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Volumn 272, Issue 2, 1997, Pages 226-236

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

Author keywords

Basement membranes; Calcium binding; Kinetic analysis; Recombinant proteins; Site directed mutagenesis

Indexed keywords

CALCIUM BINDING PROTEIN; CHIMERIC PROTEIN; ENTACTIN; EPIDERMAL GROWTH FACTOR; EPITOPE; FIBULIN; MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 0343036267     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1244     Document Type: Article
Times cited : (30)

References (47)
  • 1
    • 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. 111:1990;3155-3164.
    • (1990) J. Cell Biol. , vol.111 , pp. 3155-3164
    • Argraves, W.S.1    Tran, H.2    Burgess, W.H.3    Dickerson, K.4
  • 2
    • 0024460533 scopus 로고
    • Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV
    • Aumailley M., Wiedemann H., Mann K., Timpl R. Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV. Eur. J. Biochem. 284:1989;241-248.
    • (1989) Eur. J. Biochem. , vol.284 , pp. 241-248
    • Aumailley, M.1    Wiedemann, H.2    Mann, K.3    Timpl, R.4
  • 3
    • 0026783564 scopus 로고
    • Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin
    • Balbona K., Tran H., Godyna S., Ingham K. C., Strickland D. K., Argraves W. S. Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin. J. Biol. Chem. 267:1992;20120-20125.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20120-20125
    • Balbona, K.1    Tran, H.2    Godyna, S.3    Ingham, K.C.4    Strickland, D.K.5    Argraves, W.S.6
  • 4
    • 0028047847 scopus 로고
    • Protein binding and cell adhesion properties of two laminin isoforms (AmB1eB2e, AmB1sB2e) from human placenta
    • Brown J. C., Wiedemann H., Timpl R. Protein binding and cell adhesion properties of two laminin isoforms (AmB1eB2e, AmB1sB2e) from human placenta. J. Cell Sci. 107:1994;329-338.
    • (1994) J. Cell Sci. , vol.107 , pp. 329-338
    • Brown, J.C.1    Wiedemann, H.2    Timpl, R.3
  • 6
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C., Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:1987;2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 7
    • 0027257818 scopus 로고
    • Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′ end
    • Corson G. M., Chalberg S. C., Dietz H. C., Charbonneau N. L., Sakai L. Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5′ end. Genomics. 17:1993;476-484.
    • (1993) Genomics , vol.17 , pp. 476-484
    • Corson, G.M.1    Chalberg, S.C.2    Dietz, H.C.3    Charbonneau, N.L.4    Sakai, L.5
  • 8
    • 0028852659 scopus 로고
    • Marfan syndrome and related disorders
    • Dietz H. C., Pyeritz R. E. Marfan syndrome and related disorders. Human Mol. Gen. 4:1995;1799-1809.
    • (1995) Human Mol. Gen. , vol.4 , pp. 1799-1809
    • Dietz, H.C.1    Pyeritz, R.E.2
  • 9
    • 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., Knott V., Werner J. M., Cardy C. M., Campbell I. D., Handford P. A. Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders. Cell. 85:1996;597-605.
    • (1996) Cell , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, J.M.3    Cardy, C.M.4    Campbell, I.D.5    Handford, P.A.6
  • 10
    • 0023587128 scopus 로고
    • Electron microscopy and other physical methods for the characterization of extracellular matrix components: Laminin, fibronectin, collagen IV, collagen VI and proteoglycans
    • Engel J., Furthmayr H. Electron microscopy and other physical methods for the characterization of extracellular matrix components: laminin, fibronectin, collagen IV, collagen VI and proteoglycans. Methods Enzymol. 145:1987;3-78.
    • (1987) Methods Enzymol. , vol.145 , pp. 3-78
    • Engel, J.1    Furthmayr, H.2
  • 11
    • 0026551323 scopus 로고
    • Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis
    • Fägerstam L. G., Frostell-Karlsson A., Karlsson R., Persson B., Rönnberg I. Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis. J. Chromatog. 597:1992;397-410.
    • (1992) J. Chromatog. , vol.597 , pp. 397-410
    • Fägerstam, L.G.1    Frostell-Karlsson, A.2    Karlsson, R.3    Persson, B.4    Rönnberg, I.5
  • 13
    • 0027959729 scopus 로고
    • Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein
    • Glanville R., Qian R. Q., McClure D. W., Maslen C. L. Calcium binding, hydroxylation, and glycosylation of the precursor epidermal growth factor-like domains of fibrillin-1, the Marfan gene protein. J. Biol. Chem. 269:1994;26630-26634.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26630-26634
    • Glanville, R.1    Qian, R.Q.2    McClure, D.W.3    Maslen, C.L.4
  • 14
    • 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. 14:1994;467-477.
    • (1994) Matrix Biol. , vol.14 , pp. 467-477
    • Godyna, S.1    Mann, D.M.2    Argraves, W.S.3
  • 16
    • 0028931325 scopus 로고
    • The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1
    • Handford P. A., Downing A. K., Rao Z., Hewett D. R., Sykes B. R., Kielty C. M. The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1. J. Biol. Chem. 270:1995;6751-6756.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6751-6756
    • Handford, P.A.1    Downing, A.K.2    Rao, Z.3    Hewett, D.R.4    Sykes, B.R.5    Kielty, C.M.6
  • 18
    • 0027141134 scopus 로고
    • The role of calcium in the organization of fibrillin microfibrils
    • Kielty C. M., Shuttleworth C. A. The role of calcium in the organization of fibrillin microfibrils. FEBS Letters. 336:1993;323-326.
    • (1993) FEBS Letters , vol.336 , pp. 323-326
    • Kielty, C.M.1    Shuttleworth, C.A.2
  • 19
    • 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. 193:1990;651-659.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 651-659
    • Kluge, M.1    Mann, K.2    Dziadek, M.3    Timpl, R.4
  • 20
    • 0029977996 scopus 로고    scopus 로고
    • Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1
    • Knott V., Downing A. K., Cardy C. M., Handford P. Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. J. Mol. Biol. 255:1996;22-27.
    • (1996) J. Mol. Biol. , vol.255 , pp. 22-27
    • Knott, V.1    Downing, A.K.2    Cardy, C.M.3    Handford, P.4
  • 23
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • Mayer U., Nischt R., Pöschl E., Mann K., Fukuda K., Gerl M., Yamada Y., Timpl R. A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J. 12:1993;1879-1885.
    • (1993) EMBO J. , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Pöschl, E.3    Mann, K.4    Fukuda, K.5    Gerl, M.6    Yamada, Y.7    Timpl, R.8
  • 24
    • 0029932657 scopus 로고    scopus 로고
    • The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo
    • Miosge N., Götz W., Sasaki T., Chu M.-L., Timpl R., Herken R. The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo. Histochem. J. 28:1996;109-116.
    • (1996) Histochem. J. , vol.28 , pp. 109-116
    • Miosge, N.1    Götz, W.2    Sasaki, T.3    Chu, M.-L.4    Timpl, R.5    Herken, R.6
  • 25
    • 0025858265 scopus 로고
    • Recombinant expression and properties of the human calcium-binding extracellular matrix protein BM-40
    • Nischt R., Pottgiesser J., Krieg T., Mayer U., Aumailley M., Timpl R. Recombinant expression and properties of the human calcium-binding extracellular matrix protein BM-40. Eur. J. Biochem. 200:1991;529-536.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 529-536
    • Nischt, R.1    Pottgiesser, J.2    Krieg, T.3    Mayer, U.4    Aumailley, M.5    Timpl, R.6
  • 26
    • 0027227388 scopus 로고
    • Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands
    • Pan T.-C., Kluge M., Zhang R.-Z., Mayer U., Timpl R., Chu M.-L. Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement membrane ligands. Eur. J. Biochem. 215:1993a;733-740.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 733-740
    • Pan, T.-C.1    Kluge, M.2    Zhang, R.-Z.3    Mayer, U.4    Timpl, R.5    Chu, M.-L.6
  • 27
    • 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., Sasaki T., Zhang R.-Z., Fässler R., Timpl R., Chu M.-L. 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. 123:1993b;1269-1277.
    • (1993) J. Cell Biol. , vol.123 , pp. 1269-1277
    • Pan, T.-C.1    Sasaki, T.2    Zhang, R.-Z.3    Fässler, R.4    Timpl, R.5    Chu, M.-L.6
  • 28
    • 0029790892 scopus 로고    scopus 로고
    • Site-directed mutagenesis and structural interpretation of the nidogen binding site of laminin γ 1 chain
    • Pöschl E., Mayer U., Stetefeld J., Baumgartner R., Holak T. A., Huber R., Timpl R. Site-directed mutagenesis and structural interpretation of the nidogen binding site of laminin γ 1 chain. EMBO J. 15:1996;5154-5159.
    • (1996) EMBO J. , vol.15 , pp. 5154-5159
    • Pöschl, E.1    Mayer, U.2    Stetefeld, J.3    Baumgartner, R.4    Holak, T.A.5    Huber, R.6    Timpl, R.7
  • 29
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S. W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 31
    • 0024039803 scopus 로고
    • The role of β-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX
    • Rees D. J. G., Jones I. M., Handford P. A., Walter S. J., Esnouf M. P., Smith K. J., Brownlee G. G. The role of β-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX. EMBO J. 7:1988;2053-2061.
    • (1988) EMBO J. , vol.7 , pp. 2053-2061
    • Rees, D.J.G.1    Jones, I.M.2    Handford, P.A.3    Walter, S.J.4    Esnouf, M.P.5    Smith, K.J.6    Brownlee, G.G.7
  • 34
    • 0031030185 scopus 로고    scopus 로고
    • Calcium stabilizes fibrillin-1 against proteolytic degradation
    • Reinhardt D. P., Ono R. N., Sakai L. Y. Calcium stabilizes fibrillin-1 against proteolytic degradation. J. Biol. Chem. 272:1997;1231-1236.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1231-1236
    • Reinhardt, D.P.1    Ono, R.N.2    Sakai, L.Y.3
  • 35
  • 36
    • 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. 8:1993;538-545.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 538-545
    • Roman, J.1    McDonald, J.A.2
  • 37
  • 38
    • 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. 254:1995b;892-899.
    • (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
  • 39
    • 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. 109:1996a;2895-2904.
    • (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
  • 40
    • 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. 240:1996b;427-434.
    • (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
  • 41
    • 0030977056 scopus 로고    scopus 로고
    • Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge
    • Sasaki T., Mann K., Wiedemann H., Göhring W., Lustig A., Engel J., Chu M.-L., Timpl R. Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge. EMBO J. 16:1997;3035-3043.
    • (1997) EMBO J. , vol.16 , pp. 3035-3043
    • Sasaki, T.1    Mann, K.2    Wiedemann, H.3    Göhring, W.4    Lustig, A.5    Engel, J.6    Chu, M.-L.7    Timpl, R.8
  • 43
    • 0028837980 scopus 로고
    • Demonstration of non-linear detection in ELISA resulting in up to 1000-fold too high affinities of fibrinogen binding to integrin αiIbβ3
    • Tangemann K., Engel J. Demonstration of non-linear detection in ELISA resulting in up to 1000-fold too high affinities of fibrinogen binding to integrin αIIbβ3. FEBS Letters. 358:1995;179-181.
    • (1995) FEBS Letters , vol.358 , pp. 179-181
    • Tangemann, K.1    Engel, J.2
  • 44
    • 0027947233 scopus 로고
    • Recombinant expression and structural and binding properties of α1(VI) and α2(VI) chains of human collagen type VI
    • Tillet E., Wiedemann H., Golbik R., Pan T.-C., Zhang R.-Z., Mann K., Chu M.-L., Timpl R. Recombinant expression and structural and binding properties of α1(VI) and α2(VI) chains of human collagen type VI. Eur. J. Biochem. 221:1994;177-185.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 177-185
    • Tillet, E.1    Wiedemann, H.2    Golbik, R.3    Pan, T.-C.4    Zhang, R.-Z.5    Mann, K.6    Chu, M.-L.7    Timpl, R.8
  • 46
    • 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. 52:1993;211-220.
    • (1993) Differentiation , vol.52 , pp. 211-220
    • Zhang, H.-Y.1    Kluge, M.2    Timpl, R.3    Chu, M.-L.4    Ekblom, P.5
  • 47
    • 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. Devel. Dynam. 205:1996;348-364.
    • (1996) Devel. Dynam. , vol.205 , pp. 348-364
    • Zhang, H.-Y.1    Timpl, R.2    Sasaki, T.3    Chu, M.-L.4    Ekblom, P.5


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