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Volumn 237, Issue 10, 2008, Pages 2705-2715

Human primary corneal fibroblasts synthesize and deposit proteoglycans in long-term 3-D cultures

Author keywords

3 D culture; Glycosaminoglycans; Human fibroblasts; Microscopy; Proteoglycans

Indexed keywords

BIGLYCAN; COLLAGEN; COLLAGEN TYPE 1; DECORIN; GLYCOSAMINOGLYCAN; LUMICAN; LYASE; MIMECAN; PERLECAN; PROTEOGLYCAN; SYNDECAN 4;

EID: 54549110133     PISSN: 10588388     EISSN: 10970177     Source Type: Journal    
DOI: 10.1002/dvdy.21606     Document Type: Article
Times cited : (65)

References (40)
  • 1
    • 0019825707 scopus 로고
    • Corneal and scleral collagen fiber formation in vitro
    • Birk DE, Lande MA. 1981. Corneal and scleral collagen fiber formation in vitro. BiochimBiophys Acta 670:362-369.
    • (1981) BiochimBiophys Acta , vol.670 , pp. 362-369
    • Birk, D.E.1    Lande, M.A.2
  • 2
    • 34347331204 scopus 로고    scopus 로고
    • Injury and nucleotides induce phosphorylation of epidermal growth factor receptor: MMP and HB-EGF dependent pathway
    • Boucher I, Yang L, Mayo C, Klepeis V, Trinkaus-Randall V. 2007. Injury and nucleotides induce phosphorylation of epidermal growth factor receptor: MMP and HB-EGF dependent pathway. Exp Eye Res 85:130-141.
    • (2007) Exp Eye Res , vol.85 , pp. 130-141
    • Boucher, I.1    Yang, L.2    Mayo, C.3    Klepeis, V.4    Trinkaus-Randall, V.5
  • 4
    • 0033548618 scopus 로고    scopus 로고
    • Characterization of proteoglycans synthesized by cultured corneal fibroblasts in response to transforming growth factor beta and fetal calf serum
    • Brown CT, Nugent MA, Lau FW, Trinkaus-Randall V. 1999. Characterization of proteoglycans synthesized by cultured corneal fibroblasts in response to transforming growth factor beta and fetal calf serum. J Biol Chem 274:7111-7119.
    • (1999) J Biol Chem , vol.274 , pp. 7111-7119
    • Brown, C.T.1    Nugent, M.A.2    Lau, F.W.3    Trinkaus-Randall, V.4
  • 5
  • 7
    • 0018075307 scopus 로고
    • Biochemical and ultrastructural changes in collagen during corneal wound healing
    • Cintron C, Hassinger LC, Kublin CL, Cannon DJ. 1978. Biochemical and ultrastructural changes in collagen during corneal wound healing. J Ultrastruct Res 65:13-22.
    • (1978) J Ultrastruct Res , vol.65 , pp. 13-22
    • Cintron, C.1    Hassinger, L.C.2    Kublin, C.L.3    Cannon, D.J.4
  • 11
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV. 1997. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol 136:729-743.
    • (1997) J Cell Biol , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 12
    • 0024599079 scopus 로고
    • Proteoglycans of rabbit corneas with nonperforating wounds
    • Funderburgh JL, Chandler JW. 1989. Proteoglycans of rabbit corneas with nonperforating wounds. Invest Ophthalmol Vis Sci 30:435-442.
    • (1989) Invest Ophthalmol Vis Sci , vol.30 , pp. 435-442
    • Funderburgh, J.L.1    Chandler, J.W.2
  • 14
    • 0027280398 scopus 로고
    • Sequence and structural implications of a bovine keratan sulfate proteoglycan core protein. Protein 37B represents bovine lumican and proteins 37A and 25 are unique
    • Funderburgh JL, Funderburgh ML, Brown SJ, Vergnes JP, Hassell JR, Mann MM, Conrad GQ. 1993. Sequence and structural implications of a bovine keratan sulfate proteoglycan core protein. Protein 37B represents bovine lumican and proteins 37A and 25 are unique. J Biol Chem 268:11874-11880.
    • (1993) J Biol Chem , vol.268 , pp. 11874-11880
    • Funderburgh, J.L.1    Funderburgh, M.L.2    Brown, S.J.3    Vergnes, J.P.4    Hassell, J.R.5    Mann, M.M.6    Conrad, G.Q.7
  • 16
    • 0026446354 scopus 로고
    • Age-related changes of sulfated proteoglycans in the normal human trabecular meshwork
    • Gong H, Freddo TF, Johnson M. 1992. Age-related changes of sulfated proteoglycans in the normal human trabecular meshwork. Exp Eye Res 55:691-709.
    • (1992) Exp Eye Res , vol.55 , pp. 691-709
    • Gong, H.1    Freddo, T.F.2    Johnson, M.3
  • 17
    • 35148841944 scopus 로고    scopus 로고
    • Morphologic characterization of organized extracellular matrix deposition by ascorbic acid-stimulated human corneal fibroblasts
    • Guo X, Hutcheon AE, Melotti SA, Zieske JD, Trinkaus-Randall V, Ruberti JW. 2007. Morphologic characterization of organized extracellular matrix deposition by ascorbic acid-stimulated human corneal fibroblasts. Invest Ophthalmol Vis Sci 48:4056-4060.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 4056-4060
    • Guo, X.1    Hutcheon, A.E.2    Melotti, S.A.3    Zieske, J.D.4    Trinkaus-Randall, V.5    Ruberti, J.W.6
  • 18
    • 0020560664 scopus 로고
    • Proteoglycan changes during restoration of transparency in corneal scars
    • Hassell JR, Cintron C, Kublin C, Newsome DA. 1983. Proteoglycan changes during restoration of transparency in corneal scars. Arch Biochem Biophys 222:362-369.
    • (1983) Arch Biochem Biophys , vol.222 , pp. 362-369
    • Hassell, J.R.1    Cintron, C.2    Kublin, C.3    Newsome, D.A.4
  • 19
    • 20744439516 scopus 로고    scopus 로고
    • The mesenchymal cell, its role in the embryo, and the remarkable signaling mechanims that creat it
    • Hay Elizabeth D. 2005. The mesenchymal cell, its role in the embryo, and the remarkable signaling mechanims that creat it. Dev Dyn 233:706-720.
    • (2005) Dev Dyn , vol.233 , pp. 706-720
    • Hay Elizabeth, D.1
  • 21
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo RV. 1998. Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 67:609-652.
    • (1998) Annu Rev Biochem , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 23
    • 2142748942 scopus 로고
    • Stimulation of extracellular matrix synthesis in the developing cornea by glycosaminoglycans
    • Meier S, Hay Elizabeth D. 1974. Stimulation of extracellular matrix synthesis in the developing cornea by glycosaminoglycans. Proc Nat Acad Sci 71:2310-2313.
    • (1974) Proc Nat Acad Sci , vol.71 , pp. 2310-2313
    • Meier, S.1    Hay Elizabeth, D.2
  • 24
    • 0024493131 scopus 로고
    • Analysis of the proteoglycans synthesized by corneal explants from embryonic chicken. II. Structural characterization of the keratan sulfate and dermatan sulfate proteoglycans from corneal stroma
    • Midura RJ, Hascall VC. 1989. Analysis of the proteoglycans synthesized by corneal explants from embryonic chicken. II. Structural characterization of the keratan sulfate and dermatan sulfate proteoglycans from corneal stroma. J Biol Chem 264:1423-1430.
    • (1989) J Biol Chem , vol.264 , pp. 1423-1430
    • Midura, R.J.1    Hascall, V.C.2
  • 25
    • 34447136376 scopus 로고    scopus 로고
    • Characterization and distribution of hyaluronan and the proteoglycans decorin, biglycan and perlecan in the developing embryonic mouse gonad
    • Miqueloto CA, Zorn TM. 2007. Characterization and distribution of hyaluronan and the proteoglycans decorin, biglycan and perlecan in the developing embryonic mouse gonad. J Anat 211:16-25.
    • (2007) J Anat , vol.211 , pp. 16-25
    • Miqueloto, C.A.1    Zorn, T.M.2
  • 26
    • 0842331844 scopus 로고    scopus 로고
    • A new three-dimensional model of the organization of proteoglycans and collagen fibrils in the human corneal stroma
    • Müller LJ, Pels E, Schurmans LR, Vrensen GF. 2004. A new three-dimensional model of the organization of proteoglycans and collagen fibrils in the human corneal stroma. Exp Eye Res 78:493-501.
    • (2004) Exp Eye Res , vol.78 , pp. 493-501
    • Müller, L.J.1    Pels, E.2    Schurmans, L.R.3    Vrensen, G.F.4
  • 28
    • 33646370762 scopus 로고    scopus 로고
    • Big-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation and participates in ternary complexing with these macromolecules
    • Reinboth Betty, Thomas John, Hanssen Eric, Gibson Mark A. 2006. Big-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation and participates in ternary complexing with these macromolecules. J Biol Chem 281:7816-7824.
    • (2006) J Biol Chem , vol.281 , pp. 7816-7824
    • Betty, R.1    John, T.2    Hanssen Eric, G.M.A.3
  • 29
    • 84885165215 scopus 로고    scopus 로고
    • Ruberti J, Zieske JD, Trinkaus-Randall V. 2007. Corneal tissue replacement. In: Lanza, Langer, Vacanti, editors. Principles of tissue engineering, 68. Elsevier. p 1021-1043.
    • Ruberti J, Zieske JD, Trinkaus-Randall V. 2007. Corneal tissue replacement. In: Lanza, Langer, Vacanti, editors. Principles of tissue engineering, vol. 68. Elsevier. p 1021-1043.
  • 30
    • 0029809861 scopus 로고    scopus 로고
    • Human corneal fibrillogenesis. Collagen V structural analysis and fibrillar assembly by stromal fibroblasts in culture
    • Ruggiero F, Burillon C, Garrone R. 1996. Human corneal fibrillogenesis. Collagen V structural analysis and fibrillar assembly by stromal fibroblasts in culture. Invest Ophthalmol Vis Sci 37:1749-1760.
    • (1996) Invest Ophthalmol Vis Sci , vol.37 , pp. 1749-1760
    • Ruggiero, F.1    Burillon, C.2    Garrone, R.3
  • 31
    • 0023810860 scopus 로고
    • Identification of specific binding sites for keratan sulphate proteoglycans and chondroitindermatan sulphate proteoglycans on collagen fibrils in cornea by the use of cupromeronic blue in 'critical-electrolyte-concentration' techniques
    • Scott JE, Haigh M. 1988. Identification of specific binding sites for keratan sulphate proteoglycans and chondroitindermatan sulphate proteoglycans on collagen fibrils in cornea by the use of cupromeronic blue in 'critical-electrolyte-concentration' techniques. Biochem J 253:607-610.
    • (1988) Biochem J , vol.253 , pp. 607-610
    • Scott, J.E.1    Haigh, M.2
  • 32
    • 33744965090 scopus 로고    scopus 로고
    • Crystal structure of the Biglycan dimer and evidence that dimerization is essential for folding and stability of class I small leucine-rich repeat proteoglycans
    • Scott PG, Dodd CM, Bergmann EM, Sheehan JK, Bishop PN. 2006. Crystal structure of the Biglycan dimer and evidence that dimerization is essential for folding and stability of class I small leucine-rich repeat proteoglycans. J Biol Chem 281:13324-13332.
    • (2006) J Biol Chem , vol.281 , pp. 13324-13332
    • Scott, P.G.1    Dodd, C.M.2    Bergmann, E.M.3    Sheehan, J.K.4    Bishop, P.N.5
  • 34
    • 0021234218 scopus 로고
    • Analysis of the role of microfilaments and microtubules in acquisition of bipolarity and elongation of fibroblasts in hydrated collagen gels
    • Tomasek JJ, Hay ED. 1984. Analysis of the role of microfilaments and microtubules in acquisition of bipolarity and elongation of fibroblasts in hydrated collagen gels. J Cell Biol 99:536-549.
    • (1984) J Cell Biol , vol.99 , pp. 536-549
    • Tomasek, J.J.1    Hay, E.D.2
  • 35
    • 0019977865 scopus 로고
    • Collagen modulates cell shape and cytoskeleton of embryonic corneal and fibroma fibroblasts: Distribution of actin, a-actinin, and myosin
    • Tomasek JJ, Hay ED, Fujiwara K. 1982. Collagen modulates cell shape and cytoskeleton of embryonic corneal and fibroma fibroblasts: distribution of actin, a-actinin, and myosin. Dev Biol 92:107-122.
    • (1982) Dev Biol , vol.92 , pp. 107-122
    • Tomasek, J.J.1    Hay, E.D.2    Fujiwara, K.3
  • 36
    • 54549086020 scopus 로고    scopus 로고
    • nd ed. Academic Press. p 471-491.
    • nd ed. Academic Press. p 471-491.
  • 37
    • 0021261946 scopus 로고
    • Role of calcium and calmodulin in hemidesmosome formation in vitro
    • Trinkaus-Randall V, Gipson IK. 1984. Role of calcium and calmodulin in hemidesmosome formation in vitro. J Cell Biol 98:1565-1571.
    • (1984) J Cell Biol , vol.98 , pp. 1565-1571
    • Trinkaus-Randall, V.1    Gipson, I.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.