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Volumn 8, Issue 2, 1997, Pages 143-156

TSG-6: An IL-1/TNF-inducible protein with anti-inflammatory activity

Author keywords

CUB domain; Extracellular matrix degradation; Hyaladherins; Inflammation; Inter inhibitor; TSG 6

Indexed keywords

ANTIINFLAMMATORY AGENT; CELL ADHESION MOLECULE; CYTOKINE; HYALURONIC ACID; INTERLEUKIN 1; PROTEIN; TSG-6 PROTEIN; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 0343742633     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6101(97)00008-7     Document Type: Short Survey
Times cited : (172)

References (135)
  • 1
  • 3
    • 0025360897 scopus 로고
    • Isolation and characterization of eight tumor necrosis factor-induced gene sequences from human fibroblasts
    • Lee TH, Lee GW, Ziff EB, Vilček J. Isolation and characterization of eight tumor necrosis factor-induced gene sequences from human fibroblasts. Mol Cell Biol 1990, 10, 1982-1988.
    • (1990) Mol Cell Biol , vol.10 , pp. 1982-1988
    • Lee, T.H.1    Lee, G.W.2    Ziff, E.B.3    Vilček, J.4
  • 4
    • 0027205162 scopus 로고
    • Identification of a novel serum and growth factor-inducible gene in vascular smooth muscle cells
    • erratum in J Biol Chem 1993, 268, 21453
    • Feng P, Liau G. Identification of a novel serum and growth factor-inducible gene in vascular smooth muscle cells [erratum in J Biol Chem 1993, 268, 21453]. J Biol Chem 1993, 268, 9387-9392.
    • (1993) J Biol Chem , vol.268 , pp. 9387-9392
    • Feng, P.1    Liau, G.2
  • 5
    • 0026597436 scopus 로고
    • A novel secretory tumor necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44
    • Lee TH, Wisniewski H-G, Vilček J. A novel secretory tumor necrosis factor-inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44. J Cell Biol 1992, 116, 545-557.
    • (1992) J Cell Biol , vol.116 , pp. 545-557
    • Lee, T.H.1    Wisniewski, H.-G.2    Vilček, J.3
  • 6
    • 0027486712 scopus 로고
    • TSG-6: A TNF-, IL-1-, and LPS-inducible secreted glycoprotein associated with arthritis
    • Wisniewski H-G, Maier R, Lotz M, Lee S, Klampfer L, Lee TH, Vilček J. TSG-6: a TNF-, IL-1-, and LPS-inducible secreted glycoprotein associated with arthritis. J Immunol 1993, 151, 6593-6601.
    • (1993) J Immunol , vol.151 , pp. 6593-6601
    • Wisniewski, H.-G.1    Maier, R.2    Lotz, M.3    Lee, S.4    Klampfer, L.5    Lee, T.H.6    Vilček, J.7
  • 7
    • 0025283586 scopus 로고
    • Transforming growth factor-beta and cellular immune responses in synovial fluids
    • Lotz M, Kekow J, Carson DA. Transforming growth factor-beta and cellular immune responses in synovial fluids. J Immunol 1990, 144, 4189-4194.
    • (1990) J Immunol , vol.144 , pp. 4189-4194
    • Lotz, M.1    Kekow, J.2    Carson, D.A.3
  • 8
    • 0025166982 scopus 로고
    • Low levels of interleukin-4 and high levels of transforming growth factor beta in rheumatoid synovitis
    • Miossec P, Naviliat M, Dupuy d'Angeac A, Sany J, Banchereau J. Low levels of interleukin-4 and high levels of transforming growth factor beta in rheumatoid synovitis. Arth Rheum 1990, 33, 1180-1187.
    • (1990) Arth Rheum , vol.33 , pp. 1180-1187
    • Miossec, P.1    Naviliat, M.2    Dupuy D'Angeac, A.3    Sany, J.4    Banchereau, J.5
  • 9
    • 0026656850 scopus 로고
    • Involvement of endogenous tumor necrosis factor alpha and transforming growth factor beta during induction of collagen type II arthritis in mice
    • Thorbecke GJ, Shah R, Leu CH, Kuruvilla AP, Hardison AM, Palladino MA. Involvement of endogenous tumor necrosis factor alpha and transforming growth factor beta during induction of collagen type II arthritis in mice. Proc Natl Acad Sci USA 1992, 89, 7375-7379.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7375-7379
    • Thorbecke, G.J.1    Shah, R.2    Leu, C.H.3    Kuruvilla, A.P.4    Hardison, A.M.5    Palladino, M.A.6
  • 10
    • 0029936595 scopus 로고    scopus 로고
    • TSG-6 expression in human articular chondrocytes: Possible implications in joint inflammation and cartilage degradation
    • Maier R, Wisniewski H-G, Vilček J, Lotz M. TSG-6 expression in human articular chondrocytes: possible implications in joint inflammation and cartilage degradation. Arth Rheum 1996, 39, 552-559.
    • (1996) Arth Rheum , vol.39 , pp. 552-559
    • Maier, R.1    Wisniewski, H.-G.2    Vilček, J.3    Lotz, M.4
  • 12
    • 0030572693 scopus 로고    scopus 로고
    • Solution structure of the link module: A hyaluronan-binding domain involved in extracellular matrix stability and cell migration
    • Kohda D, Morton CJ, Parkar AA, Hatanaka H, Inagaki FM, Campbell ID, Day AJ. Solution structure of the link module: A hyaluronan-binding domain involved in extracellular matrix stability and cell migration. Cell 1996, 86, 767-775.
    • (1996) Cell , vol.86 , pp. 767-775
    • Kohda, D.1    Morton, C.J.2    Parkar, A.A.3    Hatanaka, H.4    Inagaki, F.M.5    Campbell, I.D.6    Day, A.J.7
  • 13
    • 0025038449 scopus 로고
    • Hyaluronan and its binding proteins, the hyaladherins
    • Toole BP. Hyaluronan and its binding proteins, the hyaladherins. Curr Opin Cell Biol 1990, 2, 839-844.
    • (1990) Curr Opin Cell Biol , vol.2 , pp. 839-844
    • Toole, B.P.1
  • 14
    • 0002915419 scopus 로고
    • Proteoglycans and hyaluronan in morphogenesis and differentiation
    • ed. E. D. Hay. Plenum Press, New York
    • Toole BP, Proteoglycans and hyaluronan in morphogenesis and differentiation. In Cell Biology and Extracellular Matrix, ed. E. D. Hay. Plenum Press, New York, 1992, pp. 305-341.
    • (1992) Cell Biology and Extracellular Matrix , pp. 305-341
    • Toole, B.P.1
  • 15
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo RV, Murdoch AD. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J 1996, 10, 598-614.
    • (1996) FASEB J , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 16
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork P, Beckmann G. The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol 1993, 231, 539-545.
    • (1993) J Mol Biol , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 17
    • 0024746112 scopus 로고
    • Structural analysis of the uEGF gene in the sea urchin strongylocentrotus purpuratus reveals more similarity to vertebrate than to invertebrate genes with EGF-like repeats
    • Delgadillo-Reynoso MG, Rollo DR, Hursh DA, Raff RA. Structural analysis of the uEGF gene in the sea urchin strongylocentrotus purpuratus reveals more similarity to vertebrate than to invertebrate genes with EGF-like repeats. J Mol Evol 1989, 29, 314-327.
    • (1989) J Mol Evol , vol.29 , pp. 314-327
    • Delgadillo-Reynoso, M.G.1    Rollo, D.R.2    Hursh, D.A.3    Raff, R.A.4
  • 20
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J Mol Biol 1994, 242, 309-320.
    • (1994) J Mol Biol , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 21
    • 0029943733 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains
    • Romero A, Varela PF, Sanz L, Topfer-Petersen E, Calvete JJ. Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains. FEBS Lett 1996, 382, 15-17.
    • (1996) FEBS Lett , vol.382 , pp. 15-17
    • Romero, A.1    Varela, P.F.2    Sanz, L.3    Topfer-Petersen, E.4    Calvete, J.J.5
  • 22
    • 0027263129 scopus 로고
    • Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: A dual role for spermadhesins in fertilization
    • Sanz L, Calvete JJ, Mann K, Gabius HJ, Topfer-Petersen E. Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: a dual role for spermadhesins in fertilization. Mol Reprod Dev 1993, 35, 37-43.
    • (1993) Mol Reprod Dev , vol.35 , pp. 37-43
    • Sanz, L.1    Calvete, J.J.2    Mann, K.3    Gabius, H.J.4    Topfer-Petersen, E.5
  • 23
    • 0027382435 scopus 로고
    • Characterization of AWN-1 glycosylated isoforms helps define the zona pellucida and serine proteinase inhibitor-binding region on boar spermadhesins
    • Calvete JJ, Sanz L, Dostalova Z, Topfer-Petersen E. Characterization of AWN-1 glycosylated isoforms helps define the zona pellucida and serine proteinase inhibitor-binding region on boar spermadhesins. FEBS Lett 1993, 334, 37-40.
    • (1993) FEBS Lett , vol.334 , pp. 37-40
    • Calvete, J.J.1    Sanz, L.2    Dostalova, Z.3    Topfer-Petersen, E.4
  • 24
    • 0026580870 scopus 로고
    • Isolation and biochemical characterization of two isoforms of a boar sperm zona pellucida-binding protein
    • Sanz L, Calvete JJ, Schafer W, Mann K, Topfer-Petersen E. Isolation and biochemical characterization of two isoforms of a boar sperm zona pellucida-binding protein. Biochim Biophys Acta 1992, 1119, 127-132.
    • (1992) Biochim Biophys Acta , vol.1119 , pp. 127-132
    • Sanz, L.1    Calvete, J.J.2    Schafer, W.3    Mann, K.4    Topfer-Petersen, E.5
  • 25
    • 0029058523 scopus 로고
    • Boar spermadhesin AWN-1. Oligosaccharide and zona pellucida binding characteristics
    • Dostalova Z, Calvete JJ, Sanz L, Topfer-Petersen E. Boar spermadhesin AWN-1. Oligosaccharide and zona pellucida binding characteristics. Eur J Biochem 1995, 230, 329-336.
    • (1995) Eur J Biochem , vol.230 , pp. 329-336
    • Dostalova, Z.1    Calvete, J.J.2    Sanz, L.3    Topfer-Petersen, E.4
  • 26
    • 0026604921 scopus 로고
    • Boar spermadhesins AQN-1 and AWN are sperm-associated acrosin inhibitor acceptor proteins
    • Sanz L, Calvete JJ, Jonakova V, Topfer-Petersen E. Boar spermadhesins AQN-1 and AWN are sperm-associated acrosin inhibitor acceptor proteins. FEBS Lett 1992, 300, 63-66.
    • (1992) FEBS Lett , vol.300 , pp. 63-66
    • Sanz, L.1    Calvete, J.J.2    Jonakova, V.3    Topfer-Petersen, E.4
  • 28
    • 0027416471 scopus 로고
    • Transcriptional regulation of TSG6, a tumor necrosis factor- and interleukin-1-inducible primary response gene coding for a secreted hyaluronan-binding protein
    • Lee TH, Klampfer L, Shows TB, Vilček J. Transcriptional regulation of TSG6, a tumor necrosis factor- and interleukin-1-inducible primary response gene coding for a secreted hyaluronan-binding protein. J Biol Chem 1993, 268, 6154-6160.
    • (1993) J Biol Chem , vol.268 , pp. 6154-6160
    • Lee, T.H.1    Klampfer, L.2    Shows, T.B.3    Vilček, J.4
  • 29
    • 0028088168 scopus 로고
    • NF-IL6 and AP-1 cooperatively modulate the activation of the TSG-6 gene by tumor necrosis factor alpha and interleukin-1
    • Klampfer L, Lee TH, Hsu W, Vilček J, Chen-Kiang S. NF-IL6 and AP-1 cooperatively modulate the activation of the TSG-6 gene by tumor necrosis factor alpha and interleukin-1. Mol Cell Biol 1994, 14, 6561-6569.
    • (1994) Mol Cell Biol , vol.14 , pp. 6561-6569
    • Klampfer, L.1    Lee, T.H.2    Hsu, W.3    Vilček, J.4    Chen-Kiang, S.5
  • 30
    • 0028931847 scopus 로고
    • Activation of the TSG-6 gene by NF-IL6 requires two adjacent NF-IL6 binding sites
    • Klampfer L, Chen-Kiang S, Vilček J. Activation of the TSG-6 gene by NF-IL6 requires two adjacent NF-IL6 binding sites. J Biol Chem 1995, 270, 3677-3682.
    • (1995) J Biol Chem , vol.270 , pp. 3677-3682
    • Klampfer, L.1    Chen-Kiang, S.2    Vilček, J.3
  • 31
    • 0025014781 scopus 로고
    • IL-6 production by human articular chondrocytes. Modulation of its synthesis by cytokines, growth factors, and hormones in vitro
    • Guerne PA, Carson DA, Lotz M. IL-6 production by human articular chondrocytes. Modulation of its synthesis by cytokines, growth factors, and hormones in vitro. J Immunol 1990, 144, 499-505.
    • (1990) J Immunol , vol.144 , pp. 499-505
    • Guerne, P.A.1    Carson, D.A.2    Lotz, M.3
  • 32
    • 0026802287 scopus 로고
    • Detection of cytokines at the cartilage/pannus junction in patients with rheumatoid arthritis: Implications for the role of cytokines in cartilage destruction and repair
    • Chu CQ, Field M, Allard S, Abney E, Feldmann M, Maini RN. Detection of cytokines at the cartilage/pannus junction in patients with rheumatoid arthritis: implications for the role of cytokines in cartilage destruction and repair. Brit J Rheumatol 1992, 31, 653-661.
    • (1992) Brit J Rheumatol , vol.31 , pp. 653-661
    • Chu, C.Q.1    Field, M.2    Allard, S.3    Abney, E.4    Feldmann, M.5    Maini, R.N.6
  • 33
    • 0022479614 scopus 로고
    • Link protein cDNA sequence reveals a tandemly repeated protein structure
    • Doege K, Hassell JR, Caterson B, Yamada Y. Link protein cDNA sequence reveals a tandemly repeated protein structure. Proc Natl Acad Sci USA 1986, 83, 3761-3765.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3761-3765
    • Doege, K.1    Hassell, J.R.2    Caterson, B.3    Yamada, Y.4
  • 34
    • 0023609134 scopus 로고
    • The tandemly repeated sequences of cartilage link protein contain the sites for interaction with hyaluronic acid
    • Goetinck PF, Stirpe NS, Tsonis PA, Carlone D. The tandemly repeated sequences of cartilage link protein contain the sites for interaction with hyaluronic acid. J Cell Biol 1987, 105, 2403-2408.
    • (1987) J Cell Biol , vol.105 , pp. 2403-2408
    • Goetinck, P.F.1    Stirpe, N.S.2    Tsonis, P.A.3    Carlone, D.4
  • 36
    • 0028338551 scopus 로고
    • Link protein is ubiquitously expressed in noncartilaginous tissues where it enhances and stabilizes the interaction of proteoglycans with hyaluronic acid
    • Binette F, Cravens J, Kahoussi B, Haudenschild DR, Goetinck PF. Link protein is ubiquitously expressed in noncartilaginous tissues where it enhances and stabilizes the interaction of proteoglycans with hyaluronic acid. J Biol Chem 1994, 269, 19116-19122.
    • (1994) J Biol Chem , vol.269 , pp. 19116-19122
    • Binette, F.1    Cravens, J.2    Kahoussi, B.3    Haudenschild, D.R.4    Goetinck, P.F.5
  • 37
    • 0028239180 scopus 로고
    • The expression of functional link protein in a baculovirus system: Analysis of mutants lacking the A, B and B' domains
    • Grover J, Roughley PJ. The expression of functional link protein in a baculovirus system: analysis of mutants lacking the A, B and B' domains. Biochem J 1994, 300, 317-324.
    • (1994) Biochem J , vol.300 , pp. 317-324
    • Grover, J.1    Roughley, P.J.2
  • 38
    • 0029091616 scopus 로고
    • Expression and characterization of a single recombinant proteoglycan tandem repeat domain of link protein that binds zinc and hyaluronate
    • Varelas JB, Kollar J, Huynh TD, Hering TM. Expression and characterization of a single recombinant proteoglycan tandem repeat domain of link protein that binds zinc and hyaluronate. Arch Biochem & Biophys 1995, 321, 21-30.
    • (1995) Arch Biochem & Biophys , vol.321 , pp. 21-30
    • Varelas, J.B.1    Kollar, J.2    Huynh, T.D.3    Hering, T.M.4
  • 39
    • 0023802130 scopus 로고
    • Cartilage proteoglycans. Assembly with hyaluronate and link protein as studied by electron microscopy
    • Morgelin M, Paulsson M, Hardingham TE, Heinegard D, Engel J. Cartilage proteoglycans. Assembly with hyaluronate and link protein as studied by electron microscopy. Biochem J 1988, 253, 175-185.
    • (1988) Biochem J , vol.253 , pp. 175-185
    • Morgelin, M.1    Paulsson, M.2    Hardingham, T.E.3    Heinegard, D.4    Engel, J.5
  • 40
    • 0025013424 scopus 로고
    • An ELISA plate-based assay for hyaluronan using biotinylated proteoglycan G1 domain (HA-binding region)
    • Fosang AJ, Hey NJ, Carney SL, Hardingham TE. An ELISA plate-based assay for hyaluronan using biotinylated proteoglycan G1 domain (HA-binding region). Matrix 1990, 10, 306-313.
    • (1990) Matrix , vol.10 , pp. 306-313
    • Fosang, A.J.1    Hey, N.J.2    Carney, S.L.3    Hardingham, T.E.4
  • 41
    • 0027269982 scopus 로고
    • Identification of hyaluronic acid binding sites in the extracellular domain of CD44
    • Peach RJ, Hollenbaugh D, Stamenkovic I, Aruffo A. Identification of hyaluronic acid binding sites in the extracellular domain of CD44. J Cell Biol 1993, 122, 257-264.
    • (1993) J Cell Biol , vol.122 , pp. 257-264
    • Peach, R.J.1    Hollenbaugh, D.2    Stamenkovic, I.3    Aruffo, A.4
  • 42
    • 0028097742 scopus 로고
    • Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein
    • Yang B, Yang BL, Savani RC, Turley EA. Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. EMBO J 1994, 13, 286-296.
    • (1994) EMBO J , vol.13 , pp. 286-296
    • Yang, B.1    Yang, B.L.2    Savani, R.C.3    Turley, E.A.4
  • 43
    • 0002252673 scopus 로고
    • Secondary structures in hyaluronan solutions: Chemical and biological implications
    • eds D. Evered and J. Whelan. John Wiley and Sons, Chichester
    • Scott JE. Secondary structures in hyaluronan solutions: chemical and biological implications. In The Biology of Hyaluronan, eds D. Evered and J. Whelan. John Wiley and Sons, Chichester, 1989, pp. 6-15.
    • (1989) The Biology of Hyaluronan , pp. 6-15
    • Scott, J.E.1
  • 44
    • 0025966878 scopus 로고
    • Hyaluronan and a cell-associated hyaluronan binding protein regulate the locomotion of ras-transformed cells
    • Turley EA, Austen L, Vandeligt K, Clary C. Hyaluronan and a cell-associated hyaluronan binding protein regulate the locomotion of ras-transformed cells. J Cell Biol 1991, 112, 1041-1047.
    • (1991) J Cell Biol , vol.112 , pp. 1041-1047
    • Turley, E.A.1    Austen, L.2    Vandeligt, K.3    Clary, C.4
  • 45
    • 0026645557 scopus 로고
    • Molecular cloning of a novel hyaluronan receptor that mediates tumor cell motility
    • published erratum appears in J Cell Biol 1992, Aug, 118(3), 753
    • Hardwick C, Hoare K, Owens R, Hohn HP, Hook M, Moore D, Cripps V, Austen L, Nance DM, Turley EA. Molecular cloning of a novel hyaluronan receptor that mediates tumor cell motility [published erratum appears in J Cell Biol 1992, Aug, 118(3), 753]. J Cell Biol 1992, 117, 1343-1350.
    • (1992) J Cell Biol , vol.117 , pp. 1343-1350
    • Hardwick, C.1    Hoare, K.2    Owens, R.3    Hohn, H.P.4    Hook, M.5    Moore, D.6    Cripps, V.7    Austen, L.8    Nance, D.M.9    Turley, E.A.10
  • 47
    • 0027504082 scopus 로고
    • Hyaluronan-binding proteins in development, tissue homeostasis, and disease
    • Knudson CB, Knudson W. Hyaluronan-binding proteins in development, tissue homeostasis, and disease. FASEB J 1993, 7, 1233-1241.
    • (1993) FASEB J , vol.7 , pp. 1233-1241
    • Knudson, C.B.1    Knudson, W.2
  • 48
    • 0028885545 scopus 로고
    • Ectodermal stimulation of the production of hyaluronan-dependent pericellular matrix by embryonic limb mesodermal cells
    • Knudson CB, Munaim SI, Toole BP. Ectodermal stimulation of the production of hyaluronan-dependent pericellular matrix by embryonic limb mesodermal cells. Dev Dynamics 1995, 204, 186-191.
    • (1995) Dev Dynamics , vol.204 , pp. 186-191
    • Knudson, C.B.1    Munaim, S.I.2    Toole, B.P.3
  • 49
    • 0029890525 scopus 로고    scopus 로고
    • Hyaluronan-mediated aggregation of limb bud mesenchyme and mesenchymal condensation during chondrogenesis
    • Maleski MP, Knudson CB. Hyaluronan-mediated aggregation of limb bud mesenchyme and mesenchymal condensation during chondrogenesis. Exp Cell Res 1996, 225, 55-66.
    • (1996) Exp Cell Res , vol.225 , pp. 55-66
    • Maleski, M.P.1    Knudson, C.B.2
  • 50
    • 0023809479 scopus 로고
    • Tumor invasion: A consequence of destructive and compositional matrix alterations
    • Pauli BU, Knudson W. Tumor invasion: a consequence of destructive and compositional matrix alterations. Human Pathol 1988, 19, 628-639.
    • (1988) Human Pathol , vol.19 , pp. 628-639
    • Pauli, B.U.1    Knudson, W.2
  • 51
    • 0030014714 scopus 로고    scopus 로고
    • Tumor-associated hyaluronan. Providing an extracellular matrix that facilitates invasion
    • Knudson W. Tumor-associated hyaluronan. Providing an extracellular matrix that facilitates invasion. Amer J Pathol 1996, 148, 1721-1726.
    • (1996) Amer J Pathol , vol.148 , pp. 1721-1726
    • Knudson, W.1
  • 52
    • 0000913748 scopus 로고
    • Hyaluronate and invasiveness of the rabbit V2 carcinoma
    • Toole BP, Biswas C, Gross J. Hyaluronate and invasiveness of the rabbit V2 carcinoma. Proc Natl Acad Sci USA 1979, 76, 6299-6303.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 6299-6303
    • Toole, B.P.1    Biswas, C.2    Gross, J.3
  • 53
    • 0006585248 scopus 로고
    • Interactions between human tumor cells and fibroblasts stimulate hyaluronate synthesis
    • Knudson W, Biswas C, Toole BP. Interactions between human tumor cells and fibroblasts stimulate hyaluronate synthesis. Proc Natl Acad Sci USA 1984, 81, 6767-6771.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6767-6771
    • Knudson, W.1    Biswas, C.2    Toole, B.P.3
  • 54
    • 0026087054 scopus 로고
    • Beneficial actions of exogenous hyaluronic acid on wound healing
    • King SR, Hickerson WL, Proctor KG. Beneficial actions of exogenous hyaluronic acid on wound healing. Surgery 1991, 109, 76-84.
    • (1991) Surgery , vol.109 , pp. 76-84
    • King, S.R.1    Hickerson, W.L.2    Proctor, K.G.3
  • 55
    • 0021834944 scopus 로고
    • Angiogenesis induced by degradation products of hyaluronic acid
    • West DC, Hampson IN, Arnold F, Kumar S. Angiogenesis induced by degradation products of hyaluronic acid. Science 1985, 228, 1324-1326.
    • (1985) Science , vol.228 , pp. 1324-1326
    • West, D.C.1    Hampson, I.N.2    Arnold, F.3    Kumar, S.4
  • 56
    • 0024508906 scopus 로고
    • Stimulation of glycosaminoglycan synthesis in cultured human dermal fibroblasts by interleukin 1. Induction of hyaluronic acid synthesis by natural and recombinant interleukin 1s and synthetic interleukin 1 β peptide 163-171
    • Postlethwaite AE, Smith GN Jr, Lachman LB, Endres RO, Poppleton HM, Hasty KA, Seyer JM, Kang AH. Stimulation of glycosaminoglycan synthesis in cultured human dermal fibroblasts by interleukin 1. Induction of hyaluronic acid synthesis by natural and recombinant interleukin 1s and synthetic interleukin 1 β peptide 163-171. J Clin Invest 1989, 83, 629-636.
    • (1989) J Clin Invest , vol.83 , pp. 629-636
    • Postlethwaite, A.E.1    Smith G.N., Jr.2    Lachman, L.B.3    Endres, R.O.4    Poppleton, H.M.5    Hasty, K.A.6    Seyer, J.M.7    Kang, A.H.8
  • 57
    • 0023761434 scopus 로고
    • Stimulation of the hyaluronic acid levels of human synovial fibroblasts by recombinant human tumor necrosis factor α, tumor necrosis factor β (lymphotoxin), interleukin-1 α, and interleukin-1 β
    • Butler DM, Vitti GF, Leizer T, Hamilton JA. Stimulation of the hyaluronic acid levels of human synovial fibroblasts by recombinant human tumor necrosis factor α, tumor necrosis factor β (lymphotoxin), interleukin-1 α, and interleukin-1 β. Arth Rheum 1988, 31, 1281-1289.
    • (1988) Arth Rheum , vol.31 , pp. 1281-1289
    • Butler, D.M.1    Vitti, G.F.2    Leizer, T.3    Hamilton, J.A.4
  • 58
    • 0026750564 scopus 로고
    • Correlation between increased hyaluronan localized in arthritic synovium and the presence of proliferating cells. A role for macrophage-derived factors
    • Wells AF, Klareskog L, Lindblad S, Laurent TC. Correlation between increased hyaluronan localized in arthritic synovium and the presence of proliferating cells. A role for macrophage-derived factors. Arth Rheum 1992, 35, 391-396.
    • (1992) Arth Rheum , vol.35 , pp. 391-396
    • Wells, A.F.1    Klareskog, L.2    Lindblad, S.3    Laurent, T.C.4
  • 59
    • 0026320564 scopus 로고
    • Morphological localization of hyaluronan in normal and diseased synovium
    • Worrall JG, Bayliss MT, Edwards JCW. Morphological localization of hyaluronan in normal and diseased synovium. J Rheum 1991, 18, 1466-1472.
    • (1991) J Rheum , vol.18 , pp. 1466-1472
    • Worrall, J.G.1    Bayliss, M.T.2    Edwards, J.C.W.3
  • 60
    • 0029002861 scopus 로고
    • Anti-CD44 treatment abrogates tissue oedema and leukocyte infiltration in murine arthritis
    • Mikecz K, Brennan FR, Kim JH, Glant TT. Anti-CD44 treatment abrogates tissue oedema and leukocyte infiltration in murine arthritis. Nature Med 1995, 1, 558-563.
    • (1995) Nature Med , vol.1 , pp. 558-563
    • Mikecz, K.1    Brennan, F.R.2    Kim, J.H.3    Glant, T.T.4
  • 61
    • 0037848790 scopus 로고
    • TSG-6: A TNF-and IL-1-inducible 39 kD hyaluronate binding protein with homology to the cartilage link protein family
    • eds A. Mantovani and P. Ghezzi. Biomedical Press, Augusta, GA
    • Wisniewski H-G, Lee TH, Lee S. Vilček J. TSG-6: A TNF-and IL-1-inducible 39 kD hyaluronate binding protein with homology to the cartilage link protein family. In Physiology and Pathophysiology of Cytokines, eds A. Mantovani and P. Ghezzi. Biomedical Press, Augusta, GA, 1992, pp. 149-155.
    • (1992) Physiology and Pathophysiology of Cytokines , pp. 149-155
    • Wisniewski, H.-G.1    Lee, T.H.2    Lee, S.3    Vilček, J.4
  • 62
    • 0028365753 scopus 로고
    • TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-α-inhibitor
    • Wisniewski H-G, Burgess WH, Oppenheim JD, Vilček J. TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-α-inhibitor. Biochemistry 1994, 33, 7423-7429.
    • (1994) Biochemistry , vol.33 , pp. 7423-7429
    • Wisniewski, H.-G.1    Burgess, W.H.2    Oppenheim, J.D.3    Vilček, J.4
  • 63
    • 0004801943 scopus 로고
    • 2-globulin from human plasma
    • 2-globulin from human plasma. Nature 1961, 192, 1196.
    • (1961) Nature , vol.192 , pp. 1196
    • Steinbuch, M.1    Loeb, J.2
  • 65
    • 0029669926 scopus 로고    scopus 로고
    • The inter-α-inhibitor family: From structure to regulation
    • Salier JP, Rouet P, Raguenez G, Daveau M. The inter-α-inhibitor family: from structure to regulation. Biochem J 1996, 315, 1-9.
    • (1996) Biochem J , vol.315 , pp. 1-9
    • Salier, J.P.1    Rouet, P.2    Raguenez, G.3    Daveau, M.4
  • 66
    • 0024459170 scopus 로고
    • Analysis of inter-α-trypsin inhibitor and a novel trypsin inhibitor, pre-α-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycan
    • Enghild JJ, Thøgersen IB, Pizzo SV, Salvesen G. Analysis of inter-α-trypsin inhibitor and a novel trypsin inhibitor, pre-α-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycan. J Biol Chem 1989, 264, 15975-15981.
    • (1989) J Biol Chem , vol.264 , pp. 15975-15981
    • Enghild, J.J.1    Thøgersen, I.B.2    Pizzo, S.V.3    Salvesen, G.4
  • 67
    • 0024355203 scopus 로고
    • Two out of the three kinds of subunits of inter-a-trypsin inhibitor are structurally related
    • Gebhard W, Schreitmfller T, Hochstrasser K, Wachter E. Two out of the three kinds of subunits of inter-a-trypsin inhibitor are structurally related. Eur J Biochem 1989, 181, 571-576.
    • (1989) Eur J Biochem , vol.181 , pp. 571-576
    • Gebhard, W.1    Schreitmfller, T.2    Hochstrasser, K.3    Wachter, E.4
  • 68
    • 0025147205 scopus 로고
    • Structure of inter-α-inhibitor (inter-α-trypsin inhibitor) and pre-α-inhibitor: Current state and proposition of a new terminology
    • Gebhard W, Hochstrasser K, Fritz H, Enghild JJ, Pizzo SV, Salvesen G. Structure of inter-α-inhibitor (inter-α-trypsin inhibitor) and pre-α-inhibitor: current state and proposition of a new terminology. Biol Chem Hoppe-Seyler 1990, 371, 13-22.
    • (1990) Biol Chem Hoppe-seyler , vol.371 , pp. 13-22
    • Gebhard, W.1    Hochstrasser, K.2    Fritz, H.3    Enghild, J.J.4    Pizzo, S.V.5    Salvesen, G.6
  • 69
    • 0023841833 scopus 로고
    • Carbohydrate as covalent crosslink in human inter-α-trypsin inhibitor: A novel plasma protein structure
    • Jessen TE, Faarvang KL, Ploug M. Carbohydrate as covalent crosslink in human inter-α-trypsin inhibitor: a novel plasma protein structure. FEBS Lett 1988, 230, 195-200.
    • (1988) FEBS Lett , vol.230 , pp. 195-200
    • Jessen, T.E.1    Faarvang, K.L.2    Ploug, M.3
  • 70
    • 0024551443 scopus 로고
    • A proteoglycan related to the urinary trypsin inhibitor (UTI) links the two heavy chains of inter-α-trypsin inhibitor
    • Balduyck M, Laroui S, Mizon C, Mizon J. A proteoglycan related to the urinary trypsin inhibitor (UTI) links the two heavy chains of inter-α-trypsin inhibitor. Biol Chem Hoppe-Seyler 1989, 370, 329-336.
    • (1989) Biol Chem Hoppe-seyler , vol.370 , pp. 329-336
    • Balduyck, M.1    Laroui, S.2    Mizon, C.3    Mizon, J.4
  • 71
    • 0027479832 scopus 로고
    • Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-α-inhibitor-related proteinase inhibitor heavy chain 2/bikunin
    • Enghild JJ, Salvesen G, Thøgersen IB, Valnickova Z, Pizzo SV, Hefta SA. Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-α-inhibitor-related proteinase inhibitor heavy chain 2/bikunin. J Biol Chem 1993, 268, 8711-8716.
    • (1993) J Biol Chem , vol.268 , pp. 8711-8716
    • Enghild, J.J.1    Salvesen, G.2    Thøgersen, I.B.3    Valnickova, Z.4    Pizzo, S.V.5    Hefta, S.A.6
  • 72
    • 0026089274 scopus 로고
    • Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-α-inhibitor
    • Enghild JJ, Salvesen G, Hefta SA, Thøgersen IB, Rutherfurd S, Pizzo SV. Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-α-inhibitor. J Biol Chem 1991, 266, 747-751.
    • (1991) J Biol Chem , vol.266 , pp. 747-751
    • Enghild, J.J.1    Salvesen, G.2    Hefta, S.A.3    Thøgersen, I.B.4    Rutherfurd, S.5    Pizzo, S.V.6
  • 73
    • 0025816344 scopus 로고
    • A chondroitin-sulfate chain is located on serine-10 of the urinary trypsin inhibitor
    • Chirat F, Balduyck M, Mizon C, Laroui S, Sautiere P, Mizon J. A chondroitin-sulfate chain is located on serine-10 of the urinary trypsin inhibitor. Int J Biochem 1991, 23, 1201-1203.
    • (1991) Int J Biochem , vol.23 , pp. 1201-1203
    • Chirat, F.1    Balduyck, M.2    Mizon, C.3    Laroui, S.4    Sautiere, P.5    Mizon, J.6
  • 74
    • 0027208218 scopus 로고
    • Human inter-α-inhibitor family in inflammation: Simultaneous synthesis of positive and negative acute-phase proteins
    • Daveau M, Rouet P, Scotte M, Faye L, Hiron M, Lebreton J-P, Salier J-P. Human inter-α-inhibitor family in inflammation: simultaneous synthesis of positive and negative acute-phase proteins. Biochem J 1993, 292, 485-492.
    • (1993) Biochem J , vol.292 , pp. 485-492
    • Daveau, M.1    Rouet, P.2    Scotte, M.3    Faye, L.4    Hiron, M.5    Lebreton, J.-P.6    Salier, J.-P.7
  • 75
    • 0015153170 scopus 로고
    • The source of the inter-α trypsin inhibitor in pathologic hyaluronateprotein
    • Becker A, Sandson J. The source of the inter-α trypsin inhibitor in pathologic hyaluronateprotein. Arth Rheum 1971, 14, 764-766.
    • (1971) Arth Rheum , vol.14 , pp. 764-766
    • Becker, A.1    Sandson, J.2
  • 76
    • 0023928493 scopus 로고
    • Binding of haptoglobin, inter-α-trypsin inhibitor, and α 1 proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals
    • Hutadilok N, Ghosh P, Brooks PM. Binding of haptoglobin, inter-α-trypsin inhibitor, and α 1 proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals. Ann Rheum Dis 1988, 47, 377-385.
    • (1988) Ann Rheum Dis , vol.47 , pp. 377-385
    • Hutadilok, N.1    Ghosh, P.2    Brooks, P.M.3
  • 77
    • 0016787622 scopus 로고
    • Proteinase inhibitors in rheumatoid arthritis
    • Brackertz D, Hagmann J, Kueppers F. Proteinase inhibitors in rheumatoid arthritis. Ann Rheum Dis 1975, 34, 225-230.
    • (1975) Ann Rheum Dis , vol.34 , pp. 225-230
    • Brackertz, D.1    Hagmann, J.2    Kueppers, F.3
  • 78
    • 0028485259 scopus 로고
    • In vivo binding of human inter-alpha-trypsin inhibitor free heavy chains to hyaluronic acid
    • Jessen TE, Odum L, Johnsen AH. In vivo binding of human inter-alpha-trypsin inhibitor free heavy chains to hyaluronic acid. Biol Chem Hoppe-Sevler 1994, 375, 521-526.
    • (1994) Biol Chem Hoppe-Seyler , vol.375 , pp. 521-526
    • Jessen, T.E.1    Odum, L.2    Johnsen, A.H.3
  • 79
    • 0024428832 scopus 로고
    • Inter-α-trypsin inhibitor. Inhibition spectrum of native and derived forms
    • Potempa J, Kwon K, Chawla R, Travis J. Inter-α-trypsin inhibitor. Inhibition spectrum of native and derived forms. J Biol Chem 1989, 264, 15109-15114.
    • (1989) J Biol Chem , vol.264 , pp. 15109-15114
    • Potempa, J.1    Kwon, K.2    Chawla, R.3    Travis, J.4
  • 80
    • 0019282838 scopus 로고
    • Pathophysiological interpretation of kinetic constants of protease inhibitors
    • Bieth JG. Pathophysiological interpretation of kinetic constants of protease inhibitors. Bull Europ Physiopath Resp 1980, 16, 183-197.
    • (1980) Bull Europ Physiopath Resp , vol.16 , pp. 183-197
    • Bieth, J.G.1
  • 81
    • 0030056876 scopus 로고    scopus 로고
    • TNF/IL-1-inducible protein TSG-6 potentiates plasmin inhibition by inter-α-inhibitor and exerts a strong anti-inflammatory effect in vivo
    • Wisniewski H-G, Hua J-C, Poppers DM, Naime D, Vilček J, Cronstein BN. TNF/IL-1-inducible protein TSG-6 potentiates plasmin inhibition by inter-α-inhibitor and exerts a strong anti-inflammatory effect in vivo. J Immunol 1996, 156, 1609-1615.
    • (1996) J Immunol , vol.156 , pp. 1609-1615
    • Wisniewski, H.-G.1    Hua, J.-C.2    Poppers, D.M.3    Naime, D.4    Vilček, J.5    Cronstein, B.N.6
  • 82
    • 0026890915 scopus 로고
    • Cytokines and proteases in invasive processes: Molecular similarities between inflammation and cancer
    • Opdenakker G, Van Damme J. Cytokines and proteases in invasive processes: molecular similarities between inflammation and cancer. Cytokine 1992, 4, 251-258.
    • (1992) Cytokine , vol.4 , pp. 251-258
    • Opdenakker, G.1    Van Damme, J.2
  • 83
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss SJ. Tissue destruction by neutrophils. New Eng J Med 1989, 320, 365-376.
    • (1989) New Eng J Med , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 84
  • 85
    • 0001817366 scopus 로고
    • Cellular biology of cartilage degradation
    • eds B. Henderson, J. C. W. Edwards and E. R. Pettipher. Academic Press, London
    • Poole AR, Alini M, Hollander AP. Cellular biology of cartilage degradation. In Mechanisms and Models in Rheumatoid Arthritis, eds B. Henderson, J. C. W. Edwards and E. R. Pettipher. Academic Press, London, 1995, pp. 163-204.
    • (1995) Mechanisms and Models in Rheumatoid Arthritis , pp. 163-204
    • Poole, A.R.1    Alini, M.2    Hollander, A.P.3
  • 86
    • 0019159671 scopus 로고
    • Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages
    • Werb Z, Banda MJ, Jones PA. Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages. J Exp Med 1980, 152, 1340-1357.
    • (1980) J Exp Med , vol.152 , pp. 1340-1357
    • Werb, Z.1    Banda, M.J.2    Jones, P.A.3
  • 87
    • 0024146930 scopus 로고
    • Cell-associated plasminogen activation: Regulation and physiological functions
    • Saksela O, Rifkin DB. Cell-associated plasminogen activation: regulation and physiological functions. Ann Rev Cell Biol 1988, 4, 93-126.
    • (1988) Ann Rev Cell Biol , vol.4 , pp. 93-126
    • Saksela, O.1    Rifkin, D.B.2
  • 88
    • 0027263891 scopus 로고
    • Molecular mechanisms of protease-mediated tumor invasiveness
    • Blasi F. Molecular mechanisms of protease-mediated tumor invasiveness. J Surg Oncol Suppl 1993, 3, 21-23.
    • (1993) J Surg Oncol Suppl , vol.3 , pp. 21-23
    • Blasi, F.1
  • 90
    • 0343000402 scopus 로고
    • Growth factors in the pathogenesis of rheumatoid arthritis
    • eds B. Henderson, J. C. W. Edwards and E. R. Pettipher. Academic Press, London
    • Zagorski J, Wahl SM. Growth factors in the pathogenesis of rheumatoid arthritis. In Mechanisms and models in rheumatoid arthritis, eds B. Henderson, J. C. W. Edwards and E. R. Pettipher. Academic Press, London, 1995, pp. 243-259.
    • (1995) Mechanisms and Models in Rheumatoid Arthritis , pp. 243-259
    • Zagorski, J.1    Wahl, S.M.2
  • 91
    • 0024382711 scopus 로고
    • Inhibition of endothelial cell movement by pericytes and smooth muscle cells: Activation of a latent transforming growth factor-beta 1-like molecule by plasmin during co-culture
    • Sato Y, Rifkin DB. Inhibition of endothelial cell movement by pericytes and smooth muscle cells: activation of a latent transforming growth factor-beta 1-like molecule by plasmin during co-culture. J Cell Biol 1989, 109, 309-315.
    • (1989) J Cell Biol , vol.109 , pp. 309-315
    • Sato, Y.1    Rifkin, D.B.2
  • 92
    • 0025310993 scopus 로고
    • Characterization of the activation of latent TGF-beta 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 DB. Characterization of the activation of latent TGF-beta by co-cultures of endothelial cells and pericytes or smooth muscle cells: a self-regulating system. J Cell Biol 1990, 111, 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.B.5
  • 93
    • 0027270094 scopus 로고
    • Cartilage degradation by cocultures of transformed macrophage and fibroblast cell lines. A model of metalloproteinase-mediated connective tissue degradation
    • Janusz MJ, Hare M. Cartilage degradation by cocultures of transformed macrophage and fibroblast cell lines. A model of metalloproteinase-mediated connective tissue degradation. J Immunol 1993, 150, 1922-1931.
    • (1993) J Immunol , vol.150 , pp. 1922-1931
    • Janusz, M.J.1    Hare, M.2
  • 94
    • 0000999998 scopus 로고
    • Extracellular matrix degradation
    • ed. E. D. Hay. Plenum Press, New York
    • Alexander CM, Werb Z. Extracellular matrix degradation. In Cell Biology of Extracellular Matrix, ed. E. D. Hay. Plenum Press, New York, 1991, pp. 255-302.
    • (1991) Cell Biology of Extracellular Matrix , pp. 255-302
    • Alexander, C.M.1    Werb, Z.2
  • 95
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian LM. The matrix-degrading metalloproteinases. Bioessays 1992, 14, 455-463.
    • (1992) Bioessays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 96
    • 0023746649 scopus 로고
    • Membrane and matrix localization of proteinases: A common theme in tumor cell invasion and angiogenesis
    • Moscatelli D, Rifkin DB. Membrane and matrix localization of proteinases: a common theme in tumor cell invasion and angiogenesis. Biochim Biophys Acta 1988, 948, 67-85.
    • (1988) Biochim Biophys Acta , vol.948 , pp. 67-85
    • Moscatelli, D.1    Rifkin, D.B.2
  • 97
    • 0027015335 scopus 로고
    • Physiological mechanisms for metalloproteinase activation
    • Murphy G, Ward R, Gavrilovic J, Atkinson S. Physiological mechanisms for metalloproteinase activation. Matrix Suppl 1992, 1, 224-230.
    • (1992) Matrix Suppl , vol.1 , pp. 224-230
    • Murphy, G.1    Ward, R.2    Gavrilovic, J.3    Atkinson, S.4
  • 98
    • 0027683226 scopus 로고
    • Structural biochemistry and activation of matrix metalloproteases
    • Kleiner DE Jr. Stetler-Stevenson WG. Structural biochemistry and activation of matrix metalloproteases. Curr Opin Cell Biol 1993, 5, 891-897.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 891-897
    • Kleiner D.E., Jr.1    Stetler-Stevenson, W.G.2
  • 99
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti P, Rifkin DB. Biology and biochemistry of proteinases in tumor invasion. Physiol Revs 1993, 73, 161-195.
    • (1993) Physiol Revs , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 100
    • 0020431191 scopus 로고
    • Secretion of basement membrane collagen degrading enzyme and plasminogen activator by transformed cells-role in metastasis
    • Salo T, Liotta LA, Keski-Oja J, Turpeenniemi-Hujanen T, Tryggvason K. Secretion of basement membrane collagen degrading enzyme and plasminogen activator by transformed cells-role in metastasis. Int J Cancer 1982, 30, 669-673.
    • (1982) Int J Cancer , vol.30 , pp. 669-673
    • Salo, T.1    Liotta, L.A.2    Keski-Oja, J.3    Turpeenniemi-Hujanen, T.4    Tryggvason, K.5
  • 102
    • 0023902208 scopus 로고
    • Activation of human neutrophil gelatinase by endogenous serine proteinases
    • Vissers MCM. Winterbourn CC. Activation of human neutrophil gelatinase by endogenous serine proteinases. Biochem J 1988, 249, 327-331.
    • (1988) Biochem J , vol.249 , pp. 327-331
    • Vissers, M.C.M.1    Winterbourn, C.C.2
  • 103
    • 0029121925 scopus 로고
    • Gene targeting and gene transfer studies of the biological role of the plasminogen/plasmin system
    • Carmeliet P, Collen D. Gene targeting and gene transfer studies of the biological role of the plasminogen/plasmin system. Thrombosis & Haemostasis 1995, 74, 429-436.
    • (1995) Thrombosis & Haemostasis , vol.74 , pp. 429-436
    • Carmeliet, P.1    Collen, D.2
  • 105
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • Collen D, Lijnen HR. Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 1991, 78, 3114-3124.
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D.1    Lijnen, H.R.2
  • 107
    • 0026462546 scopus 로고
    • The plasminogen-plasmin system in malignancy
    • Kwaan HC. The plasminogen-plasmin system in malignancy. Cancer Metastasis Rev 1992, 11, 291-311.
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 291-311
    • Kwaan, H.C.1
  • 108
    • 0024508318 scopus 로고
    • Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes
    • Ellis V, Scully MF, Kakkar VV. Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes. J Biol Chem 1989, 264, 2185-2188.
    • (1989) J Biol Chem , vol.264 , pp. 2185-2188
    • Ellis, V.1    Scully, M.F.2    Kakkar, V.V.3
  • 109
    • 0021984227 scopus 로고
    • A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase
    • Vassalli JD, Baccino D, Belin D. A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase. J Cell Biol 1985, 100, 86-92.
    • (1985) J Cell Biol , vol.100 , pp. 86-92
    • Vassalli, J.D.1    Baccino, D.2    Belin, D.3
  • 113
    • 0025052018 scopus 로고
    • Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis
    • Roldan AL, Cubellis MV, Masucci MT, Behrendt N, Lund LR, Dano K, Appella E, Blasi F. Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis. EMBO J 1990, 9, 467-474.
    • (1990) EMBO J , vol.9 , pp. 467-474
    • Roldan, A.L.1    Cubellis, M.V.2    Masucci, M.T.3    Behrendt, N.4    Lund, L.R.5    Dano, K.6    Appella, E.7    Blasi, F.8
  • 114
    • 0026063532 scopus 로고
    • Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol
    • Ploug M, Ronne E, Behrendt N, Jensen AL, Blasi F, Dano K. Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol. J Biol Chem 1991, 266, 1926-1933.
    • (1991) J Biol Chem , vol.266 , pp. 1926-1933
    • Ploug, M.1    Ronne, E.2    Behrendt, N.3    Jensen, A.L.4    Blasi, F.5    Dano, K.6
  • 115
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor
    • Miles LA, Dahlberg CM, Plescia J, Felez J, Kato K, Plow EF. Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 1991, 30, 1682-1691.
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 116
    • 0025833080 scopus 로고
    • Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen
    • Kanalas JJ, Makker SP. Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen. J Biol Chem 1991, 266, 10825-10829.
    • (1991) J Biol Chem , vol.266 , pp. 10825-10829
    • Kanalas, J.J.1    Makker, S.P.2
  • 117
    • 0028095128 scopus 로고
    • Characterization of the plasminogen receptors of normal and rheumatoid arthritis human synovial fibroblasts
    • Gonzalez-Gronow M, Gawdi G, Pizzo SV. Characterization of the plasminogen receptors of normal and rheumatoid arthritis human synovial fibroblasts. J Biol Chem 1994, 269, 4360-4366.
    • (1994) J Biol Chem , vol.269 , pp. 4360-4366
    • Gonzalez-Gronow, M.1    Gawdi, G.2    Pizzo, S.V.3
  • 118
    • 0023025270 scopus 로고
    • The plasminogen system and cell surfaces: Evidence for plasminogen and urokinase receptors on the same cell type
    • Plow EF, Freaney DE, Plescia J, Miles LA. The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type. J Cell Biol 1986, 103, 2411-2420.
    • (1986) J Cell Biol , vol.103 , pp. 2411-2420
    • Plow, E.F.1    Freaney, D.E.2    Plescia, J.3    Miles, L.A.4
  • 120
    • 0027458531 scopus 로고
    • Plasminogen and plasminogen activator assembly on the human endothelial cell
    • Shih GC, Hajjar KA. Plasminogen and plasminogen activator assembly on the human endothelial cell. Proc Soc Exp Biol & Med 1993, 202, 258-264.
    • (1993) Proc Soc Exp Biol & Med , vol.202 , pp. 258-264
    • Shih, G.C.1    Hajjar, K.A.2
  • 121
    • 0024365970 scopus 로고
    • Further characterization of the binding of plasminogen to heparin: Evidence for the involvement of lysine residues
    • Soeda S, Ohki H, Shimeno H, Nagamatsu A. Further characterization of the binding of plasminogen to heparin: evidence for the involvement of lysine residues. Biochim Biophys Acta 1989, 999, 29-35.
    • (1989) Biochim Biophys Acta , vol.999 , pp. 29-35
    • Soeda, S.1    Ohki, H.2    Shimeno, H.3    Nagamatsu, A.4
  • 122
    • 0025354583 scopus 로고
    • Kinetic analysis of the effects of heparin and lipoproteins on tissue plasminogen activator mediated plasminogen activation
    • Edelberg JM, Pizzo SV. Kinetic analysis of the effects of heparin and lipoproteins on tissue plasminogen activator mediated plasminogen activation. Biochemistry 1990, 29, 5906-5911.
    • (1990) Biochemistry , vol.29 , pp. 5906-5911
    • Edelberg, J.M.1    Pizzo, S.V.2
  • 123
    • 0025802985 scopus 로고
    • Kinetic analysis of the effects of glycosaminoglycans and lipoproteins on urokinase-mediated plasminogen activation
    • Edelberg JM, Weissler M, Pizzo SV. Kinetic analysis of the effects of glycosaminoglycans and lipoproteins on urokinase-mediated plasminogen activation. Biochem J 1991, 276, 785-791.
    • (1991) Biochem J , vol.276 , pp. 785-791
    • Edelberg, J.M.1    Weissler, M.2    Pizzo, S.V.3
  • 124
    • 0025173417 scopus 로고
    • Animal models of chronic inflammatory arthritis
    • Magilavy DB. Animal models of chronic inflammatory arthritis. Clin Orthopaedics Related Res 1990, 259, 38-45.
    • (1990) Clin Orthopaedics Related Res , vol.259 , pp. 38-45
    • Magilavy, D.B.1
  • 125
    • 0027139914 scopus 로고
    • The antiinflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation
    • Cronstein BN, Naime D, Ostad E. The antiinflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation. J Clin Invest 1993, 92, 2675-2682.
    • (1993) J Clin Invest , vol.92 , pp. 2675-2682
    • Cronstein, B.N.1    Naime, D.2    Ostad, E.3
  • 126
    • 0027284754 scopus 로고
    • Modulation of IL-1-induced neutrophil migration by dexamethasone and lipocortin 1
    • Perretti M, Flower RJ. Modulation of IL-1-induced neutrophil migration by dexamethasone and lipocortin 1. J Immunol 1993, 150, 992-999.
    • (1993) J Immunol , vol.150 , pp. 992-999
    • Perretti, M.1    Flower, R.J.2
  • 127
    • 0019424377 scopus 로고
    • The formation of a structure with the features of synovial lining by subcutaneous injection of air: An in vivo tissue culture system
    • Edwards JC, Sedgwick AD, Willoughby DA. The formation of a structure with the features of synovial lining by subcutaneous injection of air: an in vivo tissue culture system. J Pathol 1981, 134, 147-156.
    • (1981) J Pathol , vol.134 , pp. 147-156
    • Edwards, J.C.1    Sedgwick, A.D.2    Willoughby, D.A.3
  • 128
  • 129
    • 0029064789 scopus 로고
    • Effects of serine protease inhibitors on accumulation of polymorphonuclear leukocytes in the lung induced by acute pancreatitis in rats
    • Okumura Y, Inoue H, Fujiyama Y, Bamba T. Effects of serine protease inhibitors on accumulation of polymorphonuclear leukocytes in the lung induced by acute pancreatitis in rats. J Gastroenterol 1995, 30, 379-386.
    • (1995) J Gastroenterol , vol.30 , pp. 379-386
    • Okumura, Y.1    Inoue, H.2    Fujiyama, Y.3    Bamba, T.4
  • 130
    • 0024560984 scopus 로고
    • A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family
    • Stamenkovic I, Amiot M, Pesando JM, Seed B. A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family. Cell 1989, 56, 1057-1062.
    • (1989) Cell , vol.56 , pp. 1057-1062
    • Stamenkovic, I.1    Amiot, M.2    Pesando, J.M.3    Seed, B.4
  • 131
    • 0024517268 scopus 로고
    • A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins
    • Goldstein LA, Zhou DF, Picker LJ, Minty CN, Bargatze RF, Ding JF, Butcher EC. A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins. Cell 1989, 56, 1063-1072.
    • (1989) Cell , vol.56 , pp. 1063-1072
    • Goldstein, L.A.1    Zhou, D.F.2    Picker, L.J.3    Minty, C.N.4    Bargatze, R.F.5    Ding, J.F.6    Butcher, E.C.7
  • 132
    • 0023632550 scopus 로고
    • Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones
    • published erratum appears in J Biol Chem 1988 Jul 15; 263(20): 10040
    • Doege K, Sasaki M, Horigan E, Hassell JR, Yamada Y. Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones [published erratum appears in J Biol Chem 1988 Jul 15; 263(20): 10040]. J Biol Chem 1987, 262, 17757-17767.
    • (1987) J Biol Chem , vol.262 , pp. 17757-17767
    • Doege, K.1    Sasaki, M.2    Horigan, E.3    Hassell, J.R.4    Yamada, Y.5
  • 133
    • 0024397823 scopus 로고
    • Multiple domains of the large fibroblast proteoglycan, versican
    • Zimmermann DR, Ruoslahti E. Multiple domains of the large fibroblast proteoglycan, versican. EMBO J 1989, 8, 2975-2981.
    • (1989) EMBO J , vol.8 , pp. 2975-2981
    • Zimmermann, D.R.1    Ruoslahti, E.2
  • 134
    • 0028586829 scopus 로고
    • Molecular cloning of a mammalian hyaluronidase reveals identity with hemopexin, a serum heme-binding protein
    • Zhu L, Hope TJ, Hall J, Davies A, Stern M, Muller-Eberhard U, Stern R, Parslow TG. Molecular cloning of a mammalian hyaluronidase reveals identity with hemopexin, a serum heme-binding protein. J Biol Chem 1994, 269, 32092-32097.
    • (1994) J Biol Chem , vol.269 , pp. 32092-32097
    • Zhu, L.1    Hope, T.J.2    Hall, J.3    Davies, A.4    Stern, M.5    Muller-Eberhard, U.6    Stern, R.7    Parslow, T.G.8


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