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Volumn 4, Issue 6, 2003, Pages 479-489

Fibulins: A versatile family of extracellular matrix proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANAPHYLATOXIN; ARGINYLGLYCYLASPARTIC ACID; CALCIUM BINDING PROTEIN; ENTACTIN; EPIDERMAL GROWTH FACTOR; FIBRILLIN; FIBRONECTIN; FIBULIN; FIBULIN 1; FIBULIN 2; FIBULIN 3; FIBULIN 4; FIBULIN 5; LAMININ; MEMBRANE PROTEIN; PERLECAN; PROTEOGLYCAN; SCLEROPROTEIN; TROPOELASTIN; UNCLASSIFIED DRUG;

EID: 0037686257     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1130     Document Type: Review
Times cited : (411)

References (89)
  • 1
    • 0024339149 scopus 로고
    • Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain
    • Argraves, W. S., Dickerson, K., Burgess, W. H. & Ruoslahti, E. Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain. Cell 58, 623-629 (1989).
    • (1989) Cell , vol.58 , pp. 623-629
    • Argraves, W.S.1    Dickerson, K.2    Burgess, W.H.3    Ruoslahti, E.4
  • 2
    • 0025642484 scopus 로고
    • Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure
    • Argraves, W. S., Tran, H., Burgess, W. H. & Dickerson, K. Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure. J. Cell Biol. 111, 3155-3164 (1990). Fibulin-1 is identified and is found to be a new class of ECM protein.
    • (1990) J. Cell Biol. , vol.111 , pp. 3155-3164
    • Argraves, W.S.1    Tran, H.2    Burgess, W.H.3    Dickerson, K.4
  • 3
    • 0025107413 scopus 로고
    • Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum
    • Kluge, M., Mann, K., Dziadek, M. & Timpl, R. Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum. Eur. J. Biochem. 193, 651-659 (1990).
    • (1990) Eur. J. Biochem. , vol.193 , pp. 651-659
    • Kluge, M.1    Mann, K.2    Dziadek, M.3    Timpl, R.4
  • 4
    • 0027227388 scopus 로고
    • Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands
    • Pan, T.-C. et al. Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands. Eur. J. Biochem. 215, 733-740 (1993).
    • (1993) Eur. J. Biochem. , vol.215 , pp. 733-740
    • Pan, T.-C.1
  • 5
    • 0027380642 scopus 로고
    • Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium-binding
    • Pan, T.-C. et al. Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium-binding. J. Cell Biol. 123, 1269-1277 (1993). The first evidence that there is a fibulin protein family that contains different fibulin isoforms.
    • (1993) J. Cell Biol. , vol.123 , pp. 1269-1277
    • Pan, T.-C.1
  • 6
    • 0028136804 scopus 로고
    • Fibulin-2 (FBLN2): Human cDNA sequence, mRNA expression and mapping of the gene on human and mouse chromosomes
    • Zhang, R.-Z. et al. Fibulin-2 (FBLN2): human cDNA sequence, mRNA expression and mapping of the gene on human and mouse chromosomes. Genomics 22, 425-430 (1994).
    • (1994) Genomics , vol.22 , pp. 425-430
    • Zhang, R.-Z.1
  • 7
    • 0029584361 scopus 로고
    • Binding of mouse and human fibulin-2 to extracellular matrix ligands
    • Sasaki, T., Göhring, W., Pan, T.-C., Chu, M.-L. & Timpl, R. Binding of mouse and human fibulin-2 to extracellular matrix ligands. J. Mol. Biol. 254, 892-899 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 892-899
    • Sasaki, T.1    Göhring, W.2    Pan, T.-C.3    Chu, M.-L.4    Timpl, R.5
  • 8
    • 0030977056 scopus 로고    scopus 로고
    • Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge
    • Sasaki, T. et al. Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge. EMBO J. 16, 3035-3043 (1997). The first extensive model of the fibulin-2 structure.
    • (1997) EMBO J. , vol.16 , pp. 3035-3043
    • Sasaki, T.1
  • 9
    • 0030958107 scopus 로고    scopus 로고
    • Human fibulin-1D: Molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin-1 gene family
    • Tran. H., Mattei, M., Godyna, S. & Argraves, W. S. Human Fibulin-1D: molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin-1 gene family. Matrix Biol. 15, 479-493 (1997).
    • (1997) Matrix Biol. , vol.15 , pp. 479-493
    • Tran, H.1    Mattei, M.2    Godyna, S.3    Argraves, W.S.4
  • 10
    • 0032703916 scopus 로고    scopus 로고
    • Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4
    • Giltay, R., Timpl, R. & Kostka, G. Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4. Matrix Biol. 18, 469-480 (1999).
    • (1999) Matrix Biol. , vol.18 , pp. 469-480
    • Giltay, R.1    Timpl, R.2    Kostka, G.3
  • 11
    • 0030693203 scopus 로고    scopus 로고
    • Sequence of zebrafish fibulin-1 and its expression in developing heart and other embryonic organs
    • Zhang, H.-Y., Lardelli, M. & Ekblom, P. Sequence of zebrafish fibulin-1 and its expression in developing heart and other embryonic organs. Dev. Genes Evol. 207, 340-351 (1997).
    • (1997) Dev. Genes Evol. , vol.207 , pp. 340-351
    • Zhang, H.-Y.1    Lardelli, M.2    Ekblom, P.3
  • 12
    • 0032433523 scopus 로고    scopus 로고
    • Identification of chicken and C. elegans fibulin-1 homologs and characterization of the C. elegans fibulin-1 gene
    • Barth, J. L., Argraves, K. M., Roark, E. F., Little, C. D. & Argraves, W. S. Identification of chicken and C. elegans fibulin-1 homologs and characterization of the C. elegans fibulin-1 gene. Matrix Biol. 17, 635-646 (1998).
    • (1998) Matrix Biol. , vol.17 , pp. 635-646
    • Barth, J.L.1    Argraves, K.M.2    Roark, E.F.3    Little, C.D.4    Argraves, W.S.5
  • 14
    • 0028943214 scopus 로고
    • An overexpressed gene transcript in senescent and quiescent human fibroblasts encoding a novel protein in the epidermal growth factor-like repeat family stimulates DNA synthesis
    • Lecka-Czernik, B., Lumpkin, C. K. & Goldstein, S. An overexpressed gene transcript in senescent and quiescent human fibroblasts encoding a novel protein in the epidermal growth factor-like repeat family stimulates DNA synthesis. Mol. Cell. Biol. 15, 120-129 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 120-129
    • Lecka-Czernik, B.1    Lumpkin, C.K.2    Goldstein, S.3
  • 15
    • 0035951381 scopus 로고    scopus 로고
    • Human fibulin-4: Analysis of its biosynthetic processing and mRNA expression in normal and tumour tissues
    • Gallagher, W. M. et al. Human fibulin-4: analysis of its biosynthetic processing and mRNA expression in normal and tumour tissues. FEBS Lett. 489, 59-66 (2001).
    • (2001) FEBS Lett. , vol.489 , pp. 59-66
    • Gallagher, W.M.1
  • 16
    • 0030888219 scopus 로고    scopus 로고
    • Structural and functional aspects of calcium-binding in extracellular matrix proteins
    • Maurer, P. & Hohenester, E. Structural and functional aspects of calcium-binding in extracellular matrix proteins. Matrix Biol. 15, 569-580 (1997).
    • (1997) Matrix Biol. , vol.15 , pp. 569-580
    • Maurer, P.1    Hohenester, E.2
  • 17
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factor-like domains: Implications for the Marfan syndrome and other genetic disorders
    • Downing, A. K. et al. Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders. Cell 85, 597-605 (1996). This paper explains how the structure of cbEGF-like modules is stabilized by calcium ligation.
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1
  • 18
    • 0029808227 scopus 로고    scopus 로고
    • Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by matrix metalloproteinases and other tissue proteases
    • Sasaki, T., Mann, K., Murphy, G., Chu, M.-L. & Timpl, R. Different susceptibilities of fibulin-1 and fibulin-2 to cleavage by matrix metalloproteinases and other tissue proteases. Eur. J. Biochem. 240, 427-434 (1996).
    • (1996) Eur. J. Biochem. , vol.240 , pp. 427-434
    • Sasaki, T.1    Mann, K.2    Murphy, G.3    Chu, M.-L.4    Timpl, R.5
  • 19
    • 0028815977 scopus 로고
    • Structural characterization of two variants of fibulin-1 that differ in nidogen affinity
    • Sasaki, T. et al. Structural characterization of two variants of fibulin-1 that differ in nidogen affinity. J. Mol. Biol. 245, 241-250 (1995).
    • (1995) J. Mol. Biol. , vol.245 , pp. 241-250
    • Sasaki, T.1
  • 20
    • 0028961103 scopus 로고
    • The association of human fibulin-1 with elastic fibers: An immunohistological, ultrastructural, and RNA study
    • Roark, E. F. et al. The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study. J. Histochem. Cytochem. 43, 401-411 (1995).
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 401-411
    • Roark, E.F.1
  • 21
    • 0033027071 scopus 로고    scopus 로고
    • A single EFEMP 1 mutation associated with both Malattia Leventinese and Doyne honeycomb retinal dystrophy
    • Stone, E. M. et al. A single EFEMP1 mutation associated with both Malattia Leventinese and Doyne honeycomb retinal dystrophy. Nature Genet. 22, 199-202 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 199-202
    • Stone, E.M.1
  • 22
    • 0037050030 scopus 로고    scopus 로고
    • Fibulin-5/DANCE is essential for elastogenesis in vivo
    • Nakamura, T. et al. Fibulin-5/DANCE is essential for elastogenesis in vivo. Nature 415, 171-175 (2002).
    • (2002) Nature , vol.415 , pp. 171-175
    • Nakamura, T.1
  • 23
    • 0037049996 scopus 로고    scopus 로고
    • Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo
    • Yanagisawa, H. et al. Fibulin-5 is an elastin-binding protein essential for elastic fibre development in vivo. Nature 415, 168-171 (2002). This work describes, together with reference 22, the role of fibulin-5 in stabilizing elastic fibres.
    • (2002) Nature , vol.415 , pp. 168-171
    • Yanagisawa, H.1
  • 24
    • 0026708249 scopus 로고
    • Fibulin is localized at sites of epithelial - Mesenchymal transitions in the early avian embryo
    • Spence, S. G., Argraves, W. S., Walters, L., Hungerford, J. E. & Little, C. Fibulin is localized at sites of epithelial - mesenchymal transitions in the early avian embryo. Dev. Biol. 151, 473-484 (1992).
    • (1992) Dev. Biol. , vol.151 , pp. 473-484
    • Spence, S.G.1    Argraves, W.S.2    Walters, L.3    Hungerford, J.E.4    Little, C.5
  • 25
    • 0029935171 scopus 로고    scopus 로고
    • Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo
    • Zhang, H.-Y., Timpl, R., Sasaki, T., Chu, M.-L. & Ekblom, P. Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo. Dev. Dyn. 205, 348-364 (1996).
    • (1996) Dev. Dyn. , vol.205 , pp. 348-364
    • Zhang, H.-Y.1    Timpl, R.2    Sasaki, T.3    Chu, M.-L.4    Ekblom, P.5
  • 26
    • 0029932657 scopus 로고    scopus 로고
    • The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo
    • Miosge, N. et al. The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo. Histochem. J. 28, 109-116 (1996).
    • (1996) Histochem. J. , vol.28 , pp. 109-116
    • Miosge, N.1
  • 27
    • 0030587609 scopus 로고    scopus 로고
    • Development of aortic vessel wall as defined by vascular smooth muscle and extracellular matrix markers
    • Hungerford, J. E., Owens, G. K., Argraves, W. S. & Little, C. D. Development of aortic vessel wall as defined by vascular smooth muscle and extracellular matrix markers. Dev. Biol. 178, 375-392 (1996).
    • (1996) Dev. Biol. , vol.178 , pp. 375-392
    • Hungerford, J.E.1    Owens, G.K.2    Argraves, W.S.3    Little, C.D.4
  • 28
    • 0029878173 scopus 로고    scopus 로고
    • Fibulin-1, vitronectin expression during avian cardiac valve and septa development
    • Bouchey, D., Argraves, W. S. & Little, C. D. Fibulin-1, vitronectin expression during avian cardiac valve and septa development. Anat. Rec. 244, 540-551 (1996).
    • (1996) Anat. Rec. , vol.244 , pp. 540-551
    • Bouchey, D.1    Argraves, W.S.2    Little, C.D.3
  • 29
    • 0027461522 scopus 로고
    • The extracellular matrix glycoproteins BM-90 and tenascin are expressed in the mesenchyme at sites of endothelial - Mesenchymal conversion in the embryonic mouse heart
    • Zhang, H.-Y., Kluge, M., Timpl, R., Chu, M.-L. & Ekblom, P. The extracellular matrix glycoproteins BM-90 and tenascin are expressed in the mesenchyme at sites of endothelial - mesenchymal conversion in the embryonic mouse heart. Differentiation 52, 211-220 (1993).
    • (1993) Differentiation , vol.52 , pp. 211-220
    • Zhang, H.-Y.1    Kluge, M.2    Timpl, R.3    Chu, M.-L.4    Ekblom, P.5
  • 30
    • 0028893858 scopus 로고
    • Extracellular matrix protein fibulin-2 is expressed in the embryonic endocardial cushion tissue and is a prominent component of valves in adult heart
    • Zhang, H.-Y. et al. Extracellular matrix protein fibulin-2 is expressed in the embryonic endocardial cushion tissue and is a prominent component of valves in adult heart. Dev. Biol. 167, 18-26 (1995).
    • (1995) Dev. Biol. , vol.167 , pp. 18-26
    • Zhang, H.-Y.1
  • 31
    • 0034873979 scopus 로고    scopus 로고
    • Fibulin-2 expression marks transformed mesenchymal cells in developing cardiac valves, aortic arch vessels and coronary vessels
    • Tsuda, T., Wang, H., Timpl, R. & Chu, M.-L. Fibulin-2 expression marks transformed mesenchymal cells in developing cardiac valves, aortic arch vessels and coronary vessels. Dev. Dyn. 222, 89-100 (2001).
    • (2001) Dev. Dyn. , vol.222 , pp. 89-100
    • Tsuda, T.1    Wang, H.2    Timpl, R.3    Chu, M.-L.4
  • 32
    • 0031842794 scopus 로고    scopus 로고
    • Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations
    • Miosge, N., Sasaki, T., Chu, M.-L., Herken, R. & Timpl, R. Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations. Cell. Mol. Life Sci. 54, 606-613 (1997).
    • (1997) Cell. Mol. Life Sci. , vol.54 , pp. 606-613
    • Miosge, N.1    Sasaki, T.2    Chu, M.-L.3    Herken, R.4    Timpl, R.5
  • 33
    • 0033577993 scopus 로고    scopus 로고
    • MBP1: A novel mutant p53-specific protein partner with oncogenic properties
    • Gallagher, W. M. et al. MBP1: a novel mutant p53-specific protein partner with oncogenic properties. Oncogene 18, 3608-3616 (1999).
    • (1999) Oncogene , vol.18 , pp. 3608-3616
    • Gallagher, W.M.1
  • 34
    • 0033612354 scopus 로고    scopus 로고
    • EVEC A novel epidermal growth factor-like repeat containing protein upregulated in embryonic and injured adult vasulature
    • Kowal, R. C., Richardson, J. A., Miano, J. M. & Olsen, E. N. EVEC. A novel epidermal growth factor-like repeat containing protein upregulated in embryonic and injured adult vasulature. Circ. Res. 84, 1166-1176 (1999).
    • (1999) Circ. Res. , vol.84 , pp. 1166-1176
    • Kowal, R.C.1    Richardson, J.A.2    Miano, J.M.3    Olsen, E.N.4
  • 35
    • 0035096910 scopus 로고    scopus 로고
    • Fibulin-1 binds the amino-terminal head of β-amyloid precursor protein
    • Ohsawa, I., Takamura, C. & Kohsaka, S. Fibulin-1 binds the amino-terminal head of β-amyloid precursor protein. J. Neurochem. 76, 1411-1420 (2001).
    • (2001) J. Neurochem. , vol.76 , pp. 1411-1420
    • Ohsawa, I.1    Takamura, C.2    Kohsaka, S.3
  • 36
    • 0029761338 scopus 로고    scopus 로고
    • Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues
    • Reinhardt, D. P. et al. Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues. J. Biol. Chem. 271, 19489-19496 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 19489-19496
    • Reinhardt, D.P.1
  • 37
    • 0345061697 scopus 로고    scopus 로고
    • Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins
    • Sasaki, T. et al. Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins. FEBS Lett. 460, 280-284 (1999).
    • (1999) FEBS Lett. , vol.460 , pp. 280-284
    • Sasaki, T.1
  • 38
    • 0030447865 scopus 로고    scopus 로고
    • Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix
    • Sasaki, T., Wiedemann, H., Matzner, M., Chu, M.-L. & Timpl, R. Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix. J. Cell Sci. 109, 2895-2904 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 2895-2904
    • Sasaki, T.1    Wiedemann, H.2    Matzner, M.3    Chu, M.-L.4    Timpl, R.5
  • 39
    • 0031956936 scopus 로고    scopus 로고
    • Developmental changes in the basement membrane of the normal and hypothyroid postnatal rat testis: Segmental localization of fibulin-2 and fibronectin
    • Loveland, K. et al. Developmental changes in the basement membrane of the normal and hypothyroid postnatal rat testis: segmental localization of fibulin-2 and fibronectin. Biol. Reprod. 58, 1123-1130 (1998).
    • (1998) Biol. Reprod. , vol.58 , pp. 1123-1130
    • Loveland, K.1
  • 40
    • 0032900611 scopus 로고    scopus 로고
    • Confocal laser scanning analysis of the association of fibulin-2 with fibrillin-1 and fibronectin define different stages of skin regeneration
    • Raghunath, M. et al. Confocal laser scanning analysis of the association of fibulin-2 with fibrillin-1 and fibronectin define different stages of skin regeneration. J. Invest. Dermatol. 112, 97-101 (1999).
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 97-101
    • Raghunath, M.1
  • 41
    • 0040761696 scopus 로고    scopus 로고
    • Differential regulation of fibulin, tenascin and nidogen expression during wound healing of normal and glucocorticoid-treated mice
    • Fässler, R., Sasaki, T., Timpl, R., Chu, M.-L. & Werner, S. Differential regulation of fibulin, tenascin and nidogen expression during wound healing of normal and glucocorticoid-treated mice. Exp. Cell Res. 222, 111-116 (1996).
    • (1996) Exp. Cell Res. , vol.222 , pp. 111-116
    • Fässler, R.1    Sasaki, T.2    Timpl, R.3    Chu, M.-L.4    Werner, S.5
  • 42
    • 0034798690 scopus 로고    scopus 로고
    • Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibers
    • Hunzelmann, N., Nischt, R., Brenneisen, P., Eickert, A. & Krieg, T. Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibers. Brit. J. Dermatol. 145, 217-222 (2001).
    • (2001) Brit. J. Dermatol. , vol.145 , pp. 217-222
    • Hunzelmann, N.1    Nischt, R.2    Brenneisen, P.3    Eickert, A.4    Krieg, T.5
  • 43
    • 0033400241 scopus 로고    scopus 로고
    • Spatiotemporal changes of fibronectin, tenascin-C, fibulin-1, and fibulin-2 in the skin during the development of chronic contact dermatitis
    • Kusubata, M. et al. Spatiotemporal changes of fibronectin, tenascin-C, fibulin-1, and fibulin-2 in the skin during the development of chronic contact dermatitis. J. Invest. Dermatol. 113, 906-912 (1999).
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 906-912
    • Kusubata, M.1
  • 44
    • 0031768032 scopus 로고    scopus 로고
    • Increased immunostaining of fibulin-1, an estrogen-regulated protein in the stroma of human ovarian epithelial tumors
    • Roger, P., Pujol, P., Lucas, A., Baldet, P. & Rochefort, H. Increased immunostaining of fibulin-1, an estrogen-regulated protein in the stroma of human ovarian epithelial tumors. Am. J. Pathol. 153, 1579-1588 (1998).
    • (1998) Am. J. Pathol. , vol.153 , pp. 1579-1588
    • Roger, P.1    Pujol, P.2    Lucas, A.3    Baldet, P.4    Rochefort, H.5
  • 45
    • 0026783564 scopus 로고
    • Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin
    • Balbona, K. et al. Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin. J. Biol. Chem. 267, 20120-20125 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 20120-20125
    • Balbona, K.1
  • 46
    • 0030928119 scopus 로고    scopus 로고
    • The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains
    • Tran, H., Van Dusen, W. J. & Argraves, W. S. The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains. J. Biol. Chem. 272, 22600-22606 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 22600-22606
    • Tran, H.1    Van Dusen, W.J.2    Argraves, W.S.3
  • 47
    • 0027598038 scopus 로고
    • Fibulin's organization into the extracellular matrix of fetal lung fibroblasts is dependent on fibronectin matrix assembly
    • Roman, J. & McDonald, J. A. Fibulin's organization into the extracellular matrix of fetal lung fibroblasts is dependent on fibronectin matrix assembly. Am. J. Respir. Cell Mol. Biol. 8, 538-545 (1993).
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 538-545
    • Roman, J.1    McDonald, J.A.2
  • 48
    • 0028648870 scopus 로고
    • A quantitative analysis of the incorporation of fibulin-1 into the extracellular matrix indicates that fibronectin assembly is required
    • Godyna, S., Mann, D. M. & Argraves, W. S. A quantitative analysis of the incorporation of fibulin-1 into the extracellular matrix indicates that fibronectin assembly is required. Matrix Biol. 14, 467-477 (1994).
    • (1994) Matrix Biol. , vol.14 , pp. 467-477
    • Godyna, S.1    Mann, D.M.2    Argraves, W.S.3
  • 49
    • 0343036267 scopus 로고    scopus 로고
    • Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules
    • Adam, S. et al. Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules. J. Mol. Biol. 272, 226-236 (1997).
    • (1997) J. Mol. Biol. , vol.272 , pp. 226-236
    • Adam, S.1
  • 50
    • 0034791903 scopus 로고    scopus 로고
    • Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies
    • Ries, A., Göhring, W., Fox, J. W., Timpl, R. & Sasaki, T. Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies. Eur. J. Biochem. 268, 5119-5128 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5119-5128
    • Ries, A.1    Göhring, W.2    Fox, J.W.3    Timpl, R.4    Sasaki, T.5
  • 51
    • 0345148341 scopus 로고    scopus 로고
    • Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V
    • Friedrich, M. V. K. et al. Structural basis of glycosaminoglycan modification and of heterotypic interactions of perlecan domain V. J. Mol. Biol. 294, 259-270 (1999).
    • (1999) J. Mol. Biol. , vol.294 , pp. 259-270
    • Friedrich, M.V.K.1
  • 52
    • 0035902836 scopus 로고    scopus 로고
    • Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan
    • Hopf, M., Göhring, W., Mann, K. & Timpl, R. Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan. J. Mol. Biol. 311, 529-541 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 529-541
    • Hopf, M.1    Göhring, W.2    Mann, K.3    Timpl, R.4
  • 53
    • 0034254083 scopus 로고    scopus 로고
    • Structure and function of laminin LG modules
    • Timpl, R. et al. Structure and function of laminin LG modules. Matrix Biol. 19, 309-317 (2000).
    • (2000) Matrix Biol. , vol.19 , pp. 309-317
    • Timpl, R.1
  • 54
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins
    • Talts, J. F., Andac, Z., Göhring, W., Brancaccio, A. & Timpl, R. Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins. EMBO J. 18, 863-870 (1999).
    • (1999) EMBO J. , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Göhring, W.3    Brancaccio, A.4    Timpl, R.5
  • 55
    • 0031020164 scopus 로고    scopus 로고
    • Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences
    • Utani, A., Nomizu, M. & Yamada, Y. Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences. J. Biol. Chem. 272, 2814-2820 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 2814-2820
    • Utani, A.1    Nomizu, M.2    Yamada, Y.3
  • 56
    • 0035824882 scopus 로고    scopus 로고
    • Short arm region of laminin-5 γ-2 chain: Structure, mechanism of processing and binding to heparin and proteins
    • Sasaki, T. et al. Short arm region of laminin-5 γ-2 chain: structure, mechanism of processing and binding to heparin and proteins. J. Mol. Biol. 314, 751-763 (2001).
    • (2001) J. Mol. Biol. , vol.314 , pp. 751-763
    • Sasaki, T.1
  • 57
    • 0032479999 scopus 로고    scopus 로고
    • Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin
    • Sasaki, T. et al. Structure, function and tissue forms of the C-terminal globular domain of collagen XVIII containing the angiogenesis inhibitor endostatin. EMBO J. 17, 4249-4256 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4249-4256
    • Sasaki, T.1
  • 58
    • 0034283571 scopus 로고    scopus 로고
    • Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity
    • Sasaki, T. et al. Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity. J. Mol. Biol. 301, 1179-1190 (2000).
    • (2000) J. Mol. Biol. , vol.301 , pp. 1179-1190
    • Sasaki, T.1
  • 59
    • 0036001158 scopus 로고    scopus 로고
    • Structure and function of collagen-derived endostatin inhibitors of angiogenesis
    • Sasaki, T., Hohenester, E. & Timpl, R. Structure and function of collagen-derived endostatin inhibitors of angiogenesis. IUBMB Life 53, 77-84 (2002).
    • (2002) IUBMB Life , vol.53 , pp. 77-84
    • Sasaki, T.1    Hohenester, E.2    Timpl, R.3
  • 60
    • 0029823181 scopus 로고    scopus 로고
    • Brain extracellular matrix
    • Ruoslahti, E. Brain extracellular matrix. Glycobiology 6, 489-492 (1996).
    • (1996) Glycobiology , vol.6 , pp. 489-492
    • Ruoslahti, E.1
  • 61
    • 0033575208 scopus 로고    scopus 로고
    • Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican
    • Aspberg, A., Adam, S., Kostka, G., Timpl, R. & Heinegard, D. Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican. J. Biol. Chem. 274, 20444-20449 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 20444-20449
    • Aspberg, A.1    Adam, S.2    Kostka, G.3    Timpl, R.4    Heinegard, D.5
  • 62
    • 0035847046 scopus 로고    scopus 로고
    • The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding
    • Olin, A. J. et al. The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding. J. Biol. Chem. 276, 1253-1261 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 1253-1261
    • Olin, A.J.1
  • 63
    • 0029098811 scopus 로고
    • The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis
    • Tran, H. et al. The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis. J. Biol. Chem. 270, 19458-19464 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 19458-19464
    • Tran, H.1
  • 64
    • 0029822772 scopus 로고    scopus 로고
    • Fibulin-1 mediates platelet adhesion via a bridge of fibrinogen
    • Godyna, S., Dias-Ricart, M. & Argraves, W. S. Fibulin-1 mediates platelet adhesion via a bridge of fibrinogen. Blood 88, 2569-2577 (1996).
    • (1996) Blood , vol.88 , pp. 2569-2577
    • Godyna, S.1    Dias-Ricart, M.2    Argraves, W.S.3
  • 65
    • 0034802720 scopus 로고    scopus 로고
    • Perinatal lethality and endothedlial cell abnormalities in several vessel compartments of fibulin-1 deficient mice
    • Kostka, G. et al. Perinatal lethality and endothedlial cell abnormalities in several vessel compartments of fibulin-1 deficient mice. Mol. Cell. Biol. 21, 7025-7034 (2001). This paper shows that a fibulin-1 deficiency causes a haemorrhagic phenotype.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7025-7034
    • Kostka, G.1
  • 66
    • 0033514408 scopus 로고    scopus 로고
    • The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin-1C: A clue for a role of NOVH in cell-adhesion signalling
    • Perbal, B. et al. The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin-1C: a clue for a role of NOVH in cell-adhesion signalling. Proc. Natl Acad. Sci. USA 96, 869-874 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 869-874
    • Perbal, B.1
  • 67
    • 0029087888 scopus 로고
    • Integrin-binding and cell-adhesion studies of fibulins reveal a particular affinity for αllbβ3
    • Pfaff, M., Sasaki, T., Tangemann, K., Chu, M.-L. & Timpl, R. Integrin-binding and cell-adhesion studies of fibulins reveal a particular affinity for αllbβ3. Exp. Cell Res. 219, 87-92 (1995).
    • (1995) Exp. Cell Res. , vol.219 , pp. 87-92
    • Pfaff, M.1    Sasaki, T.2    Tangemann, K.3    Chu, M.-L.4    Timpl, R.5
  • 68
    • 0035694454 scopus 로고    scopus 로고
    • Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility
    • Twal, W. O. et al. Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility. J. Cell Sci. 114, 4587-4598 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 4587-4598
    • Twal, W.O.1
  • 69
    • 0033529668 scopus 로고    scopus 로고
    • DANCE, a novel secreted RGD protein expressed in developing, atherosclerotic, and balloon-injured arteries
    • Nakamura, T. et al. DANCE, a novel secreted RGD protein expressed in developing, atherosclerotic, and balloon-injured arteries. J. Biol. Chem. 274, 22476-22483 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22476-22483
    • Nakamura, T.1
  • 70
    • 0037178816 scopus 로고    scopus 로고
    • Context-specific effects of fibulin-5 (DANCE/EVEC) on cell proliferation, motility, and invasion. Fibulin-5 is induced by transforming growth factor-β and affects protein kinase cascades
    • Schiemann, W. P., Blobe, G. C., Kalume, D. E., Pandey, A. & Lodish, H. F. Context-specific effects of fibulin-5 (DANCE/EVEC) on cell proliferation, motility, and invasion. Fibulin-5 is induced by transforming growth factor-β and affects protein kinase cascades. J. Biol. Chem. 277, 27367-27377 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 27367-27377
    • Schiemann, W.P.1    Blobe, G.C.2    Kalume, D.E.3    Pandey, A.4    Lodish, H.F.5
  • 71
    • 0033597914 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces expression of the stress response genes hop and H 411
    • Heine, H., Delude, R. L., Monks, B. G., Esperik, T. & Golenbock, D. T. Bacterial lipopolysaccharide induces expression of the stress response genes hop and H411. J. Biol. Chem. 274, 21049-21055 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21049-21055
    • Heine, H.1    Delude, R.L.2    Monks, B.G.3    Esperik, T.4    Golenbock, D.T.5
  • 72
    • 0030814850 scopus 로고    scopus 로고
    • Surpression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines
    • Qing, J. et al. Surpression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines. Oncogene 15, 2159-2168 (1997).
    • (1997) Oncogene , vol.15 , pp. 2159-2168
    • Qing, J.1
  • 73
    • 0030060325 scopus 로고    scopus 로고
    • Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells
    • Clinton, G. M. et al. Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells. Proc. Natl Acad Sci. USA 93, 316-320 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 316-320
    • Clinton, G.M.1
  • 74
    • 0032498551 scopus 로고    scopus 로고
    • Estradiol and fibulin-1 inhibit motility of human ovarian-and breast-cancer cells induced by fibronectin
    • Hayashido, Y. et al. Estradiol and fibulin-1 inhibit motility of human ovarian- and breast-cancer cells induced by fibronectin. Int. J. Cancer 75, 654-658 (1998).
    • (1998) Int. J. Cancer , vol.75 , pp. 654-658
    • Hayashido, Y.1
  • 75
    • 0036171086 scopus 로고    scopus 로고
    • The fibulin-1 gene (FLBN1) is disrupted in a t(12;22) associated with a complex type of synpolydactyly
    • Debeer, P. et al. The fibulin-1 gene (FLBN1) is disrupted in a t(12;22) associated with a complex type of synpolydactyly. J. Med. Genet. 39, 98-104 (2002).
    • (2002) J. Med. Genet. , vol.39 , pp. 98-104
    • Debeer, P.1
  • 76
    • 0034979562 scopus 로고    scopus 로고
    • Molecular genetic heterogeneity in autosomal dominant drusen
    • Tartellin, E. E. et al. Molecular genetic heterogeneity in autosomal dominant drusen. J. Med. Genet. 38, 381-384 (2001).
    • (2001) J. Med. Genet. , vol.38 , pp. 381-384
    • Tartellin, E.E.1
  • 77
    • 0036792087 scopus 로고    scopus 로고
    • Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration
    • Marmorstein, L. Y. et al. Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration. Proc. Natl Acad. Sci. USA 99, 13067-13072 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13067-13072
    • Marmorstein, L.Y.1
  • 78
    • 0037117796 scopus 로고    scopus 로고
    • Elastic fibres: Building bridges between cells and their matrix
    • Midwood, K. S. & Schwarzbauer, J. E. Elastic fibres: building bridges between cells and their matrix. Curr. Biol. 12, R279-R281 (2002).
    • (2002) Curr. Biol. , vol.12
    • Midwood, K.S.1    Schwarzbauer, J.E.2
  • 79
    • 0036713921 scopus 로고    scopus 로고
    • Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in a severe form of cutis laxa
    • Loeys, B. et al. Homozygosity for a missense mutation in fibulin-5 (FBLN5) results in a severe form of cutis laxa. Hum. Mol. Genet. 11, 2113-2118 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2113-2118
    • Loeys, B.1
  • 80
    • 0037386112 scopus 로고    scopus 로고
    • Genetic heterogeneity of cutis laxa: A heterozygous tandem duplication within the fibulin-5 (FBLN5) gene
    • Markova, D. et al. Genetic heterogeneity of cutis laxa: a heterozygous tandem duplication within the fibulin-5 (FBLN5) gene. Am. J. Hum. Genet. 72, 998-1004 (2003).
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 998-1004
    • Markova, D.1
  • 82
    • 0033787772 scopus 로고    scopus 로고
    • Mouse models of genetic diseases resulting from mutations in elastic fiber proteins
    • Dietz, H. C. & Mecham, R. P. Mouse models of genetic diseases resulting from mutations in elastic fiber proteins. Matrix Biol. 19, 481-488 (2000).
    • (2000) Matrix Biol. , vol.19 , pp. 481-488
    • Dietz, H.C.1    Mecham, R.P.2
  • 83
    • 0033783405 scopus 로고    scopus 로고
    • Genetic disorders of the elastic fiber system
    • Milewicz, D. M., Urban, Z. & Boyd, C. Genetic disorders of the elastic fiber system. Matrix Biol. 19, 471-480 (2000).
    • (2000) Matrix Biol. , vol.19 , pp. 471-480
    • Milewicz, D.M.1    Urban, Z.2    Boyd, C.3
  • 84
    • 0032966019 scopus 로고    scopus 로고
    • Complete exon-intron organization of the mouse fibulin-1 gene and its comparison with the human fibulin-1 gene
    • Pan, T.-C., Kostka, G., Zhang, R.-Z., Timpl, R. & Chu, M.-L. Complete exon-intron organization of the mouse fibulin-1 gene and its comparison with the human fibulin-1 gene. FEBS Lett. 444, 38-42 (1999).
    • (1999) FEBS Lett. , vol.444 , pp. 38-42
    • Pan, T.-C.1    Kostka, G.2    Zhang, R.-Z.3    Timpl, R.4    Chu, M.-L.5
  • 85
    • 0027939751 scopus 로고
    • The fibulin-1 gene (FBLN1) is located on human chromosome 22 and mouse chromosome 15
    • Mattei, M. G., Pan, T.-C., Zhang, R.-Z., Timpl, R. & Chu, M.-L. The fibulin-1 gene (FBLN1) is located on human chromosome 22 and mouse chromosome 15. Genomics 22, 437-438 (1994).
    • (1994) Genomics , vol.22 , pp. 437-438
    • Mattei, M.G.1    Pan, T.-C.2    Zhang, R.-Z.3    Timpl, R.4    Chu, M.-L.5
  • 86
    • 0001229004 scopus 로고    scopus 로고
    • Mouse fibulin-2 gene. Complete exon-intron organization and promoter characterization
    • Grässel, S., Sicot, F.-X., Gotta, S. & Chu, M.-L. Mouse fibulin-2 gene. Complete exon-intron organization and promoter characterization. Eur. J. Biochem. 263, 471-477 (1999).
    • (1999) Eur. J. Biochem. , vol.263 , pp. 471-477
    • Grässel, S.1    Sicot, F.-X.2    Gotta, S.3    Chu, M.-L.4
  • 87
    • 0030219709 scopus 로고    scopus 로고
    • Structure and chromosomal assignment of the human S1-5 gene (FBNL) that is highly homologous to fibrillin
    • Ikegawa, S., Toda, T., Okui, K. & Nakamura, Y. Structure and chromosomal assignment of the human S1-5 gene (FBNL) that is highly homologous to fibrillin. Genomics 35, 590-592 (1996).
    • (1996) Genomics , vol.35 , pp. 590-592
    • Ikegawa, S.1    Toda, T.2    Okui, K.3    Nakamura, Y.4
  • 88
    • 0034099229 scopus 로고    scopus 로고
    • Isolation of a paralog of the Doyne honeycombe retinal dystrophy gene from the multiple retinopathy critical region on 11q13
    • Katsanis, N., Venable, S., Smith, J. R. & Lupski, J. R. Isolation of a paralog of the Doyne honeycombe retinal dystrophy gene from the multiple retinopathy critical region on 11q13. Hum. Genet. 106, 66-72 (2000).
    • (2000) Hum. Genet. , vol.106 , pp. 66-72
    • Katsanis, N.1    Venable, S.2    Smith, J.R.3    Lupski, J.R.4
  • 89
    • 0033388454 scopus 로고    scopus 로고
    • Assignment of fibulin-5 (FBLN5) to human chromosome 14q31 by in situ hybridization and radiation hybrid mapping
    • Kowal, R. C., Jolsin, J. M., Olson, E. N. & Schultz, R. A. Assignment of fibulin-5 (FBLN5) to human chromosome 14q31 by in situ hybridization and radiation hybrid mapping. Cytogenet. Cell Genet. 87, 2-3 (1999).
    • (1999) Cytogenet. Cell Genet. , vol.87 , pp. 2-3
    • Kowal, R.C.1    Jolsin, J.M.2    Olson, E.N.3    Schultz, R.A.4


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