Effect of fibrinolysis on neurite growth from dorsal root ganglia cultured in two-and three-dimensional fibrin gels
    • Herbert, C. B., Bittner, G. D., and Hubbell, J. A. (1996) Effect of fibrinolysis on neurite growth from dorsal root ganglia cultured in two-and three-dimensional fibrin gels. J. Comp. Neurol. 365, 380-391
    • (1996) J. Comp. Neurol. , vol.365 , pp. 380-391
    • Herbert, C.B.1    Bittner, G.D.2    Hubbell, J.A.3
  • 26
    • 0032940534 scopus 로고    scopus 로고
    • Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa
    • Schense, J. C., and Hubbell, J. A. (1999) Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa. Bioconjug. Chem. 10, 75-81
    • (1999) Bioconjug. Chem. , vol.10 , pp. 75-81
    • Schense, J.C.1    Hubbell, J.A.2
  • 27
    • 0020575314 scopus 로고
    • 2-terminal peptide of α2-plasmin inhibitor to fibrin
    • 2-terminal peptide of α2-plasmin inhibitor to fibrin. FEBS Lett. 153, 369-371
    • (1983) FEBS Lett. , vol.153 , pp. 369-371
    • Ichinose, A.1    Tamaki, T.2    Aoki, N.3
  • 28
    • 0028210837 scopus 로고
    • Heparin binding domain peptides of antithrombin III: Analysis by isothermal titration calorimetry and circular dichroism spectroscopy
    • Tyler-Cross, R., Sobel, M., Marques, D., and Harris, R. B. (1994) Heparin binding domain peptides of antithrombin III: analysis by isothermal titration calorimetry and circular dichroism spectroscopy. Protein Sci. 3, 620-627
    • (1994) Protein Sci. , vol.3 , pp. 620-627
    • Tyler-Cross, R.1    Sobel, M.2    Marques, D.3    Harris, R.B.4
  • 29
    • 0025944268 scopus 로고
    • Platelet factor 4: Production, structure and physiologic and immunologic action
    • Zucker, M. B., and Katz, I. R. (1991) Platelet factor 4: production, structure and physiologic and immunologic action. Proc. Soc. Exp. Biol. Med. 198, 93-702
    • (1991) Proc. Soc. Exp. Biol. Med. , vol.198 , pp. 93-702
    • Zucker, M.B.1    Katz, I.R.2
  • 30
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B., and Noble, R. L. (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35, 161-214
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 31
    • 0002883735 scopus 로고
    • The isolation and assay of the NGF proteins
    • Freid, R., ed, Marcel Dekker, Inc., New York
    • Varon, S. (1972) The isolation and assay of the NGF proteins. In Methods in Neurochemistry (Freid, R., ed) pp. 203-209, Marcel Dekker, Inc., New York
    • (1972) Methods in Neurochemistry , pp. 203-209
    • Varon, S.1
  • 32
    • 0029764173 scopus 로고    scopus 로고
    • Developmentally regulated neunte outgrowth response from dorsal root ganglion neurons to heparin-binding growth-associated molecule (HB-GAM) and the expression of HB-GAM in the targets of the developing dorsal root ganglion neurites
    • Nolo, R., Kaksonen, M., and Ravuvala, H. (1996) Developmentally regulated neunte outgrowth response from dorsal root ganglion neurons to heparin-binding growth-associated molecule (HB-GAM) and the expression of HB-GAM in the targets of the developing dorsal root ganglion neurites. Eur. J. Neurosci. 8, 1658-1665
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 1658-1665
    • Nolo, R.1    Kaksonen, M.2    Ravuvala, H.3
  • 33
    • 85012344316 scopus 로고
    • Cell-substratum adhesion in chick neural retina depends upon protein-heparan sulfate interactions
    • Cole, G. J., Schubert, D., and Glaser, L. (1985) Cell-substratum adhesion in chick neural retina depends upon protein-heparan sulfate interactions. J. Cell Biol. 100, 1192-1199
    • (1985) J. Cell Biol. , vol.100 , pp. 1192-1199
    • Cole, G.J.1    Schubert, D.2    Glaser, L.3
  • 34
    • 0023940554 scopus 로고
    • Differential outgrowth of retinal neurites on purified extracellular matrix molecules
    • Carri, N., Perrish, R., Johnasson, S., and Edbenal, T. (1988) Differential outgrowth of retinal neurites on purified extracellular matrix molecules. J. Neurosci. Res. 19, 428-439
    • (1988) J. Neurosci. Res. , vol.19 , pp. 428-439
    • Carri, N.1    Perrish, R.2    Johnasson, S.3    Edbenal, T.4
  • 35
    • 0030984729 scopus 로고    scopus 로고
    • Derivitized cyclodextrins as peptidomimetics: Influence on neunte growth
    • Borrajo, A., Gorin, B., Dostaler, S., Riopelle, R., and Thatcher, G. (1997) Derivitized cyclodextrins as peptidomimetics: influence on neunte growth. Bioorg. Med. Chem. 7, 1185-1190
    • (1997) Bioorg. Med. Chem. , vol.7 , pp. 1185-1190
    • Borrajo, A.1    Gorin, B.2    Dostaler, S.3    Riopelle, R.4    Thatcher, G.5
  • 36
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek, S. P., Loftus, J. C., Ginsburg, M. H., Lauffenburger, D. A., and Horwitz, A. F. (1997) Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature (London) 385, 537-540
    • (1997) Nature (London) , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsburg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 37
    • 0032514145 scopus 로고    scopus 로고
    • Involvement of receptor-like protein tyrosine phosphatase ζ/RPTPβ and its ligand pleitrophin/heparin-binding growth-associated molecule (HB-GAM) in neuronal migration
    • Maeda, N., and Noda, M. (1998) Involvement of receptor-like protein tyrosine phosphatase ζ/RPTPβ and its ligand pleitrophin/heparin-binding growth-associated molecule (HB-GAM) in neuronal migration. J. Cell Biol. 142, 203-216
    • (1998) J. Cell Biol. , vol.142 , pp. 203-216
    • Maeda, N.1    Noda, M.2
  • 38
    • 0028109453 scopus 로고
    • Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan
    • Maeda, N., Hamanaka, H., Shintani, T., Nishiwaki, T., and Noda, M. (1994) Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan. FEBS Lett. 354, 67-70
    • (1994) FEBS Lett. , vol.354 , pp. 67-70
    • Maeda, N.1    Hamanaka, H.2    Shintani, T.3    Nishiwaki, T.4    Noda, M.5
  • 39
    • 0028216755 scopus 로고
    • Isolation of a neuronal cell surface receptor of heparin-binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3)
    • Raolo, E., Chernousov, M. A., Carey, D. J., Nolo, R., and Rauvala, H. (1994) Isolation of a neuronal cell surface receptor of heparin-binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3). J. Biol. Chem. 269, 12999-13004
    • (1994) J. Biol. Chem. , vol.269 , pp. 12999-13004
    • Raolo, E.1    Chernousov, M.A.2    Carey, D.J.3    Nolo, R.4    Rauvala, H.5
  • 40
    • 0030050980 scopus 로고    scopus 로고
    • Neurite outgrowth in brain neurons induced by heparin-binding growth-associated molecule (HB-GAM) depends on the specific interaction of HB-GAM with heparan sulfate at the cell surface
    • Kinnunen, T., Raulo, E., Nolo, R., Maccarana, M., Lindahl, U., and Rauvala, H. (1996) Neurite outgrowth in brain neurons induced by heparin-binding growth-associated molecule (HB-GAM) depends on the specific interaction of HB-GAM with heparan sulfate at the cell surface. J. Biol. Chem. 271, 2243-2248
    • (1996) J. Biol. Chem. , vol.271 , pp. 2243-2248
    • Kinnunen, T.1    Raulo, E.2    Nolo, R.3    Maccarana, M.4    Lindahl, U.5    Rauvala, H.6
  • 41
    • 2642619407 scopus 로고    scopus 로고
    • A completely biological tissue-engineered human blood vessel
    • L'Heureux, N., Pauet, S., Labbe, R., Germain, L., and Auger, F. A. (1998) A completely biological tissue-engineered human blood vessel. FASEB J. 12, 47-56
    • (1998) FASEB J. , vol.12 , pp. 47-56
    • L'Heureux, N.1    Pauet, S.2    Labbe, R.3    Germain, L.4    Auger, F.A.5
  • 42
    • 0031666409 scopus 로고    scopus 로고
    • In vitro reconstruction of a human capillary-like network in a tissue-engineered skin equivalent
    • Black, A. F., Berthod, F., L'Heureux, N., Germain, L., and Auger, F. A. (1998) In vitro reconstruction of a human capillary-like network in a tissue-engineered skin equivalent. FASEB J. 12, 1331-1340
    • (1998) FASEB J. , vol.12 , pp. 1331-1340
    • Black, A.F.1    Berthod, F.2    L'Heureux, N.3    Germain, L.4    Auger, F.A.5
  • 48
    • 0024854138 scopus 로고
    • Neuronal plasminogen activators: Cell surface binding sites and involvement in neurite outgrowth
    • Pittman, R. N., Ivins, J. K., and Buettner, H. M. (1989) Neuronal plasminogen activators: cell surface binding sites and involvement in neurite outgrowth. J. Neurosci. 9, 4269-4286
    • (1989) J. Neurosci. , vol.9 , pp. 4269-4286
    • Pittman, R.N.1    Ivins, J.K.2    Buettner, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.