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Volumn 10, Issue 2, 1999, Pages 99-117

Latent transforming growth factor-β binding proteins (LTBPs) - Structural extracellular matrix proteins for targeting TGF-β action

Author keywords

Fibrillins; Growth factor targeting activation; LTBP; Microfibrils; TGF

Indexed keywords

ACTIN BINDING PROTEIN; BINDING PROTEIN; CARRIER PROTEIN; CYSTEINE; EPIDERMAL GROWTH FACTOR; FIBRILLIN; LTBP-2 PROTEIN; LTBP-4 PROTEIN; SCLEROPROTEIN; TGF-BETA1 BINDING PROTEIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 0344721500     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6101(99)00010-6     Document Type: Short Survey
Times cited : (261)

References (207)
  • 1
    • 0028180315 scopus 로고
    • The TGF-β superfamily: New members, new receptors, and new genetic tests of function in different organisms
    • Kingsley D. The TGF-β superfamily: new members, new receptors, and new genetic tests of function in different organisms. Genes Dev. 8:1994;133-146.
    • (1994) Genes Dev , vol.8 , pp. 133-146
    • Kingsley, D.1
  • 3
    • 0022373618 scopus 로고
    • Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells
    • Derynck R., Jarrett J., Chen E., Eaton D., Bell J., Assoian R., Roberts A., Spom M., Goeddel D. Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells. Nature. 316:1985;701-705.
    • (1985) Nature , vol.316 , pp. 701-705
    • Derynck, R.1    Jarrett, J.2    Chen, E.3    Eaton, D.4    Bell, J.5    Assoian, R.6    Roberts, A.7    Spom, M.8    Goeddel, D.9
  • 5
    • 0023704384 scopus 로고
    • Amino acid sequence of the BSC-1 cell growth inhibitor (polyergin) deduced from the nucleotide sequence of the cDNA
    • Hanks S., Armour R., Baldwin J., Maldonado F., Spiess J., Holley R. Amino acid sequence of the BSC-1 cell growth inhibitor (polyergin) deduced from the nucleotide sequence of the cDNA. Proc Natl Acad Sci. 85:1988;79-82.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 79-82
    • Hanks, S.1    Armour, R.2    Baldwin, J.3    Maldonado, F.4    Spiess, J.5    Holley, R.6
  • 7
    • 0005862522 scopus 로고
    • Identification of another member of the transforming growth factor type β gene family
    • ten Dijke P., Hansen P., Iwata K., Pieler C., Foulkes J. Identification of another member of the transforming growth factor type β gene family. Proc Natl Acad Sci USA. 85:1988;4715-4719.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4715-4719
    • Ten Dijke, P.1    Hansen, P.2    Iwata, K.3    Pieler, C.4    Foulkes, J.5
  • 8
    • 0024260928 scopus 로고
    • Complementary deoxyribonucleic acid cloning of a messenger ribonucleic acid encoding transforming growth factor β4 from chicken embryo chondrocytes
    • Jakowlew S., Dillard P., Sporn M., Roberts A. Complementary deoxyribonucleic acid cloning of a messenger ribonucleic acid encoding transforming growth factor β4 from chicken embryo chondrocytes. Mol Endocrinol. 2:1988;1186-1195.
    • (1988) Mol Endocrinol , vol.2 , pp. 1186-1195
    • Jakowlew, S.1    Dillard, P.2    Sporn, M.3    Roberts, A.4
  • 9
    • 0025021120 scopus 로고
    • Identification of a novel transforming growth factor-β (TGF-β5) mRNA in Xenopus Iaevis
    • Kondaiah P., Sands M., Smith J., Fields A., Roberts A., Sporn M., Melton D. Identification of a novel transforming growth factor-β (TGF-β5) mRNA in Xenopus Iaevis. J Biol Chem. 265:1990;1089-1093.
    • (1990) J Biol Chem , vol.265 , pp. 1089-1093
    • Kondaiah, P.1    Sands, M.2    Smith, J.3    Fields, A.4    Roberts, A.5    Sporn, M.6    Melton, D.7
  • 10
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massague J. The transforming growth factor-β family. Annu Rev Cell Biol. 6:1990;597-641.
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 597-641
    • Massague, J.1
  • 11
    • 0026437136 scopus 로고
    • Transforming growth factor-βs as regulators of cellular growth and phenotype
    • Laiho M., Keski-Oja J. Transforming growth factor-βs as regulators of cellular growth and phenotype. Crit Rev Oncog. 3:1992;1-26.
    • (1992) Crit Rev Oncog , vol.3 , pp. 1-26
    • Laiho, M.1    Keski-Oja, J.2
  • 12
    • 0029742706 scopus 로고    scopus 로고
    • Transforming growth factor-β: A general review
    • Lawrence D. Transforming growth factor-β: a general review. Eur Cytokine Netw. 7:1996;363-374.
    • (1996) Eur Cytokine Netw , vol.7 , pp. 363-374
    • Lawrence, D.1
  • 13
    • 0030271736 scopus 로고    scopus 로고
    • Regulation of differentiation by TGF-β
    • Moses H., Serra R. Regulation of differentiation by TGF-β Curr Opin Genet Dev. 6:1996;581-586.
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 581-586
    • Moses, H.1    Serra, R.2
  • 14
    • 0038641688 scopus 로고
    • Induction of c-sis mRNA and activity similar to platelet-derived growth factor by transforming growth factor β: A proposed model for indirect mitogenesis involving autocrine activity
    • Leof E., Proper J., Goustin A., Shipley G., DiCorleto P., Moses H. Induction of c-sis mRNA and activity similar to platelet-derived growth factor by transforming growth factor β: a proposed model for indirect mitogenesis involving autocrine activity. Proc Natl Acad Sci USA. 83:1986;2453-2457.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2453-2457
    • Leof, E.1    Proper, J.2    Goustin, A.3    Shipley, G.4    Dicorleto, P.5    Moses, H.6
  • 15
    • 0027297080 scopus 로고
    • Enhanced bFGF gene expression in response to transforming growth factor-β stimulation of AKR-2B cells
    • Pertovaara L., Saksela O., Alitalo K. Enhanced bFGF gene expression in response to transforming growth factor-β stimulation of AKR-2B cells. Growth Factors. 9:1993;81-86.
    • (1993) Growth Factors , vol.9 , pp. 81-86
    • Pertovaara, L.1    Saksela, O.2    Alitalo, K.3
  • 16
    • 0028221238 scopus 로고
    • Vascular endothelial growth factor is induced in response to transforming growth factor-β In fibroblastic and epithelial cells
    • Pertovaara L., Kaipainen A., Mustonen T., Orpana A., Ferrara N., Saksela O., Alitalo K. Vascular endothelial growth factor is induced in response to transforming growth factor-β in fibroblastic and epithelial cells. J Biol Chem. 269:1994;6271-6274.
    • (1994) J Biol Chem , vol.269 , pp. 6271-6274
    • Pertovaara, L.1    Kaipainen, A.2    Mustonen, T.3    Orpana, A.4    Ferrara, N.5    Saksela, O.6    Alitalo, K.7
  • 17
    • 0031884834 scopus 로고    scopus 로고
    • TGF-βs stimulate cell proliferation via an autocrine production of FGF-2 in corneal stromal fibroblasts
    • Kay E., Lee M., Seong G., Lee Y. TGF-βs stimulate cell proliferation via an autocrine production of FGF-2 in corneal stromal fibroblasts. Curr Eye Res. 17:1998;286-293.
    • (1998) Curr Eye Res , vol.17 , pp. 286-293
    • Kay, E.1    Lee, M.2    Seong, G.3    Lee, Y.4
  • 18
    • 0028221614 scopus 로고
    • Transforming growth factor β: A matter of life and death
    • McCartney-Francis N., Wahl S. Transforming growth factor β: a matter of life and death. J Leukoc Bio. 55:1994;401-409.
    • (1994) J Leukoc Bio , vol.55 , pp. 401-409
    • McCartney-Francis, N.1    Wahl, S.2
  • 19
  • 22
    • 0028859738 scopus 로고    scopus 로고
    • Onset and progression of pathological lesions in transforming growth factor-β1-deficient mice
    • Boivin G, O'Toole B, Ormsby I, Diebold R, Eis M, Doetschman T, Kier A. Onset and progression of pathological lesions in transforming growth factor-β1-deficient mice. Am J Pathol 1999;146:276-288.
    • (1999) Am J Pathol , vol.146 , pp. 276-288
    • Boivin, G.1    O'Toole, B.2    Ormsby, I.3    Diebold, R.4    Eis, M.5    Doetschman, T.6    Kier, A.7
  • 23
    • 0028806184 scopus 로고
    • Abnormal lung development and cleft palate in mice lacking TGF-β3 indicates defects of epithelial-mesenchymal interaction
    • Kaartinen V., Voncken J., Shuler C., Warburton D., Bu D., Heisterkamp N., Groffen J. Abnormal lung development and cleft palate in mice lacking TGF-β3 indicates defects of epithelial-mesenchymal interaction. Nat Genet. 11:1995;415-421.
    • (1995) Nat Genet , vol.11 , pp. 415-421
    • Kaartinen, V.1    Voncken, J.2    Shuler, C.3    Warburton, D.4    Bu, D.5    Heisterkamp, N.6    Groffen, J.7
  • 25
    • 0031684855 scopus 로고    scopus 로고
    • Extracellular matrix-associated transforming growth factor-β: Role in cancer cell growth and invasion
    • Taipale J., Saharinen J., Keski-Oja J. Extracellular matrix-associated transforming growth factor-β: role in cancer cell growth and invasion. Adv Cancer Res. 75:1998;87-134.
    • (1998) Adv Cancer Res , vol.75 , pp. 87-134
    • Taipale, J.1    Saharinen, J.2    Keski-Oja, J.3
  • 26
    • 0025161839 scopus 로고
    • Transforming growth factor-β regulates the splicing pattern of fibronectin messenger RNA precursor
    • Borsi L., Castellani P., Risso A., Leprini A., Zardi L. Transforming growth factor-β regulates the splicing pattern of fibronectin messenger RNA precursor. FEBS Lett. 261:1990;175-178.
    • (1990) FEBS Lett , vol.261 , pp. 175-178
    • Borsi, L.1    Castellani, P.2    Risso, A.3    Leprini, A.4    Zardi, L.5
  • 27
    • 0023834148 scopus 로고
    • Transforming growth factor-β regulates the expression and structure of extracellular matrix chondroitin/dermatan sulfate proteoglycans
    • Bassols A., Massague J. Transforming growth factor-β regulates the expression and structure of extracellular matrix chondroitin/dermatan sulfate proteoglycans. J Biol Chem. 263:1988;3039-3045.
    • (1988) J Biol Chem , vol.263 , pp. 3039-3045
    • Bassols, A.1    Massague, J.2
  • 28
    • 0031016797 scopus 로고    scopus 로고
    • Transforming growth factor-βs and wound healing
    • O'Kane S., Ferguson M. Transforming growth factor-βs and wound healing. Int J Biochem Cell Biol. 29:1997;63-78.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 63-78
    • O'Kane, S.1    Ferguson, M.2
  • 29
  • 30
    • 0028109801 scopus 로고
    • Transforming growth factor-β In tissue fibrosis
    • Border W., Noble N. Transforming growth factor-β in tissue fibrosis. N Engl J Med. 331:1994;1286-1292.
    • (1994) N Engl J Med , vol.331 , pp. 1286-1292
    • Border, W.1    Noble, N.2
  • 31
    • 0026447801 scopus 로고
    • Release of transforming growth factor-β1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin
    • Taipale J., Koli K., Keski-Oja J. Release of transforming growth factor-β1 from the pericellular matrix of cultured fibroblasts and fibrosarcoma cells by plasmin and thrombin. J Biol Chem. 267:1992;25,378-25,384.
    • (1992) J Biol Chem , vol.267 , pp. 25
    • Taipale, J.1    Koli, K.2    Keski-Oja, J.3
  • 32
    • 0028956737 scopus 로고
    • Human mast cell chymase and leukocyte elastase release latent transforming growth factor-β1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale J., Lohi J., Saharinen J., Kovanen P.T., Keski-Oja J. Human mast cell chymase and leukocyte elastase release latent transforming growth factor-β1 from the extracellular matrix of cultured human epithelial and endothelial cells. J Biol Chem. 259:1995;4689-4696.
    • (1995) J Biol Chem , vol.259 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saharinen, J.3    Kovanen, P.T.4    Keski-Oja, J.5
  • 34
    • 0021173481 scopus 로고
    • Normal embryo fibroblasts release transforming growth factors in a latent form
    • Lawrence D., Pircher R., Kryceve-Martinerie C., Jullien P. Normal embryo fibroblasts release transforming growth factors in a latent form. J Cell Physiol. 121:1984;184-188.
    • (1984) J Cell Physiol , vol.121 , pp. 184-188
    • Lawrence, D.1    Pircher, R.2    Kryceve-Martinerie, C.3    Jullien, P.4
  • 35
    • 0023732890 scopus 로고
    • Molecular events in the processing of recombinant type I pre-pro-transforming growth factor β to the mature polypeptide
    • Gentry L.E., Lioubin M.N., Purchio A.F., Marquardt H. Molecular events in the processing of recombinant type I pre-pro-transforming growth factor β to the mature polypeptide. Mol Cell Biol. 8:1988;4162-4168.
    • (1988) Mol Cell Biol , vol.8 , pp. 4162-4168
    • Gentry, L.E.1    Lioubin, M.N.2    Purchio, A.F.3    Marquardt, H.4
  • 36
    • 0025373853 scopus 로고
    • Requirement for activin A and transforming growth factor-β1 pro-regions in homodimer assembly
    • Gray A., Mason A. Requirement for activin A and transforming growth factor-β1 pro-regions in homodimer assembly. Science. 247:1990;1328-1330.
    • (1990) Science , vol.247 , pp. 1328-1330
    • Gray, A.1    Mason, A.2
  • 37
    • 0028906190 scopus 로고
    • Processing of transforming growth factor-β1 precursor by human furin convertase
    • Dubois C.M., Laprise M.H., Blanchette F., Gentry L.E., Leduc R. Processing of transforming growth factor-β1 precursor by human furin convertase. J Biol Chem. 270:1995;10,618-10,624.
    • (1995) J Biol Chem , vol.270 , pp. 10
    • Dubois, C.M.1    Laprise, M.H.2    Blanchette, F.3    Gentry, L.E.4    Leduc, R.5
  • 38
    • 0025324976 scopus 로고
    • The pro domain of pre-pro-transforming growth factor-β1 when independently expressed is a functional binding protein for the mature growth factor
    • Gentry L.E., Nash B.W. The pro domain of pre-pro-transforming growth factor-β1 when independently expressed is a functional binding protein for the mature growth factor. Biochemistry. 29:1990;6851-6857.
    • (1990) Biochemistry , vol.29 , pp. 6851-6857
    • Gentry, L.E.1    Nash, B.W.2
  • 39
    • 0030022404 scopus 로고    scopus 로고
    • Structural characterization of the latent complex between transforming growth factor β1 and β1-latency-associated peptide
    • McMahon G.A., Dignam J.D., Gentry L.E. Structural characterization of the latent complex between transforming growth factor β1 and β1-latency-associated peptide. Biochem J. 313:1996;343-351.
    • (1996) Biochem J , vol.313 , pp. 343-351
    • McMahon, G.A.1    Dignam, J.D.2    Gentry, L.E.3
  • 40
    • 0026667022 scopus 로고
    • Characterization of the binding of transforming growth factor-β1, -β2, and -β3 to recombinant β1-latency-associated peptide
    • Miller D.M., Ogawa Y., Iwata K.K., ten Dijke P., Purchio A.F., Soloff M.S., Gentry L.E. Characterization of the binding of transforming growth factor-β1, -β2, and -β3 to recombinant β1-latency-associated peptide. Mol Endocrinol. 6:1992;694-702.
    • (1992) Mol Endocrinol , vol.6 , pp. 694-702
    • Miller, D.M.1    Ogawa, Y.2    Iwata, K.K.3    Ten Dijke, P.4    Purchio, A.F.5    Soloff, M.S.6    Gentry, L.E.7
  • 41
    • 0023940794 scopus 로고
    • Latent high molecular weight complex of transforming growth factor-β1. Purification from human platelets and structural characterization
    • Miyazono K., Hellman U., Wernstedt C., Heldin C. Latent high molecular weight complex of transforming growth factor-β1. Purification from human platelets and structural characterization. J Biol Chem. 263:1988;6407-6415.
    • (1988) J Biol Chem , vol.263 , pp. 6407-6415
    • Miyazono, K.1    Hellman, U.2    Wernstedt, C.3    Heldin, C.4
  • 42
    • 0023886444 scopus 로고
    • Latent transforming growth factor-β From human platelets. A high molecular weight complex containing precursor sequences
    • Wakefield L., Smith D., Flanders K., Sporn M. Latent transforming growth factor-β from human platelets. A high molecular weight complex containing precursor sequences. J Biol Chem. 263:1988;7646-7654.
    • (1988) J Biol Chem , vol.263 , pp. 7646-7654
    • Wakefield, L.1    Smith, D.2    Flanders, K.3    Sporn, M.4
  • 44
    • 0025244163 scopus 로고
    • Molecular cloning of the large subunit of transforming growth factor type β masking protein and expression of the mRNA in various rat tissues
    • Tsuji T., Okada F., Yamaguchi K., Nakamura T. Molecular cloning of the large subunit of transforming growth factor type β masking protein and expression of the mRNA in various rat tissues. Proc Natl Acad Sci USA. 87:1990;8835-8839.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8835-8839
    • Tsuji, T.1    Okada, F.2    Yamaguchi, K.3    Nakamura, T.4
  • 45
    • 0027976521 scopus 로고
    • Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein
    • Taipale J., Miyazono K., Heldin C.H., Keski-Oja K. Latent transforming growth factor-β1 associates to fibroblast extracellular matrix via latent TGF-β binding protein. J Cell Biol. 124:1994;171-181.
    • (1994) J Cell Biol , vol.124 , pp. 171-181
    • Taipale, J.1    Miyazono, K.2    Heldin, C.H.3    Keski-Oja, K.4
  • 46
    • 0028302076 scopus 로고
    • Characterization and autoregulation of latent transforming growth factor-β (TGF-β) complexes in osteoblast-like cell lines. Production of a latent complex lacking the latent TGF-β-binding protein
    • Dallas S.L., Park-Snyder S., Miyazono K., Twardzik D., Mundy G.R., Bonewald L.F. Characterization and autoregulation of latent transforming growth factor-β (TGF-β) complexes in osteoblast-like cell lines. Production of a latent complex lacking the latent TGF-β-binding protein. J Biol Chem. 269:1994;6815-6821.
    • (1994) J Biol Chem , vol.269 , pp. 6815-6821
    • Dallas, S.L.1    Park-Snyder, S.2    Miyazono, K.3    Twardzik, D.4    Mundy, G.R.5    Bonewald, L.F.6
  • 47
    • 0026733616 scopus 로고
    • Transforming growth factor-β1, -β2, and -β3 secreted by a human glioblastoma cell line. Identification of small and different forms of large latent complexes
    • Olofsson A., Miyazono K., Kanzaki T., Colosetti P., Engstrom U., Heldin C.H. Transforming growth factor-β1, -β2, and -β3 secreted by a human glioblastoma cell line. Identification of small and different forms of large latent complexes. J Biol Chem. 267:1992;19,482-19,488.
    • (1992) J Biol Chem , vol.267 , pp. 19
    • Olofsson, A.1    Miyazono, K.2    Kanzaki, T.3    Colosetti, P.4    Engstrom, U.5    Heldin, C.H.6
  • 49
    • 0028857166 scopus 로고
    • Bovine latent transforming growth factor β1-binding protein 2: Molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils
    • Gibson M.A., Hatzinikolas G., Davis E.C., Baker E., Sutherland G.R., Mecham R.P. Bovine latent transforming growth factor β1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils. Mol Cell Biol. 15:1995;6932-6942.
    • (1995) Mol Cell Biol , vol.15 , pp. 6932-6942
    • Gibson, M.A.1    Hatzinikolas, G.2    Davis, E.C.3    Baker, E.4    Sutherland, G.R.5    Mecham, R.P.6
  • 51
    • 0031567592 scopus 로고    scopus 로고
    • Sequence and expression of a novel member (LTBP-4) of the family of latent transforming growth factor-β binding proteins
    • Giltay R., Kostka G., Timpi R. Sequence and expression of a novel member (LTBP-4) of the family of latent transforming growth factor-β binding proteins. FEBS Lett. 411:1997;164-168.
    • (1997) FEBS Lett , vol.411 , pp. 164-168
    • Giltay, R.1    Kostka, G.2    Timpi, R.3
  • 52
    • 0032540880 scopus 로고    scopus 로고
    • Identification and characterization of a new latent transforming growth factor-β-binding protein, LTBP-4
    • Saharinen J., Taipale J., Monni O., Keski-Oja J. Identification and characterization of a new latent transforming growth factor-β-binding protein, LTBP-4. J Biol Chem. 273:1998;18,439-18,469.
    • (1998) J Biol Chem , vol.273 , pp. 18
    • Saharinen, J.1    Taipale, J.2    Monni, O.3    Keski-Oja, J.4
  • 53
    • 0030943989 scopus 로고    scopus 로고
    • Latent transforming growth factor-β complex in Chinese hamster ovary cells contains the multifunctional cysteine-rich fibroblast growth factor receptor, also termed E-selection-ligand or MG-160
    • Olofsson A., Hellman U., ten Dijke P., Grimsby S., Ichijo H., Moren A., Miyazono K., Heldin C.H. Latent transforming growth factor-β complex in Chinese hamster ovary cells contains the multifunctional cysteine-rich fibroblast growth factor receptor, also termed E-selection-ligand or MG-160. Biochem J. 324:1997;427-434.
    • (1997) Biochem J , vol.324 , pp. 427-434
    • Olofsson, A.1    Hellman, U.2    Ten Dijke, P.3    Grimsby, S.4    Ichijo, H.5    Moren, A.6    Miyazono, K.7    Heldin, C.H.8
  • 54
    • 0025765844 scopus 로고
    • A role of the latent TGF-β1-binding protein in the assembly and secretion of TGF-β1
    • Miyazono K., Olofsson A., Colosetti P., Heldin C.H. A role of the latent TGF-β1-binding protein in the assembly and secretion of TGF-β1. EMBO J. 10:1991;1091-1101.
    • (1991) EMBO J , vol.10 , pp. 1091-1101
    • Miyazono, K.1    Olofsson, A.2    Colosetti, P.3    Heldin, C.H.4
  • 55
    • 0026701960 scopus 로고
    • Retention of the transforming growth factor-β1 precursor in the Golgi complex in a latent endoglycosidase H-sensitive form
    • Miyazono K., Thyberg J., Heldin C.H. Retention of the transforming growth factor-β1 precursor in the Golgi complex in a latent endoglycosidase H-sensitive form. J Biol Chem. 267:1992;5668-5675.
    • (1992) J Biol Chem , vol.267 , pp. 5668-5675
    • Miyazono, K.1    Thyberg, J.2    Heldin, C.H.3
  • 56
    • 0029813731 scopus 로고    scopus 로고
    • Latent transforming growth factor-β1 and its binding protein are components of extracellular matrix microfibrils
    • Taipale J., Saharinen J., Hedman K., Keski-Oja J. Latent transforming growth factor-β1 and its binding protein are components of extracellular matrix microfibrils. J Histochem Cytochem. 44:1996;875-889.
    • (1996) J Histochem Cytochem , vol.44 , pp. 875-889
    • Taipale, J.1    Saharinen, J.2    Hedman, K.3    Keski-Oja, J.4
  • 57
    • 0029565595 scopus 로고
    • Efficient association of an amino-terminally extended form of human latent transforming growth factor-β binding protein with the extracellular matrix
    • Olofsson A., Ichijo H., Moren A., ten Dijke P., Miyazono K., Heldin C.H. Efficient association of an amino-terminally extended form of human latent transforming growth factor-β binding protein with the extracellular matrix. J Biol Chem. 270:1995;31,294-31,297.
    • (1995) J Biol Chem , vol.270 , pp. 31
    • Olofsson, A.1    Ichijo, H.2    Moren, A.3    Ten Dijke, P.4    Miyazono, K.5    Heldin, C.H.6
  • 58
    • 0028885716 scopus 로고
    • Dual role for the latent transforming growth factor-β binding protein in storage of latent TGF-β In the extracellular matrix and as a structural matrix protein
    • Dallas S.L., Miyazono K., Skerry T.M., Mundy G.R., Bonewald L.F. Dual role for the latent transforming growth factor-β binding protein in storage of latent TGF-β in the extracellular matrix and as a structural matrix protein. J Cell Biol. 131:1995;539-549.
    • (1995) J Cell Biol , vol.131 , pp. 539-549
    • Dallas, S.L.1    Miyazono, K.2    Skerry, T.M.3    Mundy, G.R.4    Bonewald, L.F.5
  • 59
    • 0030058699 scopus 로고    scopus 로고
    • Association of the small latent transforming growth factor-β With an eight cysteine repeat of its binding protein LTBP-1
    • Saharinen J., Taipale J., Keski-Oja J. Association of the small latent transforming growth factor-β with an eight cysteine repeat of its binding protein LTBP-1. EMBO J. 15:1996;245-253.
    • (1996) EMBO J , vol.15 , pp. 245-253
    • Saharinen, J.1    Taipale, J.2    Keski-Oja, J.3
  • 60
    • 0021720359 scopus 로고
    • Growth inhibitor from BSC-1 cells closely related to platelet type-β transforming growth factor
    • Tucker R., Shipley G., Moses H., Holley R. Growth inhibitor from BSC-1 cells closely related to platelet type-β transforming growth factor. Science. 226:1984;705-707.
    • (1984) Science , vol.226 , pp. 705-707
    • Tucker, R.1    Shipley, G.2    Moses, H.3    Holley, R.4
  • 61
    • 0029097036 scopus 로고
    • Identification of a transforming growth factor-β-1 activator derived from a human gastric cancer cell line
    • Horimoto M., Kato J., Takimoto R., Terui T., Mogi Y., Niitsu Y. Identification of a transforming growth factor-β-1 activator derived from a human gastric cancer cell line. Br J Cancer. 72:1995;676-682.
    • (1995) Br J Cancer , vol.72 , pp. 676-682
    • Horimoto, M.1    Kato, J.2    Takimoto, R.3    Terui, T.4    Mogi, Y.5    Niitsu, Y.6
  • 62
    • 0022335318 scopus 로고
    • Conversion of a high molecular weight latent β-TGF from chicken embryo fibroblasts into a low molecular weight active β-TGF under acidic conditions
    • Lawrence D., Pircher R., Jullien P. Conversion of a high molecular weight latent β-TGF from chicken embryo fibroblasts into a low molecular weight active β-TGF under acidic conditions. Biochem Biophys Res Commun. 133:1985;1026-1034.
    • (1985) Biochem Biophys Res Commun , vol.133 , pp. 1026-1034
    • Lawrence, D.1    Pircher, R.2    Jullien, P.3
  • 63
    • 0024994691 scopus 로고
    • Physicochemical activation of recombinant latent transforming growth factor-β's 1, 2 and 3
    • Brown P., Wakefield L., Levinson A., Sporn M. Physicochemical activation of recombinant latent transforming growth factor-β's 1, 2 and 3. Growth Factors. 3:1990;35-43.
    • (1990) Growth Factors , vol.3 , pp. 35-43
    • Brown, P.1    Wakefield, L.2    Levinson, A.3    Sporn, M.4
  • 64
    • 0023916551 scopus 로고
    • Proteolytic activation of latent transforming growth factor-β From fibroblast-conditioned medium
    • Lyons R., Keski-Oja J., Moses H. Proteolytic activation of latent transforming growth factor-β from fibroblast-conditioned medium. J Cell Biol. 106:1988;1659-1665.
    • (1988) J Cell Biol , vol.106 , pp. 1659-1665
    • Lyons, R.1    Keski-Oja, J.2    Moses, H.3
  • 65
    • 0025215307 scopus 로고
    • Mechanism of activation of latent recombinant transforming growth factor-β1 by plasmin
    • Lyons R., Gentry L.E., Purchio A.F., Moses H.L. Mechanism of activation of latent recombinant transforming growth factor-β1 by plasmin. J Cell Biol. 110:1990;1361-1367.
    • (1990) J Cell Biol , vol.110 , pp. 1361-1367
    • Lyons, R.1    Gentry, L.E.2    Purchio, A.F.3    Moses, H.L.4
  • 66
    • 0031891656 scopus 로고    scopus 로고
    • Cell-associated activation of latent transforming growth factor-β By calpain
    • Abe M., Oda N., Sato Y. Cell-associated activation of latent transforming growth factor-β by calpain. J Cell Physiol. 174:1998;186-193.
    • (1998) J Cell Physiol , vol.174 , pp. 186-193
    • Abe, M.1    Oda, N.2    Sato, Y.3
  • 67
    • 0024360471 scopus 로고
    • Acidic cellular environments: Activation of latent TGF-β And sensitization of cellular response to TGF-β And EGF
    • Jullien P., Berg T., Lawrence D. Acidic cellular environments: activation of latent TGF-β and sensitization of cellular response to TGF-β and EGF. Int J Cancer. 43:1989;886-891.
    • (1989) Int J Cancer , vol.43 , pp. 886-891
    • Jullien, P.1    Berg, T.2    Lawrence, D.3
  • 68
    • 0027305971 scopus 로고
    • Thrombospondin causes activation of latent transforming growth factor-β secreted by endothelial cells by a novel mechanism
    • Schultz-Cherry S., Murphy-Ullrich J. Thrombospondin causes activation of latent transforming growth factor-β secreted by endothelial cells by a novel mechanism. J Cell Biol. 122:1993;923-932.
    • (1993) J Cell Biol , vol.122 , pp. 923-932
    • Schultz-Cherry, S.1    Murphy-Ullrich, J.2
  • 69
    • 0027967771 scopus 로고
    • Thrombospondin binds and activates the small and large forms of latent transforming growth factor-β In a chemically defined system
    • Schultz-Cherry S., Ribeiro S., Gentry L., Murphy-Ullrich J.E. Thrombospondin binds and activates the small and large forms of latent transforming growth factor-β in a chemically defined system. J Biol Chem. 269:1994;26,775-26,782.
    • (1994) J Biol Chem , vol.269 , pp. 26
    • Schultz-Cherry, S.1    Ribeiro, S.2    Gentry, L.3    Murphy-Ullrich, J.E.4
  • 70
    • 0028138619 scopus 로고
    • The type 1 repeats of thrombospondin 1 activate latent transforming growth factor-β
    • Schultz-Cherry S., Lawler J., Murphy-Ullrich J.E. The type 1 repeats of thrombospondin 1 activate latent transforming growth factor-β J Biol Chem. 269:1994;26,783-26,788.
    • (1994) J Biol Chem , vol.269 , pp. 26
    • Schultz-Cherry, S.1    Lawler, J.2    Murphy-Ullrich, J.E.3
  • 72
    • 0029736871 scopus 로고    scopus 로고
    • Redox-mediated activation of latent transforming growth factor-β1
    • Barcellos-Hoff M., Dix T. Redox-mediated activation of latent transforming growth factor-β1. Mol Endocrinol. 10:1996;1077-1083.
    • (1996) Mol Endocrinol , vol.10 , pp. 1077-1083
    • Barcellos-Hoff, M.1    Dix, T.2
  • 73
    • 0024539847 scopus 로고
    • Role for carbohydrate structures in TGF-β1 latency
    • Miyazono K., Heldin C. Role for carbohydrate structures in TGF-β1 latency. Nature. 338:1989;158-160.
    • (1989) Nature , vol.338 , pp. 158-160
    • Miyazono, K.1    Heldin, C.2
  • 74
    • 0024755673 scopus 로고
    • Retinoic acid induces transforming growth factor-β2 in cultured keratinocytes and mouse epidermis
    • Glick A., Flanders K., Danielpour D., Yuspa S., Sporn M. Retinoic acid induces transforming growth factor-β2 in cultured keratinocytes and mouse epidermis. Cell Regul. 1:1989;87-97.
    • (1989) Cell Regul , vol.1 , pp. 87-97
    • Glick, A.1    Flanders, K.2    Danielpour, D.3    Yuspa, S.4    Sporn, M.5
  • 75
    • 0027340165 scopus 로고
    • Vitamin D3 and calcipotriol enhance the secretion of transforming growth factor-β1 and β2 in cultured murine keratinocytes
    • Koli K., Keski-Oja J. Vitamin D3 and calcipotriol enhance the secretion of transforming growth factor-β1 and β2 in cultured murine keratinocytes. Growth Factors. 8:1993;153-163.
    • (1993) Growth Factors , vol.8 , pp. 153-163
    • Koli, K.1    Keski-Oja, J.2
  • 76
    • 0023625418 scopus 로고
    • Evidence that transforming growth factor-β is a hormonally regulated negative growth factor in human breast cancer
    • Knabbe C., Lippman M., Wakefield L., Flanders K., Kasid A., Derynck R., Dickson R. Evidence that transforming growth factor-β is a hormonally regulated negative growth factor in human breast cancer. Cell. 48:1987;417-418.
    • (1987) Cell , vol.48 , pp. 417-418
    • Knabbe, C.1    Lippman, M.2    Wakefield, L.3    Flanders, K.4    Kasid, A.5    Derynck, R.6    Dickson, R.7
  • 78
    • 0027420659 scopus 로고
    • Glucocorticoid-induced activation of latent transforming growth factor-β By normal hormone osteoblast-like cell
    • Oursler M., Riggs B., Spelsberg T. Glucocorticoid-induced activation of latent transforming growth factor-β by normal hormone osteoblast-like cell. Endocrinology. 133:1993;2187-2196.
    • (1993) Endocrinology , vol.133 , pp. 2187-2196
    • Oursler, M.1    Riggs, B.2    Spelsberg, T.3
  • 79
    • 0029034384 scopus 로고
    • Mediation of glucocorticoid receptor function by the activation of latent transforming growth factor-β1 in MG-63 human osteosarcoma cells
    • Boulanger J., Reyes-Moreno C., Koutsilieris M. Mediation of glucocorticoid receptor function by the activation of latent transforming growth factor-β1 in MG-63 human osteosarcoma cells. Int J Cancer. 61:1995;692-697.
    • (1995) Int J Cancer , vol.61 , pp. 692-697
    • Boulanger, J.1    Reyes-Moreno, C.2    Koutsilieris, M.3
  • 80
    • 0001505189 scopus 로고
    • An activated form of transforming growth factor-β is produced by cocultures of endothelial cells and pericytes
    • Antonelli-Orlidge A., Saunders K., Smith S., D'Amore P. An activated form of transforming growth factor-β is produced by cocultures of endothelial cells and pericytes. Proc Natl Acad Sci USA. 86:1989;4544-4548.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4544-4548
    • Antonelli-Orlidge, A.1    Saunders, K.2    Smith, S.3    D'Amore, P.4
  • 81
    • 0024382711 scopus 로고
    • Inhibition of endothelial cell movement by pericytes and smooth muscle cells: Activation of a latent transforming growth factor-β1-like molecule by plasmin during co-culture
    • Sato Y., Rifkin D. Inhibition of endothelial cell movement by pericytes and smooth muscle cells: activation of a latent transforming growth factor-β1-like molecule by plasmin during co-culture. J Cell Biol. 109:1989;309-315.
    • (1989) J Cell Biol , vol.109 , pp. 309-315
    • Sato, Y.1    Rifkin, D.2
  • 82
    • 0025310993 scopus 로고
    • Characterization of the activation of latent TGF-β By co-cultures of endothelial cells and pericytes or smooth muscle cells: A self-regulating system
    • Sato Y., Tsuboi R., Lyons R., Moses H., Rifkin D. Characterization of the activation of latent TGF-β by co-cultures of endothelial cells and pericytes or smooth muscle cells: a self-regulating system. J Cell Biol. 111:1990;757-763.
    • (1990) J Cell Biol , vol.111 , pp. 757-763
    • Sato, Y.1    Tsuboi, R.2    Lyons, R.3    Moses, H.4    Rifkin, D.5
  • 83
    • 0026536584 scopus 로고
    • Protease inhibitors interfere with the transforming growth factor-β-dependent but not the transforming growth factor-β-independent pathway of tumor cell-mediated immunosuppression
    • Huber D., Philipp J., Fontana A. Protease inhibitors interfere with the transforming growth factor-β-dependent but not the transforming growth factor-β-independent pathway of tumor cell-mediated immunosuppression. J Immunol. 148:1992;277-284.
    • (1992) J Immunol , vol.148 , pp. 277-284
    • Huber, D.1    Philipp, J.2    Fontana, A.3
  • 84
    • 0026059613 scopus 로고
    • Cellular activation of latent transforming growth factor-β requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor
    • Dennis P., Rifkin D. Cellular activation of latent transforming growth factor-β requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor. Proc Natl Acad Sci USA. 88:1991;580-584.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 580-584
    • Dennis, P.1    Rifkin, D.2
  • 85
    • 0024410147 scopus 로고
    • A role for the insulin-like growth factor II/mannose-6-phosphate receptor in the insulin-induced inhibition of protein catabolism
    • Kovacina K., Steele-Perkins G., Roth R. A role for the insulin-like growth factor II/mannose-6-phosphate receptor in the insulin-induced inhibition of protein catabolism. Mol Endocrinol. 3:1989;901-906.
    • (1989) Mol Endocrinol , vol.3 , pp. 901-906
    • Kovacina, K.1    Steele-Perkins, G.2    Roth, R.3
  • 86
    • 0027427964 scopus 로고
    • The mechanism for the activation of latent TGF-β During co-culture of endothelial cells and smooth muscle cells: Cell-type specific targeting of latent TGF-β To smooth muscle cells
    • Sato Y., Okada F., Abe M., Seguchi T., Kuwano M., Sato S., Furuya A., Hanai N., Tamaoki T. The mechanism for the activation of latent TGF-β during co-culture of endothelial cells and smooth muscle cells: cell-type specific targeting of latent TGF-β to smooth muscle cells. J Cell Biol. 123:1993;1249-1254.
    • (1993) J Cell Biol , vol.123 , pp. 1249-1254
    • Sato, Y.1    Okada, F.2    Abe, M.3    Seguchi, T.4    Kuwano, M.5    Sato, S.6    Furuya, A.7    Hanai, N.8    Tamaoki, T.9
  • 87
    • 0027976511 scopus 로고
    • Betaglycan can act as a dual modulator of TGF-β access to signaling receptors: Mapping of ligand binding and GAG attachment sites
    • Lopez-Casillas F., Payne H.M., Andres J.L., Massague J. Betaglycan can act as a dual modulator of TGF-β access to signaling receptors: mapping of ligand binding and GAG attachment sites. J Cell Biol. 124:1994;557-568.
    • (1994) J Cell Biol , vol.124 , pp. 557-568
    • Lopez-Casillas, F.1    Payne, H.M.2    Andres, J.L.3    Massague, J.4
  • 88
    • 0027968569 scopus 로고
    • Plasmin cleaves betaglycan and releases a 60 kDa transforming growth factor-β complex from the cell surface
    • Lamarre J., Vasudevan J., Gonias S. Plasmin cleaves betaglycan and releases a 60 kDa transforming growth factor-β complex from the cell surface. Biochem J. 302:1994;199-205.
    • (1994) Biochem J , vol.302 , pp. 199-205
    • Lamarre, J.1    Vasudevan, J.2    Gonias, S.3
  • 89
    • 0027413768 scopus 로고
    • Cranial neural crest cells synthesize and secrete a latent form of transforming growth factor-β that can be activated by neural crest cell proteolysis
    • Brauer P., Yee J. Cranial neural crest cells synthesize and secrete a latent form of transforming growth factor-β that can be activated by neural crest cell proteolysis. Dev Biol. 155:1993;281-285.
    • (1993) Dev Biol , vol.155 , pp. 281-285
    • Brauer, P.1    Yee, J.2
  • 91
    • 0029067419 scopus 로고
    • The receptor for urokinase-type plasminogen activator is not essential for mouse development or fertility
    • Bugge T., Suh T., Flick M., Daugherty C., Romer J., Solberg H., Ellis V., Dano K., Degen J. The receptor for urokinase-type plasminogen activator is not essential for mouse development or fertility. J Biol Chem. 270:1995;16,886-16,894.
    • (1995) J Biol Chem , vol.270 , pp. 16
    • Bugge, T.1    Suh, T.2    Flick, M.3    Daugherty, C.4    Romer, J.5    Solberg, H.6    Ellis, V.7    Dano, K.8    Degen, J.9
  • 92
    • 0027077495 scopus 로고
    • Transforming growth factor-β complexes with thrombospondin
    • Murphy-Ullrich J., Schultz-Cherry S., Höök M. Transforming growth factor-β complexes with thrombospondin. Mol Biol Cell. 3:1992;181-188.
    • (1992) Mol Biol Cell , vol.3 , pp. 181-188
    • Murphy-Ullrich, J.1    Schultz-Cherry, S.2    Höök, M.3
  • 93
    • 0030820363 scopus 로고    scopus 로고
    • Role of carbohydrate structures in the binding of β1-latency-associated peptide to ligands
    • Yang Y., Dignam J., Gentry L. Role of carbohydrate structures in the binding of β1-latency-associated peptide to ligands. Biochemistry. 36:1997;11,923-11,932.
    • (1997) Biochemistry , vol.36 , pp. 11
    • Yang, Y.1    Dignam, J.2    Gentry, L.3
  • 97
    • 0031773016 scopus 로고    scopus 로고
    • Two hybrid analysis reveals multiple direct interactions for thrombospondin 1
    • in process citation
    • Aho S., Uitto J. Two hybrid analysis reveals multiple direct interactions for thrombospondin 1. Matrix Biol. 17:1998;401-412. in process citation.
    • (1998) Matrix Biol , vol.17 , pp. 401-412
    • Aho, S.1    Uitto, J.2
  • 100
    • 0030770411 scopus 로고    scopus 로고
    • Latent transforming growth factor-β1 activation in situ: Quantitative and functional evidence after low-dose gamma-irradiation
    • Ehrhart E., Segarini P., Tsang M., Carroll A., Barcellos-Hoff M. Latent transforming growth factor-β1 activation in situ: quantitative and functional evidence after low-dose gamma-irradiation. FASEB J. 11:1997;991-1002.
    • (1997) FASEB J , vol.11 , pp. 991-1002
    • Ehrhart, E.1    Segarini, P.2    Tsang, M.3    Carroll, A.4    Barcellos-Hoff, M.5
  • 102
    • 0028177037 scopus 로고
    • Transforming growth factor-β activation in irradiated murine mammary gland
    • Barcellos-Hoff M., Derynck R., Tsang M., Weatherbee J. Transforming growth factor-β activation in irradiated murine mammary gland. J Clin Invest. 93:1994;892-899.
    • (1994) J Clin Invest , vol.93 , pp. 892-899
    • Barcellos-Hoff, M.1    Derynck, R.2    Tsang, M.3    Weatherbee, J.4
  • 103
    • 0027476156 scopus 로고
    • Role of the latent TGF-β binding protein in the activation of latent TGF-β By co-cultures of endothelial and smooth muscle cells
    • Flaumenhaft R., Abe M., Sato Y., Miyazono K., Harpel J., Heldin C.H., Rifkin D.B. Role of the latent TGF-β binding protein in the activation of latent TGF-β by co-cultures of endothelial and smooth muscle cells. J Cell Biol. 120:1993;995-1002.
    • (1993) J Cell Biol , vol.120 , pp. 995-1002
    • Flaumenhaft, R.1    Abe, M.2    Sato, Y.3    Miyazono, K.4    Harpel, J.5    Heldin, C.H.6    Rifkin, D.B.7
  • 104
    • 0030974902 scopus 로고    scopus 로고
    • Latent transforming growth factor-β binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-β
    • Nunes I., Gleizes P.E., Metz C.N., Rifkin D.B. Latent transforming growth factor-β binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-β J Cell Biol. 136:1997;1151-1163.
    • (1997) J Cell Biol , vol.136 , pp. 1151-1163
    • Nunes, I.1    Gleizes, P.E.2    Metz, C.N.3    Rifkin, D.B.4
  • 105
    • 0027419881 scopus 로고
    • Requirement for transglutaminase in the activation of latent transforming growth factor-β In bovine endothelial cells
    • Kojima S., Nara K., Rifkin D. Requirement for transglutaminase in the activation of latent transforming growth factor-β in bovine endothelial cells. J Cell Biol. 121:1993;439-448.
    • (1993) J Cell Biol , vol.121 , pp. 439-448
    • Kojima, S.1    Nara, K.2    Rifkin, D.3
  • 106
    • 0028984569 scopus 로고
    • Characterization of latent TGF-β activation by murine peritoneal macrophages
    • Nunes I., Shapiro R.L., Rifkin D.B. Characterization of latent TGF-β activation by murine peritoneal macrophages. J Immunol. 155:1995;1450-1459.
    • (1995) J Immunol , vol.155 , pp. 1450-1459
    • Nunes, I.1    Shapiro, R.L.2    Rifkin, D.B.3
  • 107
    • 0022976357 scopus 로고
    • Enhanced production and extracellular deposition of the endothelial-type plasminogen activator inhibitor in cultured human lung fibroblasts by transforming growth factor-β
    • Laiho M., Saksela O., Andreasen P., Keski-Oja J. Enhanced production and extracellular deposition of the endothelial-type plasminogen activator inhibitor in cultured human lung fibroblasts by transforming growth factor-β J Cell Biol. 106:1986;2403-2410.
    • (1986) J Cell Biol , vol.106 , pp. 2403-2410
    • Laiho, M.1    Saksela, O.2    Andreasen, P.3    Keski-Oja, J.4
  • 108
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massague J. TGF-β signal transduction. Annu Rev Biochem. 67:1998;753-791.
    • (1998) Annu Rev Biochem , vol.67 , pp. 753-791
    • Massague, J.1
  • 109
    • 0025833740 scopus 로고
    • Isoform-specific transforming growth factor-β binding proteins with membrane attachments sensitive to phosphatidylinositol-specific phospholipase C
    • Cheifetz S., Massague J. Isoform-specific transforming growth factor-β binding proteins with membrane attachments sensitive to phosphatidylinositol-specific phospholipase C. J Biol Chem. 266:1991;20,767-20,772.
    • (1991) J Biol Chem , vol.266 , pp. 20
    • Cheifetz, S.1    Massague, J.2
  • 110
    • 0026543813 scopus 로고
    • Two novel patterns of transforming growth factor-β (TGF-β) binding to cell surface proteins are dependent upon the binding of TGF-β1 and indicate a mechanism of positive cooperativity
    • Segarini P., Ziman J., Kane C., Dasch J. Two novel patterns of transforming growth factor-β (TGF-β) binding to cell surface proteins are dependent upon the binding of TGF-β1 and indicate a mechanism of positive cooperativity. J Biol Chem. 267:1992;1048-1053.
    • (1992) J Biol Chem , vol.267 , pp. 1048-1053
    • Segarini, P.1    Ziman, J.2    Kane, C.3    Dasch, J.4
  • 111
    • 0027321319 scopus 로고
    • A 60-kD protein mediates the binding of transforming growth factor-β To cell surface and extracellular matrix proteoglycans
    • Butzow R., Fukushima D., Twardzik D., Ruoslahti E. A 60-kD protein mediates the binding of transforming growth factor-β to cell surface and extracellular matrix proteoglycans. J Cell Biol. 122:1993;721-727.
    • (1993) J Cell Biol , vol.122 , pp. 721-727
    • Butzow, R.1    Fukushima, D.2    Twardzik, D.3    Ruoslahti, E.4
  • 112
    • 0023193194 scopus 로고
    • Latent transforming growth factor-β In serum. A specific complex with alpha 2-macroglobulin
    • O'Connor-McCourt M., Wakefield L. Latent transforming growth factor-β in serum. A specific complex with alpha 2-macroglobulin. J Biol Chem. 262:1987;14,090-14,099.
    • (1987) J Biol Chem , vol.262 , pp. 14
    • O'Connor-Mccourt, M.1    Wakefield, L.2
  • 113
    • 0023240580 scopus 로고
    • Fibronectin-associated transforming growth factor
    • Fava R., McClure D. Fibronectin-associated transforming growth factor. J Cell Biol. 131:1987;184-189.
    • (1987) J Cell Biol , vol.131 , pp. 184-189
    • Fava, R.1    McClure, D.2
  • 114
    • 0026082034 scopus 로고
    • Transforming growth factor-β type 1 binds to collagen VI of basement membrane matrix: Implications for development
    • Paralkar V., Vukicevic S., Reddi A. Transforming growth factor-β type 1 binds to collagen VI of basement membrane matrix: implications for development. Dev Biol. 143:1991;303-308.
    • (1991) Dev Biol , vol.143 , pp. 303-308
    • Paralkar, V.1    Vukicevic, S.2    Reddi, A.3
  • 115
    • 0023473081 scopus 로고
    • Hepatic processing of transforming growth factor-β In the rat. Uptake, metabolism, and biliary excretion
    • Coffey R., Kost L., Lyons R., LaRusso N. Hepatic processing of transforming growth factor-β in the rat. Uptake, metabolism, and biliary excretion. J Clin Invest. 80:1987;750-757.
    • (1987) J Clin Invest , vol.80 , pp. 750-757
    • Coffey, R.1    Kost, L.2    Lyons, R.3    Larusso, N.4
  • 116
    • 0025632985 scopus 로고
    • Recombinant latent transforming growth factor-β1 has a longer plasma half-life in rats than active transforming growth factor-β1, and a different tissue distribution
    • Wakefield L., Winokur T., Hollands R., Christopherson K., Levinson A., Sporn M. Recombinant latent transforming growth factor-β1 has a longer plasma half-life in rats than active transforming growth factor-β1, and a different tissue distribution. J Clin Invest. 86:1990;1976-1984.
    • (1990) J Clin Invest , vol.86 , pp. 1976-1984
    • Wakefield, L.1    Winokur, T.2    Hollands, R.3    Christopherson, K.4    Levinson, A.5    Sporn, M.6
  • 117
    • 0025791977 scopus 로고
    • 2-macroglobulin. Role in transforming growth factor-β1 clearance
    • 2-macroglobulin. Role in transforming growth factor-β1 clearance. J Biol Chem. 266:1991;22,290-22,296.
    • (1991) J Biol Chem , vol.266 , pp. 22
    • Philip, A.1    O'Connor-Mccourt, M.2
  • 118
    • 0026701412 scopus 로고
    • Identification of multiple active growth factors in basement membrane Matrigel suggests caution in interpretation of cellular activity related to extracellular matrix components
    • Vukicevic S., Kleinman H., Luyten F., Roberts A., Roche N., Reddi A. Identification of multiple active growth factors in basement membrane Matrigel suggests caution in interpretation of cellular activity related to extracellular matrix components. Exp Cell Res. 202:1992;1-8.
    • (1992) Exp Cell Res , vol.202 , pp. 1-8
    • Vukicevic, S.1    Kleinman, H.2    Luyten, F.3    Roberts, A.4    Roche, N.5    Reddi, A.6
  • 119
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor-β
    • Hildebrand A., Romaris M., Rasmussen L., Heinegard D., Twardzik D., Border W., Ruoslahti E. Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor-β Biochem J. 302:1994;527-534.
    • (1994) Biochem J , vol.302 , pp. 527-534
    • Hildebrand, A.1    Romaris, M.2    Rasmussen, L.3    Heinegard, D.4    Twardzik, D.5    Border, W.6    Ruoslahti, E.7
  • 120
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-β By the proteoglycan decorin
    • Yamaguchi Y., Mann D., Ruoslahti E. Negative regulation of transforming growth factor-β by the proteoglycan decorin. Nature. 346:1990;281-284.
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.2    Ruoslahti, E.3
  • 121
    • 0026676859 scopus 로고
    • Natural inhibitor of transforming growth factor-β protects against scarring in experimental kidney disease
    • Border W., Noble N., Yamamoto T., Harper J., Yamaguchi Y., Pierschbacher M., Ruoslahti E. Natural inhibitor of transforming growth factor-β protects against scarring in experimental kidney disease. Nature. 360:1992;361-364.
    • (1992) Nature , vol.360 , pp. 361-364
    • Border, W.1    Noble, N.2    Yamamoto, T.3    Harper, J.4    Yamaguchi, Y.5    Pierschbacher, M.6    Ruoslahti, E.7
  • 122
    • 0028600614 scopus 로고
    • Bone matrix decorin binds transforming growth factor-β And enhances its bioactivity
    • Takeuchi Y., Kodama Y., Matsumoto T. Bone matrix decorin binds transforming growth factor-β and enhances its bioactivity. J Biol Chem. 269:1994;32,634-32,638.
    • (1994) J Biol Chem , vol.269 , pp. 32
    • Takeuchi, Y.1    Kodama, Y.2    Matsumoto, T.3
  • 123
    • 0025989562 scopus 로고
    • Expression cloning and characterization of the TGF-β type III receptor
    • Wang X., Lin H., Ng-Eaton E., Downward J., Lodish H., Weinberg R. Expression cloning and characterization of the TGF-β type III receptor. Cell. 67:1991;797-805.
    • (1991) Cell , vol.67 , pp. 797-805
    • Wang, X.1    Lin, H.2    Ng-Eaton, E.3    Downward, J.4    Lodish, H.5    Weinberg, R.6
  • 124
    • 0026646785 scopus 로고
    • Endoglin is a component of the transforming growth factor-β receptor system in human endothelial cells
    • Cheifetz S., Bellon T., Cales C., Vera S., Bernabeu C., Massague J., Letarte M. Endoglin is a component of the transforming growth factor-β receptor system in human endothelial cells. J Biol Chem. 267:1992;19,027-19,030.
    • (1992) J Biol Chem , vol.267 , pp. 19
    • Cheifetz, S.1    Bellon, T.2    Cales, C.3    Vera, S.4    Bernabeu, C.5    Massague, J.6    Letarte, M.7
  • 125
    • 0028231917 scopus 로고
    • Molecular characterization and in situ localization of murine endoglin reveal that it is a transforming growth factor-β binding protein of endothelial and stromal cells
    • St-Jacques S., Cymerman U., Pece N., Letarte M. Molecular characterization and in situ localization of murine endoglin reveal that it is a transforming growth factor-β binding protein of endothelial and stromal cells. Endocrinology. 134:1994;2645-2657.
    • (1994) Endocrinology , vol.134 , pp. 2645-2657
    • St-Jacques, S.1    Cymerman, U.2    Pece, N.3    Letarte, M.4
  • 126
    • 0031081790 scopus 로고    scopus 로고
    • TGF-β receptors and signal transduction
    • Miyazono K. TGF-β receptors and signal transduction. Int J Hematol. 65:1997;97-104.
    • (1997) Int J Hematol , vol.65 , pp. 97-104
    • Miyazono, K.1
  • 127
  • 128
    • 0029066003 scopus 로고
    • Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor-β2
    • Sankar S., Mahooti-Brooks N., Centrella M., McCarthy T., Madri J. Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor-β2. J Biol Chem. 270:1995;13,567-13,572.
    • (1995) J Biol Chem , vol.270 , pp. 13
    • Sankar, S.1    Mahooti-Brooks, N.2    Centrella, M.3    McCarthy, T.4    Madri, J.5
  • 129
    • 0024792629 scopus 로고
    • Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-β
    • Andres J.L., Stanley K., Cheifetz S., Massague J. Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-β J Cell Biol. 109:1989;3137-3145.
    • (1989) J Cell Biol , vol.109 , pp. 3137-3145
    • Andres, J.L.1    Stanley, K.2    Cheifetz, S.3    Massague, J.4
  • 130
    • 0032170354 scopus 로고    scopus 로고
    • Immunodetection and characterisation of soluble CD105-TGF-β complexes
    • Li C., Wilson P., Bernabeu C., Raab U., Wang J., Kumar S. Immunodetection and characterisation of soluble CD105-TGF-β complexes. J Immunol Methods. 218:1998;85-93.
    • (1998) J Immunol Methods , vol.218 , pp. 85-93
    • Li, C.1    Wilson, P.2    Bernabeu, C.3    Raab, U.4    Wang, J.5    Kumar, S.6
  • 131
    • 0026776936 scopus 로고
    • Transforming growth factor-β1 is a heparin-binding protein: Identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-β1
    • McCaffrey T., Falcone D., Du B. Transforming growth factor-β1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-β1. J Cell Physiol. 152:1992;430-440.
    • (1992) J Cell Physiol , vol.152 , pp. 430-440
    • McCaffrey, T.1    Falcone, D.2    Du, B.3
  • 132
    • 0023608383 scopus 로고
    • Immunodetection and modulation of cellular growth with antibodies against native transforming growth factor-β1
    • Keski-Oja J., Lyons R., Moses H. Immunodetection and modulation of cellular growth with antibodies against native transforming growth factor-β1. Cancer Res. 47:1987;6451-6458.
    • (1987) Cancer Res , vol.47 , pp. 6451-6458
    • Keski-Oja, J.1    Lyons, R.2    Moses, H.3
  • 133
    • 0030856858 scopus 로고    scopus 로고
    • Characterization of a 60-kDa cell surface-associated transforming growth factor-β binding protein that can interfere with transforming growth factor-β receptor binding
    • Piek E., Franzen P., Heldin C.H., ten Dijke P. Characterization of a 60-kDa cell surface-associated transforming growth factor-β binding protein that can interfere with transforming growth factor-β receptor binding. J Cell Physiol. 173:1997;447-459.
    • (1997) J Cell Physiol , vol.173 , pp. 447-459
    • Piek, E.1    Franzen, P.2    Heldin, C.H.3    Ten Dijke, P.4
  • 134
    • 0031459117 scopus 로고    scopus 로고
    • Mouse latent TGF-β binding protein-2: Molecular cloning and developmental expression
    • Fang J., Li X., Smiley E., Francke U., Mecham R.P., Bonadio J. Mouse latent TGF-β binding protein-2: molecular cloning and developmental expression. Biochim Biophys Acta. 1354:1997;219-230.
    • (1997) Biochim Biophys Acta , vol.1354 , pp. 219-230
    • Fang, J.1    Li, X.2    Smiley, E.3    Francke, U.4    Mecham, R.P.5    Bonadio, J.6
  • 135
    • 0027422979 scopus 로고
    • Extracellular matrix 4: The elastic fiber
    • Rosenbloom J., Abrams W.R., Mecham R. Extracellular matrix 4: the elastic fiber. FASEB J. 7:1993;1208-1218.
    • (1993) FASEB J , vol.7 , pp. 1208-1218
    • Rosenbloom, J.1    Abrams, W.R.2    Mecham, R.3
  • 136
    • 0028929503 scopus 로고
    • Fibrillin: Monomers and microfibrils
    • Sakai L.Y., Keene D.R. Fibrillin: monomers and microfibrils. Methods Enzymol. 245:1994;29-52.
    • (1994) Methods Enzymol , vol.245 , pp. 29-52
    • Sakai, L.Y.1    Keene, D.R.2
  • 138
    • 0023002893 scopus 로고
    • Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils
    • Sakai L.Y., Keene D.R., Engvall E. Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils. J Cell Biol. 103:1986;2499-2509.
    • (1986) J Cell Biol , vol.103 , pp. 2499-2509
    • Sakai, L.Y.1    Keene, D.R.2    Engvall, E.3
  • 141
    • 0028267099 scopus 로고
    • Structure and expression of fibrillin-2, a novel microfibrillar compound preferentially located in elastic matrices
    • Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F. Structure and expression of fibrillin-2, a novel microfibrillar compound preferentially located in elastic matrices. J Cell Biol. 124:1994;855-863.
    • (1994) J Cell Biol , vol.124 , pp. 855-863
    • Zhang, H.1    Apfelroth, S.D.2    Hu, W.3    Davis, E.C.4    Sanguineti, C.5    Bonadio, J.6    Mecham, R.P.7    Ramirez, F.8
  • 142
    • 0031148156 scopus 로고    scopus 로고
    • Distribution of transforming growth factor-β1-binding proteins and low-affinity receptors during odontoblast differentiation in the mouse
    • Cam Y., Lesot H., Colosetti P., Ruch J.V. Distribution of transforming growth factor-β1-binding proteins and low-affinity receptors during odontoblast differentiation in the mouse. Arch Oral Biol. 42:1997;385-391.
    • (1997) Arch Oral Biol , vol.42 , pp. 385-391
    • Cam, Y.1    Lesot, H.2    Colosetti, P.3    Ruch, J.V.4
  • 143
    • 0032513005 scopus 로고    scopus 로고
    • Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains
    • Cardy C.M., Handford P.A. Metal ion dependency of microfibrils supports a rod-like conformation for fibrillin-1 calcium-binding epidermal growth factor-like domains. J Mol Biol. 276:1998;855-860.
    • (1998) J Mol Biol , vol.276 , pp. 855-860
    • Cardy, C.M.1    Handford, P.A.2
  • 144
    • 0023019066 scopus 로고
    • The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein
    • Gibson M., Hughes J., Fanning J., Cleary E. The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein. J Biol Chem. 261:1986;11,429-11,436.
    • (1986) J Biol Chem , vol.261 , pp. 11
    • Gibson, M.1    Hughes, J.2    Fanning, J.3    Cleary, E.4
  • 145
    • 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.W., 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;26,630-26,634.
    • (1994) J Biol Chem , vol.269 , pp. 26
    • Glanville, R.W.1    Qian, R.Q.2    McClure, D.W.3    Maslen, C.L.4
  • 146
    • 0028931325 scopus 로고
    • The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1
    • Handford P., Downing A.K., Rao Z., Hewett D.R., Sykes B.C., 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.1    Downing, A.K.2    Rao, Z.3    Hewett, D.R.4    Sykes, B.C.5    Kielty, C.M.6
  • 147
    • 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
  • 148
    • 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
  • 150
    • 0030781430 scopus 로고    scopus 로고
    • Solution structure of the transforming growth factor-β-binding protein-like module, a domain associated with matrix fibrils
    • Yuan X., Downing A.K., Knott V., Handford P.A. Solution structure of the transforming growth factor-β-binding protein-like module, a domain associated with matrix fibrils. EMBO J. 16:1997;6659-6666.
    • (1997) EMBO J , vol.16 , pp. 6659-6666
    • Yuan, X.1    Downing, A.K.2    Knott, V.3    Handford, P.A.4
  • 151
    • 0026086474 scopus 로고
    • Specific EGF repeats of Notch mediate interactions with Delta and Serrate: Implications for Notch as a multifunctional receptor
    • Rebay I., Fleming R., Fehon R., Cherbas L., Cherbas P., Artavanis-Tsakonas S. Specific EGF repeats of Notch mediate interactions with Delta and Serrate: implications for Notch as a multifunctional receptor. Cell. 67:1991;687-699.
    • (1991) Cell , vol.67 , pp. 687-699
    • Rebay, I.1    Fleming, R.2    Fehon, R.3    Cherbas, L.4    Cherbas, P.5    Artavanis-Tsakonas, S.6
  • 152
    • 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., Gohring W., Wiedemann H., Chu M.L., Timpl R., Kostka G. 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. 272:1997;226-236.
    • (1997) J Mol Biol , vol.272 , pp. 226-236
    • Adam, S.1    Gohring, W.2    Wiedemann, H.3    Chu, M.L.4    Timpl, R.5    Kostka, G.6
  • 155
    • 0029860747 scopus 로고    scopus 로고
    • Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1
    • Gleizes P.E., Beavis R.C., Mazzieri R., Shen B., Rifkin D.B. Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-β binding protein-1 that mediates bonding to the latent transforming growth factor-β1. J Biol Chem. 271:1996;29,891-29,896.
    • (1996) J Biol Chem , vol.271 , pp. 29
    • Gleizes, P.E.1    Beavis, R.C.2    Mazzieri, R.3    Shen, B.4    Rifkin, D.B.5
  • 156
    • 0032493659 scopus 로고    scopus 로고
    • Recombinant latent transforming growth factor-β-binding protein 2 assembles to fibroblast extracellular matrix and is susceptible to proteolytic processing and release
    • Hyytiäinen M., Taipale J., Heldin C.H., Keski-Oja J. Recombinant latent transforming growth factor-β-binding protein 2 assembles to fibroblast extracellular matrix and is susceptible to proteolytic processing and release. J Biol Chem. 273:1998;20,669-20,676.
    • (1998) J Biol Chem , vol.273 , pp. 20
    • Hyytiäinen, M.1    Taipale, J.2    Heldin, C.H.3    Keski-Oja, J.4
  • 157
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol. 12:1996;697-715.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 158
    • 0026457025 scopus 로고
    • Attachment of human vascular smooth muscles cells to intact microfibrillar assemblies of collagen VI and fibrillin
    • Kielty C.M., Whittaker S.P., Grant M.E., Shuttleworth C.A. Attachment of human vascular smooth muscles cells to intact microfibrillar assemblies of collagen VI and fibrillin. J Cell Sci. 103:1992;445-451.
    • (1992) J Cell Sci , vol.103 , pp. 445-451
    • Kielty, C.M.1    Whittaker, S.P.2    Grant, M.E.3    Shuttleworth, C.A.4
  • 159
    • 0029915120 scopus 로고    scopus 로고
    • Cell-type specific recognition of RGD- And non-RGD-containing cell binding domains in fibrillin-1
    • Sakamoto H., Broekelmann T., Cheresh D.A., Ramirez F., Rosenbloom J., Mecham R.P. Cell-type specific recognition of RGD- and non-RGD-containing cell binding domains in fibrillin-1. J Biol Chem. 271:1996;4916-4922.
    • (1996) J Biol Chem , vol.271 , pp. 4916-4922
    • Sakamoto, H.1    Broekelmann, T.2    Cheresh, D.A.3    Ramirez, F.4    Rosenbloom, J.5    Mecham, R.P.6
  • 160
    • 0029867570 scopus 로고    scopus 로고
    • Cell adhesion and integrin binding to recombinant human fibrillin-1
    • Pfaff M., Reinhardt D.P., Sakai L.Y., Timpl R. Cell adhesion and integrin binding to recombinant human fibrillin-1. FEBS Lett. 384:1996;247-250.
    • (1996) FEBS Lett , vol.384 , pp. 247-250
    • Pfaff, M.1    Reinhardt, D.P.2    Sakai, L.Y.3    Timpl, R.4
  • 162
    • 0031593673 scopus 로고    scopus 로고
    • TGF-β1-binding protein-like modules of fibrillin-1 and -2 mediate integrin-dependent cell adhesion
    • D'Arrigo C., Burl S., Withers A.P., Dobson H., Black C., Boxer M. TGF-β1-binding protein-like modules of fibrillin-1 and -2 mediate integrin-dependent cell adhesion. Connect Tissue Res. 37:1998;29-51.
    • (1998) Connect Tissue Res , vol.37 , pp. 29-51
    • D'Arrigo, C.1    Burl, S.2    Withers, A.P.3    Dobson, H.4    Black, C.5    Boxer, M.6
  • 163
    • 0031875947 scopus 로고    scopus 로고
    • Microfibril-associated glycoprotein-2 (MAGP-2) is specifically associated with fibrillin-containing microfibrils but exhibits more restricted patterns of tissue localization and developmental expression than its structural relative MAGP-1
    • Gibson M.A., Finnis M.L., Kumaratilake J.S., Cleary E.G. Microfibril-associated glycoprotein-2 (MAGP-2) is specifically associated with fibrillin-containing microfibrils but exhibits more restricted patterns of tissue localization and developmental expression than its structural relative MAGP-1. J Histochem Cytochem. 46:1998;871-886.
    • (1998) J Histochem Cytochem , vol.46 , pp. 871-886
    • Gibson, M.A.1    Finnis, M.L.2    Kumaratilake, J.S.3    Cleary, E.G.4
  • 165
    • 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.Y. 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.Y.5
  • 166
    • 0031789366 scopus 로고    scopus 로고
    • Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations
    • [in process citation]
    • Lonnqvist L., Reinhardt D., Sakai L., Peltonen L. Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations. Hum Mol Genet. 7:1998;2039-2044. [in process citation].
    • (1998) Hum Mol Genet , vol.7 , pp. 2039-2044
    • Lonnqvist, L.1    Reinhardt, D.2    Sakai, L.3    Peltonen, L.4
  • 167
    • 0031596123 scopus 로고    scopus 로고
    • Analysis of the expression pattern of the latent transforming growth factor-β binding protein isoforms in normal and diseased human liver reveals a new splice variant missing the proteinase-sensitive hinge region
    • Michel K., Roth S., Trautwein C., Gong W., Flemming P., Gressner A.M. Analysis of the expression pattern of the latent transforming growth factor-β binding protein isoforms in normal and diseased human liver reveals a new splice variant missing the proteinase-sensitive hinge region. Hepatology. 27:1998;1592-1599.
    • (1998) Hepatology , vol.27 , pp. 1592-1599
    • Michel, K.1    Roth, S.2    Trautwein, C.3    Gong, W.4    Flemming, P.5    Gressner, A.M.6
  • 168
    • 0032571437 scopus 로고    scopus 로고
    • Loss of a consensus heparin binding site by alternative splicing of latent transforming growth factor-β binding protein-1
    • Öklu R., Metcalfe J., Hesketh T., Kemp P. Loss of a consensus heparin binding site by alternative splicing of latent transforming growth factor-β binding protein-1. FEBS Lett. 425:1998;281-285.
    • (1998) FEBS Lett , vol.425 , pp. 281-285
    • Öklu, R.1    Metcalfe, J.2    Hesketh, T.3    Kemp, P.4
  • 170
    • 0026029066 scopus 로고
    • Extraction of extendable beaded structures and their identification as fibrillin-containing extracellular matrix microfibrils
    • Keene D., Maddox B.K., Kuo H.J., Sakai L.Y., Glanville R.W. Extraction of extendable beaded structures and their identification as fibrillin-containing extracellular matrix microfibrils. J Histochem Cytochem. 39:1991;441-449.
    • (1991) J Histochem Cytochem , vol.39 , pp. 441-449
    • Keene, D.1    Maddox, B.K.2    Kuo, H.J.3    Sakai, L.Y.4    Glanville, R.W.5
  • 171
    • 0345655218 scopus 로고    scopus 로고
    • Latent TGF-β complexes in the extracellular matrix with 8-Cys containing proteins: Characterization of the 3rd 8-Cys repeat of LTBP-1
    • Saharinen J., Hyytiäinen M., Taipale J., Keski-Oja J. Latent TGF-β complexes in the extracellular matrix with 8-Cys containing proteins: characterization of the 3rd 8-Cys repeat of LTBP-1. Mol Biol Cell. 7:(suppl. 414a):1996;2406.
    • (1996) Mol Biol Cell , vol.7 , Issue.SUPPL. 414A , pp. 2406
    • Saharinen, J.1    Hyytiäinen, M.2    Taipale, J.3    Keski-Oja, J.4
  • 173
    • 0029023792 scopus 로고
    • Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrils
    • Zhang H., Hu W., Ramirez F. Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrils. J Cell Biol. 129:1995;1165-1176.
    • (1995) J Cell Biol , vol.129 , pp. 1165-1176
    • Zhang, H.1    Hu, W.2    Ramirez, F.3
  • 175
    • 0029063160 scopus 로고
    • An extracellular matrix protein of jellyfish homologous to mammalian fibrillins forms different fibrils depending on the life stage of the animal
    • Reber-Muller S., Spissinger T., Schuchert P., Spring J., Schmid V. An extracellular matrix protein of jellyfish homologous to mammalian fibrillins forms different fibrils depending on the life stage of the animal. Dev Biol. 169:1995;662-672.
    • (1995) Dev Biol , vol.169 , pp. 662-672
    • Reber-Muller, S.1    Spissinger, T.2    Schuchert, P.3    Spring, J.4    Schmid, V.5
  • 176
    • 0030852451 scopus 로고    scopus 로고
    • Marfan syndrome - Current medical and genetic knowledge: How to treat and when
    • discussion 135-136
    • Child A.H. Marfan syndrome - current medical and genetic knowledge: how to treat and when. J Card Surg. 12:1997;131-135. discussion 135-136.
    • (1997) J Card Surg , vol.12 , pp. 131-135
    • Child, A.H.1
  • 177
    • 0029665565 scopus 로고    scopus 로고
    • Fibrillin mutation in Marfan syndrome and related phenotypes
    • Ramirez F. Fibrillin mutation in Marfan syndrome and related phenotypes. Curr Opin Genet Dev. 6:1996;309-315.
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 309-315
    • Ramirez, F.1
  • 178
    • 0017250167 scopus 로고
    • Tight-skin, a new mutation of the mouse causing excessive growth of connective tissue and skeleton
    • Green M., Sweet H., Bunker L. Tight-skin, a new mutation of the mouse causing excessive growth of connective tissue and skeleton. Am J Pathol. 82:1976;493-512.
    • (1976) Am J Pathol , vol.82 , pp. 493-512
    • Green, M.1    Sweet, H.2    Bunker, L.3
  • 181
    • 0028335388 scopus 로고
    • Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome
    • Kainulainen K., Karttunen L., Puhakka L., Sakai L., Peltonen L. Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome. Nat Genet. 6:1994;64-69.
    • (1994) Nat Genet , vol.6 , pp. 64-69
    • Kainulainen, K.1    Karttunen, L.2    Puhakka, L.3    Sakai, L.4    Peltonen, L.5
  • 182
    • 0030020322 scopus 로고    scopus 로고
    • Mutation in fibrillin-1 and the Marfanoid craniosynostosis (Shprintzen-Goldberg) syndrome
    • Sood S., Eldadah Z.A., Krause W.L., McIntosh I., Dietz H.C. Mutation in fibrillin-1 and the Marfanoid craniosynostosis (Shprintzen-Goldberg) syndrome. Nat Genet. 12:1996;209-211.
    • (1996) Nat Genet , vol.12 , pp. 209-211
    • Sood, S.1    Eldadah, Z.A.2    Krause, W.L.3    McIntosh, I.4    Dietz, H.C.5
  • 184
    • 0028902039 scopus 로고
    • A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome
    • Milewicz D.M., Grossfield J., Cao S.N., Kielty C., Covitz W., Jewett T.A. A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome. J Clin Invest. 95:1995;2373-2378.
    • (1995) J Clin Invest , vol.95 , pp. 2373-2378
    • Milewicz, D.M.1    Grossfield, J.2    Cao, S.N.3    Kielty, C.4    Covitz, W.5    Jewett, T.A.6
  • 185
    • 0031687121 scopus 로고    scopus 로고
    • Association of microsatellite markers near the fibrillin 1 gene on human chromosome 15q with scleroderma in a native American population
    • Tan F.K., Stivers D.N., Foster M.W., Chakraborty R., Howard R.F., Milewicz D.M., Arnett F.C. Association of microsatellite markers near the fibrillin 1 gene on human chromosome 15q with scleroderma in a native American population. Arthritis Rheum. 41:1998;1729-1737.
    • (1998) Arthritis Rheum , vol.41 , pp. 1729-1737
    • Tan, F.K.1    Stivers, D.N.2    Foster, M.W.3    Chakraborty, R.4    Howard, R.F.5    Milewicz, D.M.6    Arnett, F.C.7
  • 186
    • 0345223400 scopus 로고    scopus 로고
    • Latent TGF-β binding protein-2 is required for normal mouse development
    • Shipley J.M., et al. Latent TGF-β binding protein-2 is required for normal mouse development. Am Resp Crit Care Med. 157:1998;A246.
    • (1998) Am Resp Crit Care Med , vol.157 , pp. 246
    • Shipley, J.M.1
  • 187
    • 0006835637 scopus 로고    scopus 로고
    • Marfan like phenotypes caused by mutations in LTBP-2
    • Mathews K.R., Godfrey M. Marfan like phenotypes caused by mutations in LTBP-2. Am J Hum Genet. 61:(suppl):1997;A44.
    • (1997) Am J Hum Genet , vol.61 , Issue.SUPPL , pp. 44
    • Mathews, K.R.1    Godfrey, M.2
  • 188
    • 0031021557 scopus 로고    scopus 로고
    • Analysis of loss of heterozygosity on chromosome 11q13 in atypical ductal hyperplasia and in situ carcinoma of the breast
    • Chuaqui R., Zhuang Z., Emmert-Buck M., Liotta L., Merino M. Analysis of loss of heterozygosity on chromosome 11q13 in atypical ductal hyperplasia and in situ carcinoma of the breast. Am J Pathol. 150:1997;297-303.
    • (1997) Am J Pathol , vol.150 , pp. 297-303
    • Chuaqui, R.1    Zhuang, Z.2    Emmert-Buck, M.3    Liotta, L.4    Merino, M.5
  • 190
    • 0027393417 scopus 로고
    • Involvement of transforming growth factor-β In the formation of fibrotic lesions in carcinoid heart disease
    • Waltenberger J., Lundin L., Oberg K., Wilander E., Miyazono K., Heldin C.H., Funa K. Involvement of transforming growth factor-β in the formation of fibrotic lesions in carcinoid heart disease. Am J Pathol. 142:1993;71-78.
    • (1993) Am J Pathol , vol.142 , pp. 71-78
    • Waltenberger, J.1    Lundin, L.2    Oberg, K.3    Wilander, E.4    Miyazono, K.5    Heldin, C.H.6    Funa, K.7
  • 192
    • 0030786999 scopus 로고    scopus 로고
    • Transforming growth factor-β1 and its latent form binding protein-1 associate with elastic fibres in human dermis: Accumulation in actinic damage and absence in anetoderma
    • Karonen T., Jeskanen L., Keski-Oja J. Transforming growth factor-β1 and its latent form binding protein-1 associate with elastic fibres in human dermis: accumulation in actinic damage and absence in anetoderma. Br J Dermatol. 137:1997;51-58.
    • (1997) Br J Dermatol , vol.137 , pp. 51-58
    • Karonen, T.1    Jeskanen, L.2    Keski-Oja, J.3
  • 193
    • 0031691462 scopus 로고    scopus 로고
    • The cutaneous microfibrillar apparatus contains latent transforming growth factor-β binding protein-1 (LTBP-1) and is a repository for latent TGF-β1
    • Raghunath M., Unsold C., Kubitscheck U., Bruckner-Tuderman L., Peters R., Meuli M. The cutaneous microfibrillar apparatus contains latent transforming growth factor-β binding protein-1 (LTBP-1) and is a repository for latent TGF-β1. J Invest Dermatol. 111:1998;559-565.
    • (1998) J Invest Dermatol , vol.111 , pp. 559-565
    • Raghunath, M.1    Unsold, C.2    Kubitscheck, U.3    Bruckner-Tuderman, L.4    Peters, R.5    Meuli, M.6
  • 194
    • 0027237465 scopus 로고
    • Lack of the latent transforming growth factor-β binding protein in malignant, but not benign prostatic tissue
    • Eklov S., Funa K., Nordgren H., Olofsson A., Kanzaki T., Miyazono K., Nilsson S. Lack of the latent transforming growth factor-β binding protein in malignant, but not benign prostatic tissue. Cancer Res. 53:1993;3193-3197.
    • (1993) Cancer Res , vol.53 , pp. 3193-3197
    • Eklov, S.1    Funa, K.2    Nordgren, H.3    Olofsson, A.4    Kanzaki, T.5    Miyazono, K.6    Nilsson, S.7
  • 195
    • 0026937923 scopus 로고
    • Immunohistochemical identification of transforming growth factor-β And its binding protein in human gastrointestinal carcinoma
    • Mizoi T., Ohtani H., Matsuno S., Nagura H. Immunohistochemical identification of transforming growth factor-β and its binding protein in human gastrointestinal carcinoma. Tohoku J Exp Med. 168:1992;271-273.
    • (1992) Tohoku J Exp Med , vol.168 , pp. 271-273
    • Mizoi, T.1    Ohtani, H.2    Matsuno, S.3    Nagura, H.4
  • 196
    • 0027404055 scopus 로고
    • Immunoelectron microscopic localization of transforming growth factor-β1 and latent transforming growth factor-β1 binding protein in human gastrointestinal carcinomas: Qualitative difference between cancer cells and stromal cells
    • Mizoi T., Ohtani H., Miyazono K., Miyazawa M., Matsuno S., Nagura H. Immunoelectron microscopic localization of transforming growth factor-β1 and latent transforming growth factor-β1 binding protein in human gastrointestinal carcinomas: qualitative difference between cancer cells and stromal cells. Cancer Res. 53:1993;183-190.
    • (1993) Cancer Res , vol.53 , pp. 183-190
    • Mizoi, T.1    Ohtani, H.2    Miyazono, K.3    Miyazawa, M.4    Matsuno, S.5    Nagura, H.6
  • 197
    • 0027293946 scopus 로고
    • Radiation-induced transforming growth factor-β And subsequent extracellular matrix reorganization in murine mammary gland
    • Barcellos-Hoff M. Radiation-induced transforming growth factor-β and subsequent extracellular matrix reorganization in murine mammary gland. Cancer Res. 53:1993;3880-3886.
    • (1993) Cancer Res , vol.53 , pp. 3880-3886
    • Barcellos-Hoff, M.1
  • 198
    • 0027976427 scopus 로고
    • Assignment of the gene encoding the latent TGF-β1-binding protein (LTBP1) to human chromosome 2, region p12→q22
    • Stenman G., Sahlin P., Olofsson A., Geurtz van Kessel A., Miyazono K. Assignment of the gene encoding the latent TGF-β1-binding protein (LTBP1) to human chromosome 2, region p12→q22. Cytogenet Cell Genet. 66:1994;117-119.
    • (1994) Cytogenet Cell Genet , vol.66 , pp. 117-119
    • Stenman, G.1    Sahlin, P.2    Olofsson, A.3    Geurtz Van Kessel, A.4    Miyazono, K.5
  • 199
    • 0029134243 scopus 로고
    • Mapping of human and murine genes for latent TGF-β binding protein-2 (LTBP2)
    • Li X., Yin W., Perez-Jurado L., Bonadio J., Francke U. Mapping of human and murine genes for latent TGF-β binding protein-2 (LTBP2). Mamm Genome. 6:1995;42-45.
    • (1995) Mamm Genome , vol.6 , pp. 42-45
    • Li, X.1    Yin, W.2    Perez-Jurado, L.3    Bonadio, J.4    Francke, U.5
  • 200
    • 0031892802 scopus 로고    scopus 로고
    • Isoforms and splice variant of transforming growth factor β-binding protein in rat hepatic stellate cells
    • Gong W., Roth S., Michel K., Gressner A.M. Isoforms and splice variant of transforming growth factor β-binding protein in rat hepatic stellate cells. Gastroenterology. 114:1998;352-363.
    • (1998) Gastroenterology , vol.114 , pp. 352-363
    • Gong, W.1    Roth, S.2    Michel, K.3    Gressner, A.M.4
  • 201
    • 0032544382 scopus 로고    scopus 로고
    • Expression of alternatively spliced human latent transforming growth factor-β binding protein-1
    • Oklu R., Hesketh T., Metcalfe J., Kemp P. Expression of alternatively spliced human latent transforming growth factor-β binding protein-1. FEBS Lett. 435:1998;143-148.
    • (1998) FEBS Lett , vol.435 , pp. 143-148
    • Oklu, R.1    Hesketh, T.2    Metcalfe, J.3    Kemp, P.4
  • 203
    • 0027672469 scopus 로고
    • Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome
    • [published erratum appears in Hum Mol Genet 1993:1762]
    • Pereira L.M.D.A., Ramirez F., Lynch J.R., Sykes B., Pangilinan T., Bonadio J. Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome. Hum Mol Genet. 2:1993;961-968. [published erratum appears in Hum Mol Genet 1993:1762].
    • (1993) Hum Mol Genet , vol.2 , pp. 961-968
    • Pereira, L.M.D.A.1    Ramirez, F.2    Lynch, J.R.3    Sykes, B.4    Pangilinan, T.5    Bonadio, J.6
  • 206
    • 0345223395 scopus 로고    scopus 로고
    • Localization of the latent TGF-β binding protein-1 (LTBP-1) to fibrillin-containing microfibrils in bone cells in vitro and in vivo
    • (in press)
    • Dallas S, Keene D, Bruder S, Saharinen J, Sakai L, Mundy G, Bonewald L. Localization of the latent TGF-β binding protein-1 (LTBP-1) to fibrillin-containing microfibrils in bone cells in vitro and in vivo. J Bone Miner Res 1999 (in press).
    • (1999) J Bone Miner Res
    • Dallas, S.1    Keene, D.2    Bruder, S.3    Saharinen, J.4    Sakai, L.5    Mundy, G.6    Bonewald, L.7


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