메뉴 건너뛰기




Volumn 49, Issue 4, 2000, Pages 448-459

Mouse fibroblasts in long-term culture within collagen three-dimensional scaffolds: Influence of crosslinking with diphenylphosphorylazide on matrix reorganization, growth, and biosynthetic and proteolytic activities

Author keywords

Collagen scaffold; Crosslinking with diphenylphosphorylazide; Matrix metalloproteinase activity; Mouse fibroblast; Protein synthesis; Tissue engineering

Indexed keywords

ANIMAL CELL CULTURE; BIOSYNTHESIS; CALCIFICATION (BIOCHEMISTRY); CATALYST ACTIVITY; COLLAGEN; CROSSLINKING; ENZYMES; GELS; PHOSPHORUS COMPOUNDS;

EID: 0034653218     PISSN: 00219304     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4636(20000315)49:4<448::AID-JBM3>3.0.CO;2-L     Document Type: Article
Times cited : (102)

References (40)
  • 2
    • 0027955331 scopus 로고
    • Fibroblasts, myofibroblasts and wound contraction
    • Grinnell F. Fibroblasts, myofibroblasts and wound contraction. J Cell Biol 1994;124:401-404.
    • (1994) J Cell Biol , vol.124 , pp. 401-404
    • Grinnell, F.1
  • 3
    • 0020965752 scopus 로고
    • The contraction of collagen matrices by dermal fibroblasts
    • Allen TD, Schor SL. The contraction of collagen matrices by dermal fibroblasts. J Ultrastruct Res 1983;83:205-219.
    • (1983) J Ultrastruct Res , vol.83 , pp. 205-219
    • Allen, T.D.1    Schor, S.L.2
  • 4
    • 0024006111 scopus 로고
    • Quantitative evaluation of the factors affecting the process of fibroblast-mediated collagen contraction by separating the process into three phases
    • Nishiyama T, Tominaga N, Nakajima K, Hayashi T. Quantitative evaluation of the factors affecting the process of fibroblast-mediated collagen contraction by separating the process into three phases. Collagen Rel Res 1988;8:259-273.
    • (1988) Collagen Rel Res , vol.8 , pp. 259-273
    • Nishiyama, T.1    Tominaga, N.2    Nakajima, K.3    Hayashi, T.4
  • 5
    • 0024573550 scopus 로고
    • Physiological variables affecting collagen lattice contraction by human dermal fibroblasts
    • Ehrlich HP, Buttle DJ, Bernanke DH. Physiological variables affecting collagen lattice contraction by human dermal fibroblasts. Exp Mol Pathol 1989;50:220-229.
    • (1989) Exp Mol Pathol , vol.50 , pp. 220-229
    • Ehrlich, H.P.1    Buttle, D.J.2    Bernanke, D.H.3
  • 7
    • 0023498519 scopus 로고
    • Modulation of cellular biosynthetic activity in the retracting collagen lattice
    • Paye M, Nusgens B, Lapiere C. Modulation of cellular biosynthetic activity in the retracting collagen lattice. Eur J Cell Biol 1987;45:44-50.
    • (1987) Eur J Cell Biol , vol.45 , pp. 44-50
    • Paye, M.1    Nusgens, B.2    Lapiere, C.3
  • 8
    • 0024436719 scopus 로고
    • Long-term culture of fibroblasts in contracted collagen gels: Effect on cell growth and biosynthetic activity
    • Nakagawa S, Pawelek P, Grinnell F. Long-term culture of fibroblasts in contracted collagen gels: Effect on cell growth and biosynthetic activity. J Invest Dermatol 1989;93:792-798.
    • (1989) J Invest Dermatol , vol.93 , pp. 792-798
    • Nakagawa, S.1    Pawelek, P.2    Grinnell, F.3
  • 9
    • 0024594492 scopus 로고
    • Mechanical confinement inhibits collagen synthesis in gel-cultured fibroblasts
    • Thie M, Schlumberger W, Rauterberg J, Robenek H. Mechanical confinement inhibits collagen synthesis in gel-cultured fibroblasts. Eur J Cell Biol 1989;48:294-302.
    • (1989) Eur J Cell Biol , vol.48 , pp. 294-302
    • Thie, M.1    Schlumberger, W.2    Rauterberg, J.3    Robenek, H.4
  • 11
    • 0028979348 scopus 로고
    • Integrin α2β1 is a positive regulator of collagenase (MMP-) and collagen α1(I) gene expression
    • Riikonen T, Westermarck J, Koivisto L, Broberg A, Kähäri VM, Heino J. Integrin α2β1 is a positive regulator of collagenase (MMP-) and collagen α1(I) gene expression. J Biol Chem 1995; 270:13548-13552.
    • (1995) J Biol Chem , vol.270 , pp. 13548-13552
    • Riikonen, T.1    Westermarck, J.2    Koivisto, L.3    Broberg, A.4    Kähäri, V.M.5    Heino, J.6
  • 12
    • 0031048384 scopus 로고    scopus 로고
    • 2 integrin and collagenase mRNA expression
    • 2 integrin and collagenase mRNA expression. J Cell Biol 1997;136:473-483.
    • (1997) J Cell Biol , vol.136 , pp. 473-483
    • Xu, J.1    Clark, R.A.F.2
  • 13
    • 0028067549 scopus 로고
    • Activation of 72-kDa type IV collagenase/ gelatinase by normal fibroblasts in collagen lattices is mediated by integrin receptors but is not related to lattice contraction
    • Seltzer JL, Lee AY, Akers KT, Sudbeck B, Southon EA, Wayner EA, Eisen AZ. Activation of 72-kDa type IV collagenase/ gelatinase by normal fibroblasts in collagen lattices is mediated by integrin receptors but is not related to lattice contraction. Exp Cell Res 1994;213;365-374.
    • (1994) Exp Cell Res , vol.213 , pp. 365-374
    • Seltzer, J.L.1    Lee, A.Y.2    Akers, K.T.3    Sudbeck, B.4    Southon, E.A.5    Wayner, E.A.6    Eisen, A.Z.7
  • 14
    • 0027007547 scopus 로고
    • Cell growth on collagen: A review of tissue engineering using scaffolds containing extracellular matrix
    • Silver FH, Pins G. Cell growth on collagen: A review of tissue engineering using scaffolds containing extracellular matrix. J Long-Term Effects Med Implants 1992;2:67-80.
    • (1992) J Long-Term Effects Med Implants , vol.2 , pp. 67-80
    • Silver, F.H.1    Pins, G.2
  • 15
    • 0027595948 scopus 로고
    • Tissue engineering
    • Langer R, Vacanti JP. Tissue engineering. Science 1993;260:920-926.
    • (1993) Science , vol.260 , pp. 920-926
    • Langer, R.1    Vacanti, J.P.2
  • 16
    • 0007739688 scopus 로고    scopus 로고
    • Collagen-based biomaterials and tissue engineering
    • Walenkamp GHIM, editor. Stuttgart and New York: Georg Thieme Verlag
    • Chevallay B, Roche S, Herbage D. Collagen-based biomaterials and tissue engineering. In: Walenkamp GHIM, editor. Biomaterials in surgery. Stuttgart and New York: Georg Thieme Verlag; 1998. p 3-10.
    • (1998) Biomaterials in Surgery , pp. 3-10
    • Chevallay, B.1    Roche, S.2    Herbage, D.3
  • 17
    • 0024095910 scopus 로고
    • Structure of a collagen-GAG dermal skin substitute optimized for cultured human epidermal keratinocytes
    • Boyce ST, Christianson DJ, Hansbrough JF. Structure of a collagen-GAG dermal skin substitute optimized for cultured human epidermal keratinocytes. J Biomed Mater Res 1988;22:939-957.
    • (1988) J Biomed Mater Res , vol.22 , pp. 939-957
    • Boyce, S.T.1    Christianson, D.J.2    Hansbrough, J.F.3
  • 18
    • 0023996345 scopus 로고
    • Porous collagen sponge wound dressings: In vivo and in vitro studies
    • Doillon CJ. Porous collagen sponge wound dressings: in vivo and in vitro studies. J Biomater Appl 1988;2:562-577.
    • (1988) J Biomater Appl , vol.2 , pp. 562-577
    • Doillon, C.J.1
  • 19
    • 0025119616 scopus 로고
    • Influence of glycosaminoglycans on the collagen sponge component of a bilayer artificial skin
    • Matsuda K, Suzuki S, Isshiki N, Yoshioka K, Okada T, Ikada Y. Influence of glycosaminoglycans on the collagen sponge component of a bilayer artificial skin. Biomaterials 1990;11:351-355.
    • (1990) Biomaterials , vol.11 , pp. 351-355
    • Matsuda, K.1    Suzuki, S.2    Isshiki, N.3    Yoshioka, K.4    Okada, T.5    Ikada, Y.6
  • 20
    • 0025266969 scopus 로고
    • Biologically active analogues of the extracellular matrix, artificial skin and nerves
    • Yannas IV. Biologically active analogues of the extracellular matrix, artificial skin and nerves. Angew Chem Int Ed Engl 1990;29:20-35.
    • (1990) Angew Chem Int Ed Engl , vol.29 , pp. 20-35
    • Yannas, I.V.1
  • 22
    • 0028926140 scopus 로고
    • Adherence, proliferation and collagen turnover by human fibroblasts seeded into different types of collagen sponge
    • Middelkoop E, de Vries HJC, Ruuls L, Everts V, Wildevuur CHR, Westerhof W. Adherence, proliferation and collagen turnover by human fibroblasts seeded into different types of collagen sponge. Cell Tissue Res 1995;280:447-453.
    • (1995) Cell Tissue Res , vol.280 , pp. 447-453
    • Middelkoop, E.1    De Vries, H.J.C.2    Ruuls, L.3    Everts, V.4    Wildevuur, C.H.R.5    Westerhof, W.6
  • 23
    • 0030245676 scopus 로고    scopus 로고
    • Deposition of collagen fibril bundles by long-term culture of fibroblasts in collagen sponge
    • Berthod F., Sahuc F, Hayek D, Damour O, Collombel C. Deposition of collagen fibril bundles by long-term culture of fibroblasts in collagen sponge. J Biomed Mater Res 1996;32:87-93.
    • (1996) J Biomed Mater Res , vol.32 , pp. 87-93
    • Berthod, F.1    Sahuc, F.2    Hayek, D.3    Damour, O.4    Collombel, C.5
  • 24
    • 0026606757 scopus 로고
    • Collagen engineering for biomaterial use
    • Miyata T, Taria T, Noishiki Y. Collagen engineering for biomaterial use. Clin Mater 1992;9:139-148.
    • (1992) Clin Mater , vol.9 , pp. 139-148
    • Miyata, T.1    Taria, T.2    Noishiki, Y.3
  • 25
    • 0030112435 scopus 로고    scopus 로고
    • Application of slow-resorbing collagen membrane to periodontal and peri-implant guided tissue regeneration
    • Parodi R, Santarelli G, Carusi G. Application of slow-resorbing collagen membrane to periodontal and peri-implant guided tissue regeneration. Int J Periodont Rest Dent 1996;16:175-185.
    • (1996) Int J Periodont Rest Dent , vol.16 , pp. 175-185
    • Parodi, R.1    Santarelli, G.2    Carusi, G.3
  • 26
    • 0031204865 scopus 로고    scopus 로고
    • Guided tissue regeneration using a collagen membrane in chronic adult and rapidly progressive periodontitis patients in the treatment of 3-wall intrabony defects
    • Benqué E, Zahedi S, Brocard D, Oscaby F, Justumus P, Brunel G. Guided tissue regeneration using a collagen membrane in chronic adult and rapidly progressive periodontitis patients in the treatment of 3-wall intrabony defects. J Clin Periodont 1997;24:544-549.
    • (1997) J Clin Periodont , vol.24 , pp. 544-549
    • Benqué, E.1    Zahedi, S.2    Brocard, D.3    Oscaby, F.4    Justumus, P.5    Brunel, G.6
  • 27
    • 0025388772 scopus 로고
    • Use of the acyl azide method for crosslinking collagen-rich tissues such as pericardium
    • Petite H, Rault I, Huc A, Menasche P, Herbage D. Use of the acyl azide method for crosslinking collagen-rich tissues such as pericardium. J Biomed Mater Res 1990;24:179-187.
    • (1990) J Biomed Mater Res , vol.24 , pp. 179-187
    • Petite, H.1    Rault, I.2    Huc, A.3    Menasche, P.4    Herbage, D.5
  • 28
    • 0028372260 scopus 로고
    • Use of diphenylphosphorylazide for crosslinking collagen-based biomaterials
    • Petite H, Frei V, Hue A, Herbage D. Use of diphenylphosphorylazide for crosslinking collagen-based biomaterials. J Biomed Mater Res 1994;28:159-165.
    • (1994) J Biomed Mater Res , vol.28 , pp. 159-165
    • Petite, H.1    Frei, V.2    Hue, A.3    Herbage, D.4
  • 29
    • 0029361194 scopus 로고
    • Cytocompatibility of calf pericardium treated by glutaraldehyde and by the acyl azide methods in an organotypic culture model
    • Petite H, Duval JL, Frei V, Abdul-Malak N, Sigot-Luizard MF, Herbage D. Cytocompatibility of calf pericardium treated by glutaraldehyde and by the acyl azide methods in an organotypic culture model. Biomaterials 1995;16:1003-1008.
    • (1995) Biomaterials , vol.16 , pp. 1003-1008
    • Petite, H.1    Duval, J.L.2    Frei, V.3    Abdul-Malak, N.4    Sigot-Luizard, M.F.5    Herbage, D.6
  • 30
    • 0030130294 scopus 로고    scopus 로고
    • Evaluation of different chemical methods for crosslinking collagen gel, films and sponges
    • Rault I, Frei V, Herbage D, Abdul-Malak N, Hue A. Evaluation of different chemical methods for crosslinking collagen gel, films and sponges. J Mater Sci: Mater Med 1996;7:215-221.
    • (1996) J Mater Sci: Mater Med , vol.7 , pp. 215-221
    • Rault, I.1    Frei, V.2    Herbage, D.3    Abdul-Malak, N.4    Hue, A.5
  • 31
    • 0027575138 scopus 로고
    • In vitro evaluation of cell/biomaterial interaction by MTT assay
    • Ciapetti G, Cenni E, Pratelli L, Pizzoferrato A. In vitro evaluation of cell/biomaterial interaction by MTT assay. Biomaterials 1993;14:359-364.
    • (1993) Biomaterials , vol.14 , pp. 359-364
    • Ciapetti, G.1    Cenni, E.2    Pratelli, L.3    Pizzoferrato, A.4
  • 32
    • 0018175944 scopus 로고
    • Aminoterminal extension peptides from type I procollagen normalize excessive collagen synthesis of scleroderma fibroblasts
    • Krieg T, Hörlein D, Wiestner M, Müller PK. Aminoterminal extension peptides from type I procollagen normalize excessive collagen synthesis of scleroderma fibroblasts. Arch Dermatol Res 1978;2631:171-180.
    • (1978) Arch Dermatol Res , vol.2631 , pp. 171-180
    • Krieg, T.1    Hörlein, D.2    Wiestner, M.3    Müller, P.K.4
  • 33
    • 0022834093 scopus 로고
    • Direct extraction and assay of bone tissue collagenase and its relation to parathyroid-hormone-induced bone resorption
    • Eeckhout Y, Delaissé JM, Vaes GM. Direct extraction and assay of bone tissue collagenase and its relation to parathyroid-hormone-induced bone resorption. Biochem J 1986;239:793-796.
    • (1986) Biochem J , vol.239 , pp. 793-796
    • Eeckhout, Y.1    Delaissé, J.M.2    Vaes, G.M.3
  • 34
    • 0031039965 scopus 로고    scopus 로고
    • Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases
    • Butler GS, Will H, Atkinson SJ, Murphy G. Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases. Eur J Biochem 1997;244:653-657.
    • (1997) Eur J Biochem , vol.244 , pp. 653-657
    • Butler, G.S.1    Will, H.2    Atkinson, S.J.3    Murphy, G.4
  • 35
    • 0026487642 scopus 로고
    • In vitro contraction rate of collagen in sponge-shape matrices
    • Côté MF, Sirois E, Doillon CJ. In vitro contraction rate of collagen in sponge-shape matrices. J Biomater Sci, Polym Edn 1992;3:301-313.
    • (1992) J Biomater Sci, Polym Edn , vol.3 , pp. 301-313
    • Côté, M.F.1    Sirois, E.2    Doillon, C.J.3
  • 36
    • 0025486278 scopus 로고
    • Biochemical changes and cytotoxicity associated with the degradation of polymeric glutaraldehyde-derived crosslinks and dimethylsuberimidate
    • Huang-Lee LLH, Cheung DT, Nimni M. Biochemical changes and cytotoxicity associated with the degradation of polymeric glutaraldehyde-derived crosslinks and dimethylsuberimidate. J Biomed Mater Res 1990;24:1185-1201.
    • (1990) J Biomed Mater Res , vol.24 , pp. 1185-1201
    • Huang-Lee, L.L.H.1    Cheung, D.T.2    Nimni, M.3
  • 40
    • 0040945730 scopus 로고    scopus 로고
    • Differential effects of transforming growth factor-β on the expression of collagenase-1 and collagenase-3 in human fibroblasts
    • Uria JA, Jimenez M, Balbin M, Freije J, Lopez-Otin C. Differential effects of transforming growth factor-β on the expression of collagenase-1 and collagenase-3 in human fibroblasts. J Biol Chem 1998;273:9769-9777.
    • (1998) J Biol Chem , vol.273 , pp. 9769-9777
    • Uria, J.A.1    Jimenez, M.2    Balbin, M.3    Freije, J.4    Lopez-Otin, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.