메뉴 건너뛰기




Volumn 13, Issue 7, 2007, Pages 1469-1477

Characterization and inhibition of fibrin hydrogel-degrading enzymes during development of tissue engineering scaffolds

Author keywords

[No Author keywords available]

Indexed keywords

CARTILAGE; ENCAPSULATION; TISSUE ENGINEERING; TRANSCRIPTION FACTORS;

EID: 34547120714     PISSN: 10763279     EISSN: None     Source Type: Journal    
DOI: 10.1089/ten.2006.0354     Document Type: Article
Times cited : (78)

References (42)
  • 1
    • 0036680533 scopus 로고    scopus 로고
    • Tissue engineering: Advances in in-vitro cartilage generation (review)
    • Risbud, M.V., and Sittinger, M. Tissue engineering: advances in in-vitro cartilage generation (review). Trends Biotechnol. 20, 351, 2002.
    • (2002) Trends Biotechnol , vol.20 , pp. 351
    • Risbud, M.V.1    Sittinger, M.2
  • 2
    • 4644301881 scopus 로고    scopus 로고
    • Fate of transplanted bone-marrow-derived mesenchymal cells during osteochondral repair using transgenic rats to stimulate autologous transplantation
    • Oshima, Y., Watanabe, N., Matsuda, K., Takai, S., Kawata, M., and Kubo, T. Fate of transplanted bone-marrow-derived mesenchymal cells during osteochondral repair using transgenic rats to stimulate autologous transplantation. Osteoarthr. Cartil. 12, 811, 2004.
    • (2004) Osteoarthr. Cartil , vol.12 , pp. 811
    • Oshima, Y.1    Watanabe, N.2    Matsuda, K.3    Takai, S.4    Kawata, M.5    Kubo, T.6
  • 3
    • 0032813132 scopus 로고    scopus 로고
    • Histological analysis of tissue after failed cartilage repair procedures
    • Nehrer, S., Spector, M., and Minas, T. Histological analysis of tissue after failed cartilage repair procedures. Clin. Orthop. Relat. Res. 365, 149, 1999.
    • (1999) Clin. Orthop. Relat. Res , vol.365 , pp. 149
    • Nehrer, S.1    Spector, M.2    Minas, T.3
  • 5
    • 13944260854 scopus 로고    scopus 로고
    • Engineering of fibrin-based functional and implantable small-diameter blood vessels
    • Swartz, D.D., Russel, J.A., and Andreadis, S.T. Engineering of fibrin-based functional and implantable small-diameter blood vessels. Am. J. Physiol. Heart. Circ. Physiol. 288, H1451, 2005.
    • (2005) Am. J. Physiol. Heart. Circ. Physiol , vol.288
    • Swartz, D.D.1    Russel, J.A.2    Andreadis, S.T.3
  • 7
    • 1642382425 scopus 로고    scopus 로고
    • Experimental hind limb ischemia leads to neutrophil-mediated increase in gastrocnemius MMP-2 and -9 activity, a potential mechanism for ischemia induced MMP activation
    • Muhs, B.E., Gagne, P., Plitas, G., Shaw, J.P., and Shamamian, P. Experimental hind limb ischemia leads to neutrophil-mediated increase in gastrocnemius MMP-2 and -9 activity, a potential mechanism for ischemia induced MMP activation. J. Surg. Res. 117, 249, 2004.
    • (2004) J. Surg. Res , vol.117 , pp. 249
    • Muhs, B.E.1    Gagne, P.2    Plitas, G.3    Shaw, J.P.4    Shamamian, P.5
  • 8
    • 0029766216 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors and the prevention of connective tissue breakdown (review)
    • Cawston, T.E. Metalloproteinase inhibitors and the prevention of connective tissue breakdown (review). Pharmacol. Ther. 70, 163, 1996.
    • (1996) Pharmacol. Ther , vol.70 , pp. 163
    • Cawston, T.E.1
  • 9
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinase: Structures, evolution, and diversification
    • Massova, I., Kotra, L.P., Fridman, R., and Mobashery, S. Matrix metalloproteinase: structures, evolution, and diversification. FASEB J. 12, 1075, 1998.
    • (1998) FASEB J , vol.12 , pp. 1075
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 10
    • 0034692498 scopus 로고    scopus 로고
    • Rapid activation of matrix metalloproteinase-2 by glioma cells occurs through a post-translational MT1-MMP-dependent mechanism
    • Gingras, D., Page, M., Annabi, I.B., and Beliveau, R. Rapid activation of matrix metalloproteinase-2 by glioma cells occurs through a post-translational MT1-MMP-dependent mechanism. Biochem. Biophys. Acta. 1497, 341, 2000.
    • (2000) Biochem. Biophys. Acta , vol.1497 , pp. 341
    • Gingras, D.1    Page, M.2    Annabi, I.B.3    Beliveau, R.4
  • 11
    • 0035164041 scopus 로고    scopus 로고
    • The balance between proteinases and inhibitors in a murine model of proliferative retinopathy
    • Majka, S., McGuire, P., Colombo, S., and Das, A. The balance between proteinases and inhibitors in a murine model of proliferative retinopathy. Invest. Ophthalmol. Vis. Sci. 42, 210, 2001.
    • (2001) Invest. Ophthalmol. Vis. Sci , vol.42 , pp. 210
    • Majka, S.1    McGuire, P.2    Colombo, S.3    Das, A.4
  • 12
    • 0027944171 scopus 로고
    • Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteinases
    • Gijbels, K., Galardy, R.E., and Steinman, L. Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteinases. J. Clin. Invest. 94, 2177, 1994.
    • (1994) J. Clin. Invest , vol.94 , pp. 2177
    • Gijbels, K.1    Galardy, R.E.2    Steinman, L.3
  • 13
    • 0032983168 scopus 로고    scopus 로고
    • Galardin inhibits collagen degradation by rabbit keratocytes by inhibiting the activation of pro-matrix metalloproteinases
    • Hao, J.L., Nagano, T., Nakamura, M., Kumagai, N., Mishima, H., and Nishida, T. Galardin inhibits collagen degradation by rabbit keratocytes by inhibiting the activation of pro-matrix metalloproteinases. Exp. Eye Res. 68, 565, 1999.
    • (1999) Exp. Eye Res , vol.68 , pp. 565
    • Hao, J.L.1    Nagano, T.2    Nakamura, M.3    Kumagai, N.4    Mishima, H.5    Nishida, T.6
  • 14
    • 0035225553 scopus 로고    scopus 로고
    • Collen, D. Ham-Wasserman lecture: role of the plasminogen system in fibrin-homeostasis and tissue remodeling (Review). Hematology Am. Soc. Hematol. Educ. Program 1, 2001.
    • Collen, D. Ham-Wasserman lecture: role of the plasminogen system in fibrin-homeostasis and tissue remodeling (Review). Hematology Am. Soc. Hematol. Educ. Program 1, 2001.
  • 15
    • 18144417470 scopus 로고    scopus 로고
    • Human breast cancer cell-mediated bone collagen degradation requires plasminogen activation and matrix metalloproteinase activity
    • Morgan, H., and Hill, P.A. Human breast cancer cell-mediated bone collagen degradation requires plasminogen activation and matrix metalloproteinase activity. Cancer Cell Int. 5, 1, 2005.
    • (2005) Cancer Cell Int , vol.5 , pp. 1
    • Morgan, H.1    Hill, P.A.2
  • 17
    • 0029792565 scopus 로고    scopus 로고
    • Analysis of chondroprogenitor frequency and cartilage differentiation in a novel family of clonal chondrogenic rat cell lines
    • Grigoriadis, A.E., Heersche, J.N., and Aubin, J.E. Analysis of chondroprogenitor frequency and cartilage differentiation in a novel family of clonal chondrogenic rat cell lines. Differentiation 60, 299, 1996.
    • (1996) Differentiation , vol.60 , pp. 299
    • Grigoriadis, A.E.1    Heersche, J.N.2    Aubin, J.E.3
  • 18
    • 0037125032 scopus 로고    scopus 로고
    • Waas, E.T., Lomme. R.M, DeGroot, J., Wobbes, T., and Hendriks, T. Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer. Br. J. Cancer 86, 1876, 2002.
    • Waas, E.T., Lomme. R.M, DeGroot, J., Wobbes, T., and Hendriks, T. Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer. Br. J. Cancer 86, 1876, 2002.
  • 19
    • 0028334115 scopus 로고
    • Zymographic techniques for detection and characterization of microbial protease
    • Lantz, M.S., and Ciborowski, P. Zymographic techniques for detection and characterization of microbial protease. Meth. Enzymol. 235, 563, 1994.
    • (1994) Meth. Enzymol , vol.235 , pp. 563
    • Lantz, M.S.1    Ciborowski, P.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680, 1970.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 21
    • 0009482260 scopus 로고
    • Electophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelen, T., and Gordon, J. Electophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A.76, 4350, 1979.
    • (1979) Proc. Natl. Acad. Sci. U. S. A , vol.76 , pp. 4350
    • Towbin, H.1    Staehelen, T.2    Gordon, J.3
  • 22
    • 0032170936 scopus 로고    scopus 로고
    • Delivery system for targeted thrombolysis without the risk of hemorrhage
    • Byun, Y., and Yang, V.C. Delivery system for targeted thrombolysis without the risk of hemorrhage. ASAIO J. 44, M638, 1998.
    • (1998) ASAIO J , vol.44
    • Byun, Y.1    Yang, V.C.2
  • 23
    • 0036081029 scopus 로고    scopus 로고
    • A fibrin- based bioengineered ocular surface with human corneal epithelial stem cells
    • Han, B., Schwab, I.R., Madsen, T.K., and Isseroff, R.R. A fibrin- based bioengineered ocular surface with human corneal epithelial stem cells. Cornea 21, 505, 2002.
    • (2002) Cornea , vol.21 , pp. 505
    • Han, B.1    Schwab, I.R.2    Madsen, T.K.3    Isseroff, R.R.4
  • 24
    • 0032981818 scopus 로고    scopus 로고
    • Stabilization of fibrin-chondrocyte constructs for cartilage reconstruction
    • Meinhart, J., Fussenegger, M., and Hobling, W. Stabilization of fibrin-chondrocyte constructs for cartilage reconstruction. Ann. Plast. Surg. 42, 673, 1999.
    • (1999) Ann. Plast. Surg , vol.42 , pp. 673
    • Meinhart, J.1    Fussenegger, M.2    Hobling, W.3
  • 25
    • 12344328225 scopus 로고    scopus 로고
    • Effect of inhibition of matrix metalloproteinases on cartilage loss in vitro and in guinea pig model of osteoarthritis
    • Sabatini, M., Lesur, C., Thomas, M., Chomel, A., Anract, P., de Nanteuil, G., and Pastoureau, P. Effect of inhibition of matrix metalloproteinases on cartilage loss in vitro and in guinea pig model of osteoarthritis. Arthritis Rheum. 52, 171, 2005.
    • (2005) Arthritis Rheum , vol.52 , pp. 171
    • Sabatini, M.1    Lesur, C.2    Thomas, M.3    Chomel, A.4    Anract, P.5    de Nanteuil, G.6    Pastoureau, P.7
  • 26
    • 0024266559 scopus 로고
    • Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte culture
    • Yamada, H., Stephens, R.W., Nakagawa, T. and McNicol, D. Detection and partial characterization of a specific plasminogen activator inhibitor in human chondrocyte culture. J. Biochem. (Tokyo) 104, 960, 1988.
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 960
    • Yamada, H.1    Stephens, R.W.2    Nakagawa, T.3    McNicol, D.4
  • 27
    • 0033136583 scopus 로고    scopus 로고
    • Extrahepatic synthesis of plasminogen in the human cornea is up-regulated by interleukins-1 alpha and -1beta
    • Twining, S.S., Wilson, P.M., and Ngamkitidechakul, C. Extrahepatic synthesis of plasminogen in the human cornea is up-regulated by interleukins-1 alpha and -1beta. Biochem. J. 339, 705, 1999.
    • (1999) Biochem. J , vol.339 , pp. 705
    • Twining, S.S.1    Wilson, P.M.2    Ngamkitidechakul, C.3
  • 28
    • 0036829201 scopus 로고    scopus 로고
    • Mechanism of plasminogen activator inhibitor-1 regulation by oncostatin M and interleukin-1 in human astrocytes
    • Kasza, A., Kiss, D.L., Gopalan, S., Xu, W., Rydel, R.E., Koj, A., and Kordula, T. Mechanism of plasminogen activator inhibitor-1 regulation by oncostatin M and interleukin-1 in human astrocytes. J. Neurochem. 83, 696, 2002.
    • (2002) J. Neurochem , vol.83 , pp. 696
    • Kasza, A.1    Kiss, D.L.2    Gopalan, S.3    Xu, W.4    Rydel, R.E.5    Koj, A.6    Kordula, T.7
  • 29
    • 24144495591 scopus 로고    scopus 로고
    • Activation of gelatinases by fibrin is a PA/plasmin system-dependent in human glomerular endothelial cells
    • Cai, G., Chen, X., Fu, B., and Lu, Y. Activation of gelatinases by fibrin is a PA/plasmin system-dependent in human glomerular endothelial cells. Mol. Cell. Biochem. 277, 171, 2005.
    • (2005) Mol. Cell. Biochem , vol.277 , pp. 171
    • Cai, G.1    Chen, X.2    Fu, B.3    Lu, Y.4
  • 30
    • 33644814714 scopus 로고    scopus 로고
    • Stimulated tissue plasminogen activator release as a marker of endothelial functions in humans
    • Oliver, J.J., Webb, D., and Newby, D.E. Stimulated tissue plasminogen activator release as a marker of endothelial functions in humans. Arterioscler. Thromb. Vasc. Biol. 25, 2470, 2005.
    • (2005) Arterioscler. Thromb. Vasc. Biol , vol.25 , pp. 2470
    • Oliver, J.J.1    Webb, D.2    Newby, D.E.3
  • 31
    • 0024712236 scopus 로고
    • Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage
    • Dean, D.D., Martel-Pelletier, J., Pelletier, J.P., Howell, D.S., and Woessner, J.F. Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J. Clin. Invest. 84, 678, 1989.
    • (1989) J. Clin. Invest , vol.84 , pp. 678
    • Dean, D.D.1    Martel-Pelletier, J.2    Pelletier, J.P.3    Howell, D.S.4    Woessner, J.F.5
  • 32
    • 0025979486 scopus 로고
    • In vitro effects of interleukin 1 on the synthesis of metalloproteinases, TIMP, plasminogen activators and inhibitors in human articular cartilage
    • Martel-Pelletier, J., Zafarullah, M., Kodama, S., and Pelletier, J. P. In vitro effects of interleukin 1 on the synthesis of metalloproteinases, TIMP, plasminogen activators and inhibitors in human articular cartilage. J. Rheumatol. Suppl. 27, 80, 1991.
    • (1991) J. Rheumatol. Suppl , vol.27 , pp. 80
    • Martel-Pelletier, J.1    Zafarullah, M.2    Kodama, S.3    Pelletier, J.P.4
  • 33
    • 5044226624 scopus 로고    scopus 로고
    • Mechanical properties, proteolytic degradability and biological modifications affect angiogenic process extension into native and modified fibrin matrices in vitro
    • Urech, L., Bittermann, A.G., Hubbell, J.A., and Hall, Heike. Mechanical properties, proteolytic degradability and biological modifications affect angiogenic process extension into native and modified fibrin matrices in vitro. Biomaterials 26, 1369, 2005.
    • (2005) Biomaterials , vol.26 , pp. 1369
    • Urech, L.1    Bittermann, A.G.2    Hubbell, J.A.3    Hall, H.4
  • 34
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • Hiraoka, N., Allen, E., Apel, I.J., Gyetko, M.R., and Weiss, S.J. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins. Cell 95, 365, 1998.
    • (1998) Cell , vol.95 , pp. 365
    • Hiraoka, N.1    Allen, E.2    Apel, I.J.3    Gyetko, M.R.4    Weiss, S.J.5
  • 35
    • 0034693163 scopus 로고    scopus 로고
    • Matrix metalloproteinases collagenase-3, and membrane type 1- matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII
    • Hiller, O., Lichte, A., Oberpichler, A., Kocourek, A., and Tschesche, H. Matrix metalloproteinases collagenase-3, and membrane type 1- matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII. J. Biol. Chem. 275, 33008, 2000.
    • (2000) J. Biol. Chem , vol.275 , pp. 33008
    • Hiller, O.1    Lichte, A.2    Oberpichler, A.3    Kocourek, A.4    Tschesche, H.5
  • 37
    • 28444482853 scopus 로고    scopus 로고
    • The effect of structural alterations of PEG-fibrinogen hydrogel scaffolds on 3-D cellular morphology and cellular migration
    • Dikovsky, D., Bianco-Peled, H., and Seliktar, D. The effect of structural alterations of PEG-fibrinogen hydrogel scaffolds on 3-D cellular morphology and cellular migration. Biomaterials 27, 1496, 2006.
    • (2006) Biomaterials , vol.27 , pp. 1496
    • Dikovsky, D.1    Bianco-Peled, H.2    Seliktar, D.3
  • 38
    • 33646924543 scopus 로고    scopus 로고
    • Isolation of mesenchymal stem cells form G-CSF-mobilized human peripheral blood using fibrin microbeads
    • Kassis, I., Zangi, L., Levdansky, L., Samuel, S., Marx, G., and Gorodetsky, R. Isolation of mesenchymal stem cells form G-CSF-mobilized human peripheral blood using fibrin microbeads. Bone Marrow Transplant. 37, 967, 2006.
    • (2006) Bone Marrow Transplant , vol.37 , pp. 967
    • Kassis, I.1    Zangi, L.2    Levdansky, L.3    Samuel, S.4    Marx, G.5    Gorodetsky, R.6
  • 40
    • 0242302366 scopus 로고    scopus 로고
    • Transforming growth factor β1 inhibits tumor growth in a mouse melanoma model by down-regulating the plasminogen activation system
    • Ramont, L., Pasco, S., Hornebeck, W., Maquart, F.X., and Monboisse, J.C. Transforming growth factor β1 inhibits tumor growth in a mouse melanoma model by down-regulating the plasminogen activation system. Exp. Cell. Res. 291, 1, 2003.
    • (2003) Exp. Cell. Res , vol.291 , pp. 1
    • Ramont, L.1    Pasco, S.2    Hornebeck, W.3    Maquart, F.X.4    Monboisse, J.C.5
  • 41
    • 9644310212 scopus 로고    scopus 로고
    • Direct-acting fibrinolytic enzymes in shark cartilage extract: Potential therapeutic role in vascular disorders
    • Ratel, D., Glazier, G., Provencal, M., Boivin, D., Beaulieu, E., Gingras, D., and Beliveau, R. Direct-acting fibrinolytic enzymes in shark cartilage extract: potential therapeutic role in vascular disorders. Thromb. Res. 115, 143, 2005.
    • (2005) Thromb. Res , vol.115 , pp. 143
    • Ratel, D.1    Glazier, G.2    Provencal, M.3    Boivin, D.4    Beaulieu, E.5    Gingras, D.6    Beliveau, R.7
  • 42
    • 0028945629 scopus 로고
    • ECM degradation by cultured human mesangial cells is mediated by a PA/plasmin/MMP-2 cascade
    • Baricos, W.H., Cortez, S.L., El-Dahr, S.S., and Schnaper, H.W. ECM degradation by cultured human mesangial cells is mediated by a PA/plasmin/MMP-2 cascade. Kidney Int. 47, 1039, 1995.
    • (1995) Kidney Int , vol.47 , pp. 1039
    • Baricos, W.H.1    Cortez, S.L.2    El-Dahr, S.S.3    Schnaper, H.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.