메뉴 건너뛰기




Volumn 1760, Issue 3, 2006, Pages 472-486

Mammalian expression of full-length bovine aggrecan and link protein: Formation of recombinant proteoglycan aggregates and analysis of proteolytic cleavage by ADAMTS-4 and MMP-13

Author keywords

ADAMTS 4; Aggrecan; Aggrecanase; Aggrecanolysis; Link protein; MMP 13; Proteoglycan aggregate

Indexed keywords

AGGRECAN; CHONDROITIN ABC LYASE; CHONDROITIN SULFATE; COLLAGENASE 3; GLYCOSAMINOGLYCAN; HYALURONIC ACID; LINK PROTEIN; METALLOPROTEINASE; MONOMER; PROTEIN P40; PROTEIN P68; PROTEOGLYCAN; RECOMBINANT PROTEIN; SERINE;

EID: 33644912865     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.12.003     Document Type: Article
Times cited : (24)

References (78)
  • 2
    • 0024406159 scopus 로고
    • Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Identification of G2 domain and its lack of interaction with hyaluronate and link protein
    • A.J. Fosang, and T.E. Hardingham Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Identification of G2 domain and its lack of interaction with hyaluronate and link protein Biochem. J. 261 1989 801 809
    • (1989) Biochem. J. , vol.261 , pp. 801-809
    • Fosang, A.J.1    Hardingham, T.E.2
  • 3
    • 0025976188 scopus 로고
    • Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms
    • K.J. Doege, M. Sasaki, T. Kimura, and Y. Yamada Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms J. Biol. Chem. 266 1991 894 902
    • (1991) J. Biol. Chem. , vol.266 , pp. 894-902
    • Doege, K.J.1    Sasaki, M.2    Kimura, T.3    Yamada, Y.4
  • 4
    • 0030069604 scopus 로고    scopus 로고
    • Age-related changes in the content of the C-terminal region of aggrecan in human articular cartilage
    • J. Dudhia, C.M. Davidson, T.M. Wells, D.H. Vynios, T.E. Hardingham, and M.T. Bayliss Age-related changes in the content of the C-terminal region of aggrecan in human articular cartilage Biochem. J. 313 Pt. 3 1996 933 940
    • (1996) Biochem. J. , vol.313 , Issue.1 PART , pp. 933-940
    • Dudhia, J.1    Davidson, C.M.2    Wells, T.M.3    Vynios, D.H.4    Hardingham, T.E.5    Bayliss, M.T.6
  • 6
    • 0036775227 scopus 로고    scopus 로고
    • Characterization of human aggrecanase 2 (ADAM-TS5): Substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
    • M.D. Tortorella, R.Q. Liu, T. Burn, R.C. Newton, and E. Arner Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4) Matrix Biol. 21 2002 499 511
    • (2002) Matrix Biol. , vol.21 , pp. 499-511
    • Tortorella, M.D.1    Liu, R.Q.2    Burn, T.3    Newton, R.C.4    Arner, E.5
  • 14
    • 0030024311 scopus 로고    scopus 로고
    • Degradation of cartilage aggrecan by collagenase-3 (MMP-13)
    • A.J. Fosang, K. Last, V. Knauper, G. Murphy, and P.J. Neame Degradation of cartilage aggrecan by collagenase-3 (MMP-13) FEBS Lett. 380 1996 17 20
    • (1996) FEBS Lett. , vol.380 , pp. 17-20
    • Fosang, A.J.1    Last, K.2    Knauper, V.3    Murphy, G.4    Neame, P.J.5
  • 15
    • 0037151084 scopus 로고    scopus 로고
    • Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage
    • A.M. Malfait, R.Q. Liu, K. Ijiri, S. Komiya, and M.D. Tortorella Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage J. Biol. Chem. 277 2002 22201 22208
    • (2002) J. Biol. Chem. , vol.277 , pp. 22201-22208
    • Malfait, A.M.1    Liu, R.Q.2    Ijiri, K.3    Komiya, S.4    Tortorella, M.D.5
  • 16
    • 0035884605 scopus 로고    scopus 로고
    • Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo
    • J.D. Sandy, and C. Verscharen Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo Biochem. J. 358 2001 615 626
    • (2001) Biochem. J. , vol.358 , pp. 615-626
    • Sandy, J.D.1    Verscharen, C.2
  • 17
    • 4344601054 scopus 로고    scopus 로고
    • Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by m-calpain
    • H. Oshita, J.D. Sandy, K. Suzuki, A. Akaike, Y. Bai, T. Sasaki, and K. Shimizu Mature bovine articular cartilage contains abundant aggrecan that is C-terminally truncated at Ala719-Ala720, a site which is readily cleaved by m-calpain Biochem. J. 382 2004 253 259
    • (2004) Biochem. J. , vol.382 , pp. 253-259
    • Oshita, H.1    Sandy, J.D.2    Suzuki, K.3    Akaike, A.4    Bai, Y.5    Sasaki, T.6    Shimizu, K.7
  • 19
    • 0037192814 scopus 로고    scopus 로고
    • Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C-terminal truncation
    • G. Gao, J. Westling, V.P. Thompson, T.D. Howell, P.E. Gottschall, and J.D. Sandy Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C-terminal truncation J. Biol. Chem. 277 2002 11034 11041
    • (2002) J. Biol. Chem. , vol.277 , pp. 11034-11041
    • Gao, G.1    Westling, J.2    Thompson, V.P.3    Howell, T.D.4    Gottschall, P.E.5    Sandy, J.D.6
  • 21
    • 0034306104 scopus 로고    scopus 로고
    • The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1
    • J.D. Sandy, V. Thompson, K. Doege, and C. Verscharen The intermediates of aggrecanase-dependent cleavage of aggrecan in rat chondrosarcoma cells treated with interleukin-1 Biochem. J. 351 2000 161 166
    • (2000) Biochem. J. , vol.351 , pp. 161-166
    • Sandy, J.D.1    Thompson, V.2    Doege, K.3    Verscharen, C.4
  • 22
    • 0036499471 scopus 로고    scopus 로고
    • The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism
    • R. Sztrolovics, R.J. White, P.J. Roughley, and J.S. Mort The mechanism of aggrecan release from cartilage differs with tissue origin and the agent used to stimulate catabolism Biochem. J. 362 2002 465 472
    • (2002) Biochem. J. , vol.362 , pp. 465-472
    • Sztrolovics, R.1    White, R.J.2    Roughley, P.J.3    Mort, J.S.4
  • 23
    • 0030931594 scopus 로고    scopus 로고
    • Aggrecan degradation in human intervertebral disc and articular cartilage
    • R. Sztrolovics, M. Alini, P.J. Roughley, and J.S. Mort Aggrecan degradation in human intervertebral disc and articular cartilage Biochem. J. 326 Pt. 1 1997 235 241
    • (1997) Biochem. J. , vol.326 , Issue.1 PART , pp. 235-241
    • Sztrolovics, R.1    Alini, M.2    Roughley, P.J.3    Mort, J.S.4
  • 24
    • 0031282416 scopus 로고    scopus 로고
    • A structural requirement of zinc for the folding of recombinant link protein
    • J.B. Varelas, C. Roy, and T.M. Hering A structural requirement of zinc for the folding of recombinant link protein Arch. Biochem. Biophys. 347 1997 1 8
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 1-8
    • Varelas, J.B.1    Roy, C.2    Hering, T.M.3
  • 25
    • 0026531037 scopus 로고
    • Mammalian vitreous humor contains networks of hyaluronan molecules: Electron microscopic analysis using the hyaluronan-binding region (G1) of aggrecan and link protein
    • R.G. Brewton, and R. Mayne Mammalian vitreous humor contains networks of hyaluronan molecules: electron microscopic analysis using the hyaluronan-binding region (G1) of aggrecan and link protein Exp. Cell Res. 198 1992 237 249
    • (1992) Exp. Cell Res. , vol.198 , pp. 237-249
    • Brewton, R.G.1    Mayne, R.2
  • 26
    • 0017329710 scopus 로고
    • Distribution of keratan sulfate in cartilage proteoglycans
    • D. Heinegard, and I. Axelsson Distribution of keratan sulfate in cartilage proteoglycans J. Biol. Chem. 252 1977 1971 1979
    • (1977) J. Biol. Chem. , vol.252 , pp. 1971-1979
    • Heinegard, D.1    Axelsson, I.2
  • 27
    • 0015527706 scopus 로고
    • Extraction, fractionation and characterization of proteoglycans from bovine tracheal cartilage
    • D. Heinegard Extraction, fractionation and characterization of proteoglycans from bovine tracheal cartilage Biochim. Biophys. Acta 285 1972 181 192
    • (1972) Biochim. Biophys. Acta , vol.285 , pp. 181-192
    • Heinegard, D.1
  • 28
    • 0025864516 scopus 로고
    • Proteoglycans of bovine articular cartilage. the effects of divalent cations on the biochemical properties of link protein
    • L. Rosenberg, H.U. Choi, L.H. Tang, S. Pal, T. Johnson, D.A. Lyons, and T.M. Laue Proteoglycans of bovine articular cartilage. The effects of divalent cations on the biochemical properties of link protein J. Biol. Chem. 266 1991 7016 7024
    • (1991) J. Biol. Chem. , vol.266 , pp. 7016-7024
    • Rosenberg, L.1    Choi, H.U.2    Tang, L.H.3    Pal, S.4    Johnson, T.5    Lyons, D.A.6    Laue, T.M.7
  • 29
    • 0020267594 scopus 로고
    • Synthesis of cartilage matrix by mammalian chondrocytes in vitro. I. Isolation, culture characteristics, and morphology
    • K.E. Kuettner, B.U. Pauli, G. Gall, V.A. Memoli, and R.K. Schenk Synthesis of cartilage matrix by mammalian chondrocytes in vitro. I. Isolation, culture characteristics, and morphology J. Cell Biol. 93 1982 743 750
    • (1982) J. Cell Biol. , vol.93 , pp. 743-750
    • Kuettner, K.E.1    Pauli, B.U.2    Gall, G.3    Memoli, V.A.4    Schenk, R.K.5
  • 30
    • 0023161202 scopus 로고
    • Proteoglycans: Isolation and purification from tissue cultures
    • M. Yanagishita, R.J. Midura, and V.C. Hascall Proteoglycans: isolation and purification from tissue cultures Methods Enzymol. 138 1987 279 289
    • (1987) Methods Enzymol. , vol.138 , pp. 279-289
    • Yanagishita, M.1    Midura, R.J.2    Hascall, V.C.3
  • 31
    • 0031572290 scopus 로고    scopus 로고
    • Complete coding sequence of bovine aggrecan: Comparative structural analysis
    • T.M. Hering, J. Kollar, and T.D. Huynh Complete coding sequence of bovine aggrecan: comparative structural analysis Arch. Biochem. Biophys. 345 1997 259 270
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 259-270
    • Hering, T.M.1    Kollar, J.2    Huynh, T.D.3
  • 32
    • 0028841636 scopus 로고
    • Bovine chondrocyte link protein cDNA sequence: Interspecies conservation of primary structure and mRNA untranslated regions
    • T.M. Hering, J. Kollar, T.D. Huynh, and L.J. Sandell Bovine chondrocyte link protein cDNA sequence: interspecies conservation of primary structure and mRNA untranslated regions Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 112 1995 197 203
    • (1995) Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. , vol.112 , pp. 197-203
    • Hering, T.M.1    Kollar, J.2    Huynh, T.D.3    Sandell, L.J.4
  • 33
    • 0019641884 scopus 로고
    • A comparative study of the binding of cartilage link protein and the hyaluronate-binding region of the cartilage proteoglycan to hyaluronate- substituted Sepharose gel
    • A. Tengblad A comparative study of the binding of cartilage link protein and the hyaluronate-binding region of the cartilage proteoglycan to hyaluronate-substituted Sepharose gel Biochem. J. 199 1981 297 305
    • (1981) Biochem. J. , vol.199 , pp. 297-305
    • Tengblad, A.1
  • 34
    • 0025775546 scopus 로고
    • Agarose/polyacrylamide minislab gel electrophoresis of intact cartilage proteoglycans and their proteolytic degradation products
    • J.B. Varelas, N.R. Zenarosa, and C.J. Froelich Agarose/polyacrylamide minislab gel electrophoresis of intact cartilage proteoglycans and their proteolytic degradation products Anal. Biochem. 197 1991 396 400
    • (1991) Anal. Biochem. , vol.197 , pp. 396-400
    • Varelas, J.B.1    Zenarosa, N.R.2    Froelich, C.J.3
  • 35
    • 0025744238 scopus 로고
    • A spectrophotometric modification of a sensitive densitometric Safranin O assay for glycosaminoglycans
    • D.A. Carrino, J.L. Arias, and A.I. Caplan A spectrophotometric modification of a sensitive densitometric Safranin O assay for glycosaminoglycans Biochem. Int. 24 1991 485 495
    • (1991) Biochem. Int. , vol.24 , pp. 485-495
    • Carrino, D.A.1    Arias, J.L.2    Caplan, A.I.3
  • 36
    • 50549161624 scopus 로고
    • A modified uronic acid carbazole reaction
    • T. Bitter, and H.M. Muir A modified uronic acid carbazole reaction Anal. Biochem. 4 1962 330 334
    • (1962) Anal. Biochem. , vol.4 , pp. 330-334
    • Bitter, T.1    Muir, H.M.2
  • 37
    • 0015215284 scopus 로고
    • A method for the determination of the molecular weight and molecular-weight distribution of chondroitin sulphate
    • A. Wasteson A method for the determination of the molecular weight and molecular-weight distribution of chondroitin sulphate J. Chromatogr. 59 1971 87 97
    • (1971) J. Chromatogr. , vol.59 , pp. 87-97
    • Wasteson, A.1
  • 38
    • 0023657295 scopus 로고
    • A study of the interaction between cartilage proteoglycan and link protein
    • D.J. Thornton, J.K. Sheehan, and I.A. Nieduszynski A study of the interaction between cartilage proteoglycan and link protein Biochem. J. 248 1987 943 951
    • (1987) Biochem. J. , vol.248 , pp. 943-951
    • Thornton, D.J.1    Sheehan, J.K.2    Nieduszynski, I.A.3
  • 39
    • 0030046593 scopus 로고    scopus 로고
    • Biotinylated hyaluronan: A versatile and highly sensitive probe capable of detecting nanogram levels of hyaluronan binding proteins (hyaladherins) on electroblots by a novel affinity detection procedure
    • J. Melrose, Y. Numata, and P. Ghosh Biotinylated hyaluronan: a versatile and highly sensitive probe capable of detecting nanogram levels of hyaluronan binding proteins (hyaladherins) on electroblots by a novel affinity detection procedure Electrophoresis 17 1996 205 212
    • (1996) Electrophoresis , vol.17 , pp. 205-212
    • Melrose, J.1    Numata, Y.2    Ghosh, P.3
  • 40
    • 0015177830 scopus 로고
    • Gel electrophoresis of proteoglycans and glycosaminoglycans on large-pore composite polyacrylamide-agarose gels
    • C.A. McDevitt, and H. Muir Gel electrophoresis of proteoglycans and glycosaminoglycans on large-pore composite polyacrylamide-agarose gels Anal. Biochem. 44 1971 612 622
    • (1971) Anal. Biochem. , vol.44 , pp. 612-622
    • McDevitt, C.A.1    Muir, H.2
  • 41
    • 0022542863 scopus 로고
    • The antigenic determinants recognized by three monoclonal antibodies to keratan sulphate involve sulphated hepta- or larger oligosaccharides of the poly(N-acetyllactosamine) series
    • H. Mehmet, P. Scudder, P.W. Tang, E.F. Hounsell, B. Caterson, and T. Feizi The antigenic determinants recognized by three monoclonal antibodies to keratan sulphate involve sulphated hepta- or larger oligosaccharides of the poly(N-acetyllactosamine) series Eur. J. Biochem. 157 1986 385 391
    • (1986) Eur. J. Biochem. , vol.157 , pp. 385-391
    • Mehmet, H.1    Scudder, P.2    Tang, P.W.3    Hounsell, E.F.4    Caterson, B.5    Feizi, T.6
  • 42
    • 0025145612 scopus 로고
    • Biosynthesis and processing of bovine cartilage link proteins
    • T.M. Hering, and L.J. Sandell Biosynthesis and processing of bovine cartilage link proteins J. Biol. Chem. 265 1990 2375 2382
    • (1990) J. Biol. Chem. , vol.265 , pp. 2375-2382
    • Hering, T.M.1    Sandell, L.J.2
  • 43
    • 0008169626 scopus 로고
    • Identity of the protein cores of the two link proteins from bovine nasal cartilage proteoglycan complex. Localization of their sugar moieties
    • S. Le Gledic, J.P. Perin, F. Bonnet, and P. Jolles Identity of the protein cores of the two link proteins from bovine nasal cartilage proteoglycan complex. Localization of their sugar moieties J. Biol. Chem. 258 1983 14759 14761
    • (1983) J. Biol. Chem. , vol.258 , pp. 14759-14761
    • Le Gledic, S.1    Perin, J.P.2    Bonnet, F.3    Jolles, P.4
  • 44
    • 0022386760 scopus 로고
    • The origin of human cartilage proteoglycan link-protein heterogeneity and fragmentation during aging
    • J.S. Mort, B. Caterson, A.R. Poole, and P.J. Roughley The origin of human cartilage proteoglycan link-protein heterogeneity and fragmentation during aging Biochem. J. 232 1985 805 812
    • (1985) Biochem. J. , vol.232 , pp. 805-812
    • Mort, J.S.1    Caterson, B.2    Poole, A.R.3    Roughley, P.J.4
  • 45
    • 0024307651 scopus 로고
    • Studies on the hyaluronate binding properties of newly synthesized proteoglycans purified from articular chondrocyte cultures
    • J.D. Sandy, and A.H. Plaas Studies on the hyaluronate binding properties of newly synthesized proteoglycans purified from articular chondrocyte cultures Arch. Biochem. Biophys. 271 1989 300 314
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 300-314
    • Sandy, J.D.1    Plaas, A.H.2
  • 47
    • 0034671485 scopus 로고    scopus 로고
    • Age-related changes in aggrecan glycosylation affect cleavage by aggrecanase
    • M.A. Pratta, M.D. Tortorella, and E.C. Arner Age-related changes in aggrecan glycosylation affect cleavage by aggrecanase J. Biol. Chem. 275 2000 39096 39102
    • (2000) J. Biol. Chem. , vol.275 , pp. 39096-39102
    • Pratta, M.A.1    Tortorella, M.D.2    Arner, E.C.3
  • 48
    • 0033794135 scopus 로고    scopus 로고
    • Truncation of the amino-terminus of the recombinant aggrecan rAgg1mut leads to reduced cleavage at the aggrecanase site. Efficient aggrecanase catabolism may depend on multiple substrate interactions
    • C. Horber, F.H. Buttner, C. Kern, G. Schmiedeknecht, and E. Bartnik Truncation of the amino-terminus of the recombinant aggrecan rAgg1mut leads to reduced cleavage at the aggrecanase site. Efficient aggrecanase catabolism may depend on multiple substrate interactions Matrix Biol. 19 2000 533 543
    • (2000) Matrix Biol. , vol.19 , pp. 533-543
    • Horber, C.1    Buttner, F.H.2    Kern, C.3    Schmiedeknecht, G.4    Bartnik, E.5
  • 49
    • 0033571592 scopus 로고    scopus 로고
    • Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro
    • C.B. Little, C.R. Flannery, C.E. Hughes, J.S. Mort, P.J. Roughley, C. Dent, and B. Caterson Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro Biochem. J. 344 Pt. 1 1999 61 68
    • (1999) Biochem. J. , vol.344 , Issue.1 PART , pp. 61-68
    • Little, C.B.1    Flannery, C.R.2    Hughes, C.E.3    Mort, J.S.4    Roughley, P.J.5    Dent, C.6    Caterson, B.7
  • 50
    • 0036605643 scopus 로고    scopus 로고
    • Aggrecanase-mediated cartilage degradation
    • E.C. Arner Aggrecanase-mediated cartilage degradation Curr. Opin. Pharmacol. 2 2002 322 329
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 322-329
    • Arner, E.C.1
  • 52
    • 1842406549 scopus 로고    scopus 로고
    • Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems
    • C.E. Hughes, F.H. Buttner, B. Eidenmuller, B. Caterson, and E. Bartnik Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems J. Biol. Chem. 272 1997 20269 20274
    • (1997) J. Biol. Chem. , vol.272 , pp. 20269-20274
    • Hughes, C.E.1    Buttner, F.H.2    Eidenmuller, B.3    Caterson, B.4    Bartnik, E.5
  • 53
    • 0038385935 scopus 로고    scopus 로고
    • Identification of the motifs and amino acids in aggrecan G1 and G2 domains involved in product secretion
    • C. Kiani, L. Chen, V. Lee, P.S. Zheng, Y. Wu, J. Wen, L. Cao, M.E. Adams, W. Sheng, and B.B. Yang Identification of the motifs and amino acids in aggrecan G1 and G2 domains involved in product secretion Biochemistry 42 2003 7226 7237
    • (2003) Biochemistry , vol.42 , pp. 7226-7237
    • Kiani, C.1    Chen, L.2    Lee, V.3    Zheng, P.S.4    Wu, Y.5    Wen, J.6    Cao, L.7    Adams, M.E.8    Sheng, W.9    Yang, B.B.10
  • 55
    • 0033621466 scopus 로고    scopus 로고
    • The folded protein modules of the C-terminal G3 domain of aggrecan can each facilitate the translocation and secretion of the extended chondroitin sulfate attachment sequence
    • J.M. Day, A.D. Murdoch, and T.E. Hardingham The folded protein modules of the C-terminal G3 domain of aggrecan can each facilitate the translocation and secretion of the extended chondroitin sulfate attachment sequence J. Biol. Chem. 274 1999 38107 38111
    • (1999) J. Biol. Chem. , vol.274 , pp. 38107-38111
    • Day, J.M.1    Murdoch, A.D.2    Hardingham, T.E.3
  • 57
    • 0036818369 scopus 로고    scopus 로고
    • Biosynthesis of chondroitin/dermatan sulfate
    • J.E. Silbert, and G. Sugumaran Biosynthesis of chondroitin/dermatan sulfate IUBMB Life 54 2002 177 186
    • (2002) IUBMB Life , vol.54 , pp. 177-186
    • Silbert, J.E.1    Sugumaran, G.2
  • 58
    • 0029063917 scopus 로고
    • Glycosaminoglycan addition to proteoglycans by articular chondrocytes-evidence for core protein-specific pathways
    • S. Wong-Palms, and A.H. Plaas Glycosaminoglycan addition to proteoglycans by articular chondrocytes-evidence for core protein-specific pathways Arch. Biochem. Biophys. 319 1995 383 392
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 383-392
    • Wong-Palms, S.1    Plaas, A.H.2
  • 59
    • 0033064917 scopus 로고    scopus 로고
    • Proteoglycan synthesis by bovine keratocytes and corneal fibroblasts: Maintenance of the keratocyte phenotype in culture
    • M.P. Beales, J.L. Funderburgh, J.V. Jester, and J.R. Hassell Proteoglycan synthesis by bovine keratocytes and corneal fibroblasts: maintenance of the keratocyte phenotype in culture Invest. Ophthalmol. Vis. Sci. 40 1999 1658 1663
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 1658-1663
    • Beales, M.P.1    Funderburgh, J.L.2    Jester, J.V.3    Hassell, J.R.4
  • 60
    • 0035941233 scopus 로고    scopus 로고
    • Proteoglycan expression during transforming growth factor beta -induced keratocyte-myofibroblast transdifferentiation
    • J.L. Funderburgh, M.L. Funderburgh, M.M. Mann, L. Corpuz, and M.R. Roth Proteoglycan expression during transforming growth factor beta -induced keratocyte-myofibroblast transdifferentiation J. Biol. Chem. 276 2001 44173 44178
    • (2001) J. Biol. Chem. , vol.276 , pp. 44173-44178
    • Funderburgh, J.L.1    Funderburgh, M.L.2    Mann, M.M.3    Corpuz, L.4    Roth, M.R.5
  • 61
    • 0032533240 scopus 로고    scopus 로고
    • Glycosyltransferase and sulfotransferase activities in chick corneal stromal cells before and after in vitro culture
    • K. Nakazawa, I. Takahashi, and Y. Yamamoto Glycosyltransferase and sulfotransferase activities in chick corneal stromal cells before and after in vitro culture Arch. Biochem. Biophys. 359 1998 269 282
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 269-282
    • Nakazawa, K.1    Takahashi, I.2    Yamamoto, Y.3
  • 62
    • 0022347041 scopus 로고
    • Proteoglycans from bovine nasal and articular cartilages. Fractionation of the link proteins by wheat germ agglutinin affinity chromatography
    • H.U. Choi, L.H. Tang, T.L. Johnson, and L. Rosenberg Proteoglycans from bovine nasal and articular cartilages. Fractionation of the link proteins by wheat germ agglutinin affinity chromatography J. Biol. Chem. 260 1985 13370 13376
    • (1985) J. Biol. Chem. , vol.260 , pp. 13370-13376
    • Choi, H.U.1    Tang, L.H.2    Johnson, T.L.3    Rosenberg, L.4
  • 63
    • 0034213887 scopus 로고    scopus 로고
    • An N-terminal peptide from link protein can stimulate biosynthesis of collagen by human articular cartilage
    • H. Liu, L.A. McKenna, and M.F. Dean An N-terminal peptide from link protein can stimulate biosynthesis of collagen by human articular cartilage Arch. Biochem. Biophys. 378 2000 116 122
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 116-122
    • Liu, H.1    McKenna, L.A.2    Dean, M.F.3
  • 64
    • 0031961969 scopus 로고    scopus 로고
    • An N-terminal peptide from link protein stimulates proteoglycan biosynthesis in human articular cartilage in vitro
    • L.A. McKenna, H. Liu, P.A. Sansom, and M.F. Dean An N-terminal peptide from link protein stimulates proteoglycan biosynthesis in human articular cartilage in vitro Arthritis Rheum. 41 1998 157 162
    • (1998) Arthritis Rheum. , vol.41 , pp. 157-162
    • McKenna, L.A.1    Liu, H.2    Sansom, P.A.3    Dean, M.F.4
  • 65
    • 0019130250 scopus 로고
    • Delayed formation of proteoglycan aggregate structures in human articular cartilage disease states
    • T.R. Oegema Jr. Delayed formation of proteoglycan aggregate structures in human articular cartilage disease states Nature 288 1980 583 585
    • (1980) Nature , vol.288 , pp. 583-585
    • Oegema Jr., T.R.1
  • 66
    • 0021022882 scopus 로고
    • Differences in the rates of aggregation of proteoglycans from human articular cartilage and chondrosarcoma
    • M.T. Bayliss, G.D. Ridgway, and S.Y. Ali Differences in the rates of aggregation of proteoglycans from human articular cartilage and chondrosarcoma Biochem. J. 215 1983 705 708
    • (1983) Biochem. J. , vol.215 , pp. 705-708
    • Bayliss, M.T.1    Ridgway, G.D.2    Ali, S.Y.3
  • 67
    • 0022407815 scopus 로고
    • The role of link protein in mediating the interaction between hyaluronic acid and newly secreted proteoglycan subunits from adult human articular cartilage
    • L.I. Melching, and P.J. Roughley The role of link protein in mediating the interaction between hyaluronic acid and newly secreted proteoglycan subunits from adult human articular cartilage J. Biol. Chem. 260 1985 16279 16285
    • (1985) J. Biol. Chem. , vol.260 , pp. 16279-16285
    • Melching, L.I.1    Roughley, P.J.2
  • 68
    • 2442595171 scopus 로고    scopus 로고
    • Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network
    • P. Wang, M. Tortorella, K. England, A.M. Malfait, G. Thomas, E.C. Arner, and D. Pei Proprotein convertase furin interacts with and cleaves pro-ADAMTS4 (Aggrecanase-1) in the trans-Golgi network J. Biol. Chem. 279 2004 15434 15440
    • (2004) J. Biol. Chem. , vol.279 , pp. 15434-15440
    • Wang, P.1    Tortorella, M.2    England, K.3    Malfait, A.M.4    Thomas, G.5    Arner, E.C.6    Pei, D.7
  • 69
    • 1642354112 scopus 로고    scopus 로고
    • ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1
    • G. Gao, A. Plaas, V.P. Thompson, S. Jin, F. Zuo, and J.D. Sandy ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1 J. Biol. Chem. 279 2004 10042 10051
    • (2004) J. Biol. Chem. , vol.279 , pp. 10042-10051
    • Gao, G.1    Plaas, A.2    Thompson, V.P.3    Jin, S.4    Zuo, F.5    Sandy, J.D.6
  • 70
    • 14944371238 scopus 로고    scopus 로고
    • Analysis of ADAMTS4 and MT4-MMP indicates that both are involved in aggrecanolysis in interleukin-1-treated bovine cartilage
    • P. Patwari, G. Gao, J.H. Lee, A.J. Grodzinsky, and J.D. Sandy Analysis of ADAMTS4 and MT4-MMP indicates that both are involved in aggrecanolysis in interleukin-1-treated bovine cartilage Osteoarthr. Cartil. 13 2005 269 277
    • (2005) Osteoarthr. Cartil. , vol.13 , pp. 269-277
    • Patwari, P.1    Gao, G.2    Lee, J.H.3    Grodzinsky, A.J.4    Sandy, J.D.5
  • 72
    • 0036240838 scopus 로고    scopus 로고
    • Transcriptional regulation of collagenase (MMP-1, MMP-13) genes in arthritis: Integration of complex signaling pathways for the recruitment of gene-specific transcription factors
    • M.P. Vincenti, and C.E. Brinckerhoff Transcriptional regulation of collagenase (MMP-1, MMP-13) genes in arthritis: integration of complex signaling pathways for the recruitment of gene-specific transcription factors Arthritis Res. 4 2002 157 164
    • (2002) Arthritis Res. , vol.4 , pp. 157-164
    • Vincenti, M.P.1    Brinckerhoff, C.E.2
  • 76
    • 0031688163 scopus 로고    scopus 로고
    • Immunolocalization of the cleavage of the aggrecan core protein at the Asn341-Phe342 bond, as an indicator of the location of the metalloproteinases active in the lysis of the rat growth plate
    • E.R. Lee, L. Lamplugh, C.P. Leblond, S. Mordier, M.C. Magny, and J.S. Mort Immunolocalization of the cleavage of the aggrecan core protein at the Asn341-Phe342 bond, as an indicator of the location of the metalloproteinases active in the lysis of the rat growth plate Anat. Rec. 252 1998 117 132
    • (1998) Anat. Rec. , vol.252 , pp. 117-132
    • Lee, E.R.1    Lamplugh, L.2    Leblond, C.P.3    Mordier, S.4    Magny, M.C.5    Mort, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.