메뉴 건너뛰기




Volumn 32, Issue 2, 1997, Pages 141-174

The family of the small leucine-rich proteoglycans: Key regulators of matrix assembly and cellular growth

Author keywords

biglycan; decorin; epiphycan; fibromodulin; keratocan; lumican; osteoadherin; osteog lycin

Indexed keywords

BIGLYCAN; COLLAGEN; COLLAGEN FIBRIL; DECORIN; LEUCINE; MESSENGER RNA; PROTEIN P21; PROTEIN PRECURSOR; PROTEOGLYCAN; SIGNAL PEPTIDE; TRANSFORMING GROWTH FACTOR BETA;

EID: 0030986608     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.3109/10409239709108551     Document Type: Review
Times cited : (465)

References (162)
  • 1
    • 0026739743 scopus 로고
    • cDNA sequence for rat dermatan sulfate proteoglycan-II (decorin)
    • Abramson, S. R. and Woessner, J. F., Jr. 1992. cDNA sequence for rat dermatan sulfate proteoglycan-II (decorin). Biochim. Biophys. Acta 1132: 225-227.
    • (1992) Biochim. Biophys. Acta , vol.1132 , pp. 225-227
    • Abramson, S.R.1    Woessner Jr., J.F.2
  • 2
    • 0025351937 scopus 로고
    • Altered expression of chondroitin sulfate proteoglycan in the stroma of human colon carcinoma. Hypomethylation of PG-40 gene correlates with increased PG-40 content and mRNA levels
    • Adany, R., Heimer, R., Caterson, B., Sorrell, J. M., and Iozzo, R. V. 1990. Altered expression of chondroitin sulfate proteoglycan in the stroma of human colon carcinoma. Hypomethylation of PG-40 gene correlates with increased PG-40 content and mRNA levels. J. Biol. Chem. 265: 11389-11396.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11389-11396
    • Adany, R.1    Heimer, R.2    Caterson, B.3    Sorrell, J.M.4    Iozzo, R.V.5
  • 3
    • 0025761007 scopus 로고
    • Hypomethylation of the decorin proteoglycan gene in human colon cancer
    • Adany, R. and Iozzo, R. V. 1991. Hypomethylation of the decorin proteoglycan gene in human colon cancer. Biochem. J. 276: 301-306.
    • (1991) Biochem. J. , vol.276 , pp. 301-306
    • Adany, R.1    Iozzo, R.V.2
  • 4
    • 0026012416 scopus 로고
    • Posttranslational modifications of fibromodulin
    • Antonsson, P., Heinegård, D., and Oldberg, Å. 1991. Posttranslational modifications of fibromodulin. J. Biol. Chem. 266: 16859-16861.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16859-16861
    • Antonsson, P.1    Heinegård, D.2    Oldberg, Å.3
  • 5
    • 0027240239 scopus 로고
    • Structure and deduced amino acid sequence of the human fibromodulin gene
    • Antonsson, P., Heinegård, D., and Oldberg, Å. 1993. Structure and deduced amino acid sequence of the human fibromodulin gene. Biochim. Biophys. Acta 1174: 204-206.
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 204-206
    • Antonsson, P.1    Heinegård, D.2    Oldberg, Å.3
  • 6
    • 0027082262 scopus 로고
    • Molecular characterization of vascular smooth muscle decorin: Deduced core protein structure and regulation of gene expression
    • Asundi, V. K. and Dreher, K. L. 1992. Molecular characterization of vascular smooth muscle decorin: deduced core protein structure and regulation of gene expression. Eur. J. Cell Biol. 59: 314-321.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 314-321
    • Asundi, V.K.1    Dreher, K.L.2
  • 7
    • 0023834148 scopus 로고
    • Transforming growth factor β regulates the expression and structure of extracellular matrix chondroitin/ dermatan sulfate proteoglycans
    • Bassols, A. and Massagué, J. 1988. Transforming growth factor β regulates the expression and structure of extracellular matrix chondroitin/ dermatan sulfate proteoglycans. J. Biol. Chem. 263: 3039-3045.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3039-3045
    • Bassols, A.1    Massagué, J.2
  • 8
    • 0028892460 scopus 로고
    • The primary structure of a basic leucine-rich repeat protein, PRELP, found in connective tissues
    • Bengtsson, E., Neame, P. J., Heinegård, D., and Sommarin, Y. 1995. The primary structure of a basic leucine-rich repeat protein, PRELP, found in connective tissues. J. Biol. Chem. 270: 25639-25644.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25639-25644
    • Bengtsson, E.1    Neame, P.J.2    Heinegård, D.3    Sommarin, Y.4
  • 9
    • 0025110119 scopus 로고
    • Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues
    • Bianco, P., Fisher, L. W., Young, M. F., Termine, J. D., and Robey, P. G. 1990. Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues. J. Histochem. Cytochem. 38: 1549-1563.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1549-1563
    • Bianco, P.1    Fisher, L.W.2    Young, M.F.3    Termine, J.D.4    Robey, P.G.5
  • 10
    • 0003163502 scopus 로고
    • Biglycan and decorin in intact developing tissues: The in situ approach to their role in development, morphogenesis and tissue organization
    • (Scott, J. E., Ed.) London, Portland Press
    • Bianco, P., Riminucci, M., and Fisher, L. W. 1993. Biglycan and decorin in intact developing tissues: the in situ approach to their role in development, morphogenesis and tissue organization. In: Dermatan Sulphate Proteoglycans, pp. 193-205. (Scott, J. E., Ed.) London, Portland Press.
    • (1993) Dermatan Sulphate Proteoglycans , pp. 193-205
    • Bianco, P.1    Riminucci, M.2    Fisher, L.W.3
  • 12
    • 0030198753 scopus 로고    scopus 로고
    • Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon
    • Birk, D. E., Hahn, R. A., Linsenmayer, C., and Zycband, E. I. 1996. Characterization of collagen fibril segments from chicken embryo cornea, dermis and tendon. Matrix Biol. 15: 111-118.
    • (1996) Matrix Biol. , vol.15 , pp. 111-118
    • Birk, D.E.1    Hahn, R.A.2    Linsenmayer, C.3    Zycband, E.I.4
  • 13
    • 0029852530 scopus 로고    scopus 로고
    • Distinct isoforms of chicken decorin contain either one or two dermatan sulfate chains
    • Blaschke, U. K., Hedbom, E., and Bruckner, P. 1996. Distinct isoforms of chicken decorin contain either one or two dermatan sulfate chains. J. Biol. Chem. 271: 30347-30353.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30347-30353
    • Blaschke, U.K.1    Hedbom, E.2    Bruckner, P.3
  • 14
    • 0026657581 scopus 로고
    • Isolation and partial characterization of lumican and decorin from adult chicken corneas. A keratan sulfate-containing isoform of decorin is developmentally regulated
    • Blochberger, T. C., Cornuet, P. K., and Hassell, J. R. 1992a. Isolation and partial characterization of lumican and decorin from adult chicken corneas. A keratan sulfate-containing isoform of decorin is developmentally regulated. J. Biol. Chem. 267: 20613-20619.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20613-20619
    • Blochberger, T.C.1    Cornuet, P.K.2    Hassell, J.R.3
  • 15
    • 0026558368 scopus 로고
    • cDNA to chick lumican (corneal keratan sulfate proteoglycan) reveals homology to the small interstitial proteoglycan gene family and expression in muscle and intestine
    • Blochberger, T. C., Vergnes, J.-P., Hempel, J., and Hassell, J. R. 1992b. cDNA to chick lumican (corneal keratan sulfate proteoglycan) reveals homology to the small interstitial proteoglycan gene family and expression in muscle and intestine. J. Biol. Chem. 267: 347-352.
    • (1992) J. Biol. Chem. , vol.267 , pp. 347-352
    • Blochberger, T.C.1    Vergnes, J.-P.2    Hempel, J.3    Hassell, J.R.4
  • 17
    • 0025913228 scopus 로고
    • The proteoglycan decorin is synthesized and secreted by differentiated myotubes
    • Brandan, E., Fuentes, M. E., and Andrade, W. 1991. The proteoglycan decorin is synthesized and secreted by differentiated myotubes. Eur. J. Cell Biol. 55: 209-216.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 209-216
    • Brandan, E.1    Fuentes, M.E.2    Andrade, W.3
  • 18
    • 0025285463 scopus 로고
    • Non-uniform influence of transforming growth factor-β on the biosynthesis of different forms of small chondoitin sulfate/dermatan sulphate proteoglycan
    • Breuer, B., Schmidt, G., and Kresse, H. 1990. Non-uniform influence of transforming growth factor-β on the biosynthesis of different forms of small chondoitin sulfate/dermatan sulphate proteoglycan. Biochem. J. 269: 551-554.
    • (1990) Biochem. J. , vol.269 , pp. 551-554
    • Breuer, B.1    Schmidt, G.2    Kresse, H.3
  • 20
    • 0022404219 scopus 로고
    • Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulfate. Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycans
    • Chopra, R. K., Pearson, C. H., Pringle, G. A., Fackre, D. S., and Scott, P. G. 1985. Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulfate. Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycans. Biochem. J. 232: 277-279.
    • (1985) Biochem. J. , vol.232 , pp. 277-279
    • Chopra, R.K.1    Pearson, C.H.2    Pringle, G.A.3    Fackre, D.S.4    Scott, P.G.5
  • 21
    • 0027616598 scopus 로고
    • Preferential gene expression in quiescent human lung fibroblasts
    • Coppock, D. L., Kopman, C., Scandalis, S., and Gilleran, S. 1993. Preferential gene expression in quiescent human lung fibroblasts. Cell Growth Differ. 4: 483-493.
    • (1993) Cell Growth Differ. , vol.4 , pp. 483-493
    • Coppock, D.L.1    Kopman, C.2    Scandalis, S.3    Gilleran, S.4
  • 23
    • 0029887668 scopus 로고    scopus 로고
    • Molecular cloning and tissue distribution of keratocan. Bovine corneal keratan sulfate proteoglycan 37A
    • Corpuz, L. M., Funderburgh, J. L., Funderburgh, M. L., Bottomley, G. S., Prakash, S., and Conrad, G. W. 1996. Molecular cloning and tissue distribution of keratocan. Bovine corneal keratan sulfate proteoglycan 37A. J. Biol. Chem. 271: 9759-9763.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9759-9763
    • Corpuz, L.M.1    Funderburgh, J.L.2    Funderburgh, M.L.3    Bottomley, G.S.4    Prakash, S.5    Conrad, G.W.6
  • 24
    • 0003027506 scopus 로고
    • Structure and biology of pericellular proteoglycans
    • (Roberts, D.D. and Mecham, R. P., Eds.) San Diego, Academic Press
    • Couchman, J. R. and Woods, A. 1993. Structure and biology of pericellular proteoglycans. In: Cell Surface and Extracellular Glycoconjugates, PP. 33-81. (Roberts, D.D. and Mecham, R. P., Eds.) San Diego, Academic Press.
    • (1993) Cell Surface and Extracellular Glycoconjugates , pp. 33-81
    • Couchman, J.R.1    Woods, A.2
  • 25
    • 0027407559 scopus 로고
    • The human decorin gene: Intron-exon organization, discovery of two alternatively spliced exons in the 5′ untranslated region, and mapping of the gene to chromosome 12q23
    • Danielson, K. G., Fazzio, A., Cohen, I., Cannizzaro, L. A., Eichstetter, I., and Iozzo, R. V. 1993. The human decorin gene: intron-exon organization, discovery of two alternatively spliced exons in the 5′ untranslated region, and mapping of the gene to chromosome 12q23. Genomics 15: 146-160.
    • (1993) Genomics , vol.15 , pp. 146-160
    • Danielson, K.G.1    Fazzio, A.2    Cohen, I.3    Cannizzaro, L.A.4    Eichstetter, I.5    Iozzo, R.V.6
  • 26
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson, K. G., Baribault, H., Holmes, D. F., Graham, H., Kadler, K. E., and Iozzo, R. V. 1997. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 136: 729-743.
    • (1997) J. Cell Biol. , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 27
    • 0023657291 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for small proteoglycan II of bovine bone
    • Day, A. A., McQuillan, C. I., Termine, J. D., and Young, M. R. 1987. Molecular cloning and sequence analysis of the cDNA for small proteoglycan II of bovine bone. Biochem. J. 248: 801-805.
    • (1987) Biochem. J. , vol.248 , pp. 801-805
    • Day, A.A.1    McQuillan, C.I.2    Termine, J.D.3    Young, M.R.4
  • 28
    • 0029785662 scopus 로고    scopus 로고
    • Decorin-induced growth suppression is associated with upregulation of p21, an inhibitor of cyclin-dependent kinases
    • De Luca, A., Santra, M., Baldi, A., Giordano, A., and Iozzo, R. V. 1996. Decorin-induced growth suppression is associated with upregulation of p21, an inhibitor of cyclin-dependent kinases. J. Biol. Chem. 271: 18961-18965.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18961-18965
    • De Luca, A.1    Santra, M.2    Baldi, A.3    Giordano, A.4    Iozzo, R.V.5
  • 30
    • 0025668865 scopus 로고
    • Vascular smooth muscle biglycan represents a highly conserved proteoglycan within the arterial wall
    • Dreher, K. L., Asundi, V., Matzura, D., and Cowan, K. 1990. Vascular smooth muscle biglycan represents a highly conserved proteoglycan within the arterial wall. Eur. J. Cell Biol. 53: 296-304.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 296-304
    • Dreher, K.L.1    Asundi, V.2    Matzura, D.3    Cowan, K.4
  • 31
    • 0028268324 scopus 로고
    • Decorin and a large dermatan sulfate proteoglycan in bovine striated muscle
    • Eaggen, K. H., Malmström, A., and Kolset, S. O. 1994. Decorin and a large dermatan sulfate proteoglycan in bovine striated muscle. Biochim. Biophys. Acta 1204: 287-297.
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 287-297
    • Eaggen, K.H.1    Malmström, A.2    Kolset, S.O.3
  • 33
    • 0024550294 scopus 로고
    • Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species
    • Fisher, L. W., Termine, J. D., and Young, M. F. 1989. Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species. J. Biol. Chem. 264: 4571-4576.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4571-4576
    • Fisher, L.W.1    Termine, J.D.2    Young, M.F.3
  • 34
    • 0026320793 scopus 로고
    • Human biglycan gene. Putative promoter, intron-exon junctions, and chromosomal localization
    • Fisher, L. W., Heegaard, A.-M., Vetter, U., Vogel, W., Just, W., Termine, J. D., and Young, M. F. 1991. Human biglycan gene. Putative promoter, intron-exon junctions, and chromosomal localization. J. Biol. Chem. 266: 14371-14377.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14371-14377
    • Fisher, L.W.1    Heegaard, A.-M.2    Vetter, U.3    Vogel, W.4    Just, W.5    Termine, J.D.6    Young, M.F.7
  • 36
    • 0030297999 scopus 로고    scopus 로고
    • Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin
    • Font, B., Eichenberger, D., Rosenberg, L. M., and van der Rest, M. 1996. Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin. Matrix Biol. 15: 341-348.
    • (1996) Matrix Biol. , vol.15 , pp. 341-348
    • Font, B.1    Eichenberger, D.2    Rosenberg, L.M.3    Van Der Rest, M.4
  • 37
    • 0027280398 scopus 로고
    • Sequence and structural implications of a bovine corneal keratan sulfate proteoglycan core protein. Protein 37B represents bovine lumican and proteins 37A and 25 are unique
    • Funderburgh, J. L., Funderburgh, M. L., Brown, S. J., Vergnes, J.-P., Hassell, J. R., Mann, M. M., and Conrad, G. W. 1993. Sequence and structural implications of a bovine corneal keratan sulfate proteoglycan core protein. Protein 37B represents bovine lumican and proteins 37A and 25 are unique. J. Biol. Chem. 268: 11874-11880.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11874-11880
    • Funderburgh, J.L.1    Funderburgh, M.L.2    Brown, S.J.3    Vergnes, J.-P.4    Hassell, J.R.5    Mann, M.M.6    Conrad, G.W.7
  • 38
  • 39
    • 0029856498 scopus 로고    scopus 로고
    • Synthesis of corneal keratan sulfate proteoglycans by bovine keratocytes in vitro
    • Funderburgh, J. L., Funderburgh, M. L., Mann, M. M., Prakash, S., and Conrad, G. W. 1996b. Synthesis of corneal keratan sulfate proteoglycans by bovine keratocytes in vitro. J. Biol. Chem. 271: 31431-31436.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31431-31436
    • Funderburgh, J.L.1    Funderburgh, M.L.2    Mann, M.M.3    Prakash, S.4    Conrad, G.W.5
  • 42
    • 0029143935 scopus 로고
    • The human lumican gene. Organization, chromosomal location, and expression in articular cartilage
    • Grover, J., Chen, X.-N., Korenberg, J. R., and Roughley, P. J. 1995. The human lumican gene. Organization, chromosomal location, and expression in articular cartilage. J. Biol. Chem. 270: 21942-21949.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21942-21949
    • Grover, J.1    Chen, X.-N.2    Korenberg, J.R.3    Roughley, P.J.4
  • 43
    • 0030479818 scopus 로고    scopus 로고
    • The gene organization, chromosome location, and expression of a 55-kDa matrix protein (PRELP) of human articular cartilage
    • Grover, J., Chen, X.-N., Korenberg, J. R., Recklies, A. D., and Roughley, P. J. 1996. The gene organization, chromosome location, and expression of a 55-kDa matrix protein (PRELP) of human articular cartilage. Genomics 38: 109-117.
    • (1996) Genomics , vol.38 , pp. 109-117
    • Grover, J.1    Chen, X.-N.2    Korenberg, J.R.3    Recklies, A.D.4    Roughley, P.J.5
  • 44
    • 0026691510 scopus 로고
    • β-D-xyloside alters dermatan sulfate proteoglycan synthesis and the organization of the developing avian corneal stroma
    • Hahn, R. A. and Birk, D. E. 1992. β-D-xyloside alters dermatan sulfate proteoglycan synthesis and the organization of the developing avian corneal stroma. Development 115: 383-393.
    • (1992) Development , vol.115 , pp. 383-393
    • Hahn, R.A.1    Birk, D.E.2
  • 45
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper, J. W., Adami, G. R., Wei, N., Keyomarsi, K., and Elledge, S. J. 1993. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75: 805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 46
    • 0001048849 scopus 로고
    • Stiffness and energy conversation in the molecular dynamics: An improved integrator
    • Harrison, R. W. 1993. Stiffness and energy conversation in the molecular dynamics: an improved integrator. J. Comp. Chem. 14: 1112-1122.
    • (1993) J. Comp. Chem. , vol.14 , pp. 1112-1122
    • Harrison, R.W.1
  • 47
    • 0024533495 scopus 로고
    • Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II
    • Hedbom, E. and Heinegård, D. 1989. Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II. J. Biol. Chem. 264: 6898-6905.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6898-6905
    • Hedbom, E.1    Heinegård, D.2
  • 48
    • 0027717615 scopus 로고
    • Binding of fibromodulin and decorin to separate sites on fibrillar collagens
    • Hedbom, E. and Heinegård, D. 1993. Binding of fibromodulin and decorin to separate sites on fibrillar collagens. J. Biol. Chem. 268: 27307-27312.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27307-27312
    • Hedbom, E.1    Heinegård, D.2
  • 51
    • 0023025001 scopus 로고
    • Two novel matrix proteins isolated from articular cartilage show wide distributions among connective tissues
    • Heinegård, D., Larsson, T., Sommarin, Y., Franzén, A., Paulsson, M., and Hedbom, E. 1986. Two novel matrix proteins isolated from articular cartilage show wide distributions among connective tissues. J. Biol. Chem. 261: 13866-13872.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13866-13872
    • Heinegård, D.1    Larsson, T.2    Sommarin, Y.3    Franzén, A.4    Paulsson, M.5    Hedbom, E.6
  • 52
    • 0023909366 scopus 로고
    • Human recombinant interleukin-1 regulates cellular mRNA levels of dermatan sulfate proteoglycan core protein
    • Heino, J., Kähäri, V., Mauviel, A., and Krusius, T. 1988. Human recombinant interleukin-1 regulates cellular mRNA levels of dermatan sulfate proteoglycan core protein. Biochem. J. 252: 309-312.
    • (1988) Biochem. J. , vol.252 , pp. 309-312
    • Heino, J.1    Kähäri, V.2    Mauviel, A.3    Krusius, T.4
  • 53
    • 0030586874 scopus 로고    scopus 로고
    • Purification and characterization of decorin core protein expressed in Escherichia coli as a maltose-binding protein fusion
    • Hering, T. M., Kollar, J., Huynh, T. D., and Varelas, J. B. 1996. Purification and characterization of decorin core protein expressed in Escherichia coli as a maltose-binding protein fusion. Anal. Biochem. 240: 98-108.
    • (1996) Anal. Biochem. , vol.240 , pp. 98-108
    • Hering, T.M.1    Kollar, J.2    Huynh, T.D.3    Varelas, J.B.4
  • 54
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins, D. G. and Sharp, P. M. 1988. CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73: 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 55
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor β
    • Hildebrand, A., Romaris, M., Rasmussen, L. M., Heinegård, D., Twardzik, D. R., Border, W. A., and Ruoslahti, E. 1994. Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor β. Biochem. J. 302: 527-534.
    • (1994) Biochem. J. , vol.302 , pp. 527-534
    • Hildebrand, A.1    Romaris, M.2    Rasmussen, L.M.3    Heinegård, D.4    Twardzik, D.R.5    Border, W.A.6    Ruoslahti, E.7
  • 56
    • 0029766922 scopus 로고    scopus 로고
    • Eukaryotic expression of recombinant biglycan. Post-translational processing and the importance of secondary structure for biological activity
    • Hocking, A. M., Strugnell, R. A., Ramamurthy, P., and McQuillan, D. J. 1996. Eukaryotic expression of recombinant biglycan. Post-translational processing and the importance of secondary structure for biological activity. J. Biol. Chem. 271: 19571-19577.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19571-19577
    • Hocking, A.M.1    Strugnell, R.A.2    Ramamurthy, P.3    McQuillan, D.J.4
  • 57
    • 0010286212 scopus 로고    scopus 로고
    • The propeptide of biglycan regulates glycosylation of the core protein: Deletion mutagenesis and overexpression in eukaryotic cells
    • Hocking, A. M. and McQuillan, D. J. 1996. The propeptide of biglycan regulates glycosylation of the core protein: deletion mutagenesis and overexpression in eukaryotic cells. Glycobiology 6: 717.
    • (1996) Glycobiology , vol.6 , pp. 717
    • Hocking, A.M.1    McQuillan, D.J.2
  • 58
    • 0028929294 scopus 로고
    • Altered immunohistochemical expression of small proteoglycans in the tumor tissue and stroma of basal cell carcinoma
    • Hunzelmann, N., Schönherr, E., Bonnekoh, B., Hartmann, C., Kresse, H., and Krieg, T. 1995. Altered immunohistochemical expression of small proteoglycans in the tumor tissue and stroma of basal cell carcinoma. J. Invest. Dermatol. 104: 509-513.
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 509-513
    • Hunzelmann, N.1    Schönherr, E.2    Bonnekoh, B.3    Hartmann, C.4    Kresse, H.5    Krieg, T.6
  • 59
    • 0030245726 scopus 로고    scopus 로고
    • Decorin regulates collagenase gene expression in fibroblasts adhering to vitronectin
    • Huttenlocher, A., Werb, Z., Tremble, P., Huhtala, P., Rosenberg, L., and Damsky, C. H. 1996. Decorin regulates collagenase gene expression in fibroblasts adhering to vitronectin. Matrix. Biol. 15: 239-250.
    • (1996) Matrix. Biol. , vol.15 , pp. 239-250
    • Huttenlocher, A.1    Werb, Z.2    Tremble, P.3    Huhtala, P.4    Rosenberg, L.5    Damsky, C.H.6
  • 60
    • 0019944123 scopus 로고
    • Proteoglycan changes in the intercellular matrix of human colon carcinoma
    • Iozzo, R. V., Bolender, R. P., and Wight, T. N. 1982. Proteoglycan changes in the intercellular matrix of human colon carcinoma. Lab. Invest. 47: 124-138.
    • (1982) Lab. Invest. , vol.47 , pp. 124-138
    • Iozzo, R.V.1    Bolender, R.P.2    Wight, T.N.3
  • 61
    • 0021839795 scopus 로고
    • Neoplastic modulation of extracellular matrix. Colon carcinoma cells release polypeptides that alter proteoglycan metabolism in colon fibroblasts
    • Iozzo, R. V. 1985. Neoplastic modulation of extracellular matrix. Colon carcinoma cells release polypeptides that alter proteoglycan metabolism in colon fibroblasts. J. Biol. Chem. 260: 7464-7473.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7464-7473
    • Iozzo, R.V.1
  • 62
    • 0023988249 scopus 로고
    • Proteoglycans and neoplasia
    • Iozzo, R. V. 1988. Proteoglycans and neoplasia. Cancer Metast. Rev. 7: 39-50.
    • (1988) Cancer Metast. Rev. , vol.7 , pp. 39-50
    • Iozzo, R.V.1
  • 63
    • 0029353166 scopus 로고
    • Tumor stroma as a regulator of neoplastic behavior
    • Iozzo, R. V. 1995. Tumor stroma as a regulator of neoplastic behavior. Lab. Invest. 73: 157-160.
    • (1995) Lab. Invest. , vol.73 , pp. 157-160
    • Iozzo, R.V.1
  • 64
    • 0027243231 scopus 로고
    • Altered proteoglycan gene expression and the tumor stroma
    • Iozzo, R. V. and Cohen, I. 1993. Altered proteoglycan gene expression and the tumor stroma. Experientia 49: 447-455.
    • (1993) Experientia , vol.49 , pp. 447-455
    • Iozzo, R.V.1    Cohen, I.2
  • 65
    • 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, R. V. and Murdoch, A. D. 1996. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 10: 598-614.
    • (1996) FASEB J. , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 66
    • 0029905441 scopus 로고    scopus 로고
    • Gene therapy by skeletal muscle expresion of decorin prevents fibrotic disease in rat kidney
    • Isaka, Y., Brees, D. K., Ikegaya, K., Kaneda, Y., Imai, E., Noble, N. A., and Border, W. A. 1996. Gene therapy by skeletal muscle expresion of decorin prevents fibrotic disease in rat kidney. Nature Med. 2: 418-423.
    • (1996) Nature Med. , vol.2 , pp. 418-423
    • Isaka, Y.1    Brees, D.K.2    Ikegaya, K.3    Kaneda, Y.4    Imai, E.5    Noble, N.A.6    Border, W.A.7
  • 67
    • 0026352781 scopus 로고
    • Differential expression of small chondroitin/dermatan sulfate proteoglycans, PG-I/biglycan and PG-II/ decorin, by vascular smooth muscle and endothelial cells in culture
    • Järveläinen, H. T., Kinsella, M. G., Wight, T. N., and Sandell, L. J. 1991. Differential expression of small chondroitin/dermatan sulfate proteoglycans, PG-I/biglycan and PG-II/ decorin, by vascular smooth muscle and endothelial cells in culture. J. Biol. Chem. 266: 23274-23281.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23274-23281
    • Järveläinen, H.T.1    Kinsella, M.G.2    Wight, T.N.3    Sandell, L.J.4
  • 70
    • 0027275296 scopus 로고
    • Identification and characterization of glycanated and non-glycanated forms of biglycan and decorin in the human intervertebral disc
    • Johnstone, B., Markopoulos, M., Neame, P., and Caterson, B. 1993. Identification and characterization of glycanated and non-glycanated forms of biglycan and decorin in the human intervertebral disc. Biochem. J. 292: 661-666.
    • (1993) Biochem. J. , vol.292 , pp. 661-666
    • Johnstone, B.1    Markopoulos, M.2    Neame, P.3    Caterson, B.4
  • 73
    • 0025834976 scopus 로고
    • Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-β-1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fiborblasts in culture
    • Kähäri, V.-M., Larjava, H., and Uitto, J. 1991. Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-β-1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fiborblasts in culture. J. Biol. Chem. 266: 10608-10615.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10608-10615
    • Kähäri, V.-M.1    Larjava, H.2    Uitto, J.3
  • 74
    • 0028930779 scopus 로고
    • Differential regulation of decorin and biglycan gene expression by dexamethasone and retinoic acid in cultured human skin fibroblasts
    • Kähäri, V.M., Hakkinen, L., Westermarck, J., and Larjava, H. 1995. Differential regulation of decorin and biglycan gene expression by dexamethasone and retinoic acid in cultured human skin fibroblasts. J. Invest. Dermatol. 104: 503-508.
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 503-508
    • Kähäri, V.M.1    Hakkinen, L.2    Westermarck, J.3    Larjava, H.4
  • 75
    • 0031031465 scopus 로고    scopus 로고
    • Selective expression and processing of biglycan during migration of bovine aortic endothelial cells. The role of endogenous basic fibroblast growth factor
    • Kinsella, M. G., Tsoi, C. K., Järveläinen, H. T., and Wight, T. N. 1997. Selective expression and processing of biglycan during migration of bovine aortic endothelial cells. The role of endogenous basic fibroblast growth factor. J. Biol. Chem. 272: 318-325.
    • (1997) J. Biol. Chem. , vol.272 , pp. 318-325
    • Kinsella, M.G.1    Tsoi, C.K.2    Järveläinen, H.T.3    Wight, T.N.4
  • 76
    • 0025246676 scopus 로고
    • The macrophage and B cell-specific transcription factor PU. 1 is related to the ets oncogene
    • Klemsz, M. J., McKercher, S. R., Celada, A., Van Beveren, C., and Maki, R. A. 1990. The macrophage and B cell-specific transcription factor PU. 1 is related to the ets oncogene. Cell 61: 113-124.
    • (1990) Cell , vol.61 , pp. 113-124
    • Klemsz, M.J.1    McKercher, S.R.2    Celada, A.3    Van Beveren, C.4    Maki, R.A.5
  • 77
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe, B. and Deisenhofer, J. 1993. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature (London) 366: 751-756.
    • (1993) Nature (London) , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 78
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe, B. and Deisenhofer, J. 1994. The leucine-rich repeat: a versatile binding motif. Trends Biochem. Sci. 19: 415-421.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 79
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe, B. and Deisenhofer, J. 1995. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature (London) 374: 183-186.
    • (1995) Nature (London) , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 81
  • 82
    • 0026463907 scopus 로고
    • The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex
    • Krumdieck, R., Höök, M., Rosenberg, L.C., and Volanakis, J.E. 1992. The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex. J. Immunol. 149: 3695-3701.
    • (1992) J. Immunol. , vol.149 , pp. 3695-3701
    • Krumdieck, R.1    Höök, M.2    Rosenberg, L.C.3    Volanakis, J.E.4
  • 83
    • 0342465598 scopus 로고
    • Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA
    • Krusius, T. and Ruoslahti. E. 1986. Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA. Proc. Natl. Acad. Sci. U.S.A. 83: 7683-7687.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 7683-7687
    • Krusius, T.1    Ruoslahti, E.2
  • 84
    • 0029777337 scopus 로고    scopus 로고
    • Occurrence of PG-Lb, a leucine-rich small chondroitin/dermatan sulphate proteoglycan in mammalian epiphyseal cartilage: Moleclar cloning and sequence analysis of the mouse cDNA
    • Kurita, K., Shinomura, T., Ujita, M., Zako, M., Kida, D., Iwata, H., and Kimata, K. 1996. Occurrence of PG-Lb, a leucine-rich small chondroitin/dermatan sulphate proteoglycan in mammalian epiphyseal cartilage: moleclar cloning and sequence analysis of the mouse cDNA. Biochem. J. 318: 909-914.
    • (1996) Biochem. J. , vol.318 , pp. 909-914
    • Kurita, K.1    Shinomura, T.2    Ujita, M.3    Zako, M.4    Kida, D.5    Iwata, H.6    Kimata, K.7
  • 85
    • 0028102459 scopus 로고
    • Structure of the keratan sulphate chains attached to fibromodulin isolated from bovine tracheal cartilage. Oligosaccharides generated by keratanase digestion
    • Lauder, R. M., Huckerby, T. N., and Nieduszynski, I. A. 1994. Structure of the keratan sulphate chains attached to fibromodulin isolated from bovine tracheal cartilage. Oligosaccharides generated by keratanase digestion. Biochem. J. 302: 417-423.
    • (1994) Biochem. J. , vol.302 , pp. 417-423
    • Lauder, R.M.1    Huckerby, T.N.2    Nieduszynski, I.A.3
  • 86
    • 0026326492 scopus 로고
    • Generation of a monoclonal antibody against avian small dermatan sulfate proteoglycan: Immunolocalization and tissue distribution of PG-II (decorin) in embryonic tissues
    • Lennon, D. P., Carrino, D. A., Baber, M. A., and Caplan, A.I. 1991. Generation of a monoclonal antibody against avian small dermatan sulfate proteoglycan: immunolocalization and tissue distribution of PG-II (decorin) in embryonic tissues. Matrix 11: 412-427.
    • (1991) Matrix , vol.11 , pp. 412-427
    • Lennon, D.P.1    Carrino, D.A.2    Baber, M.A.3    Caplan, A.I.4
  • 87
    • 0026663405 scopus 로고
    • cDNA clone to chick corneal chondroitin/dermatan sulfate proteoglycan reveals identity to decorin
    • Li, W., Vergnes, J.-P., Cornuet, P. K., and Hassell, J. R. 1992. cDNA clone to chick corneal chondroitin/dermatan sulfate proteoglycan reveals identity to decorin. Arch. Biochem. Biophys. 296: 190-197.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 190-197
    • Li, W.1    Vergnes, J.-P.2    Cornuet, P.K.3    Hassell, J.R.4
  • 88
    • 0028073482 scopus 로고
    • The self-association of biglycan from bovine articular cartilage
    • Liu, J., Laue, T. M., Choi, H. U., Tang, L. H., and Rosenberg, L. 1994. The self-association of biglycan from bovine articular cartilage. J. Biol. Chem. 269: 28366-28373.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28366-28373
    • Liu, J.1    Laue, T.M.2    Choi, H.U.3    Tang, L.H.4    Rosenberg, L.5
  • 90
    • 0025262156 scopus 로고
    • Analysis of glycosaminoglycan substitution in decorin by site-directed mutagenesis
    • Mann, D. M., Yamaguchi, Y., Bourdon, M. A., and Ruoslahti, E. 1990. Analysis of glycosaminoglycan substitution in decorin by site-directed mutagenesis. J. Biol. Chem. 265: 5317-5323.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5317-5323
    • Mann, D.M.1    Yamaguchi, Y.2    Bourdon, M.A.3    Ruoslahti, E.4
  • 91
    • 0025913019 scopus 로고
    • The amino-terminal region of a proteochondroitin core protein, secreted by aortic smooth muscle cells, shares sequence homology with the prepropeptide region of the biglycan core prootein from human bone
    • Marcum, J. A. and Thompson, M. A. 1991. The amino-terminal region of a proteochondroitin core protein, secreted by aortic smooth muscle cells, shares sequence homology with the prepropeptide region of the biglycan core prootein from human bone. Biochem. Biophys. Res. Commun. 175: 706-712.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 706-712
    • Marcum, J.A.1    Thompson, M.A.2
  • 92
    • 0029056591 scopus 로고
    • Transcriptional regulation of decorin gene expression. Induction by quiescence and repression by tumor necrosis factor-α
    • Mauviel, A., Santra, M., Chen, Y. Q., Uitto, J., and Iozzo, R. V. 1995. Transcriptional regulation of decorin gene expression. Induction by quiescence and repression by tumor necrosis factor-α. J. Biol. Chem. 270: 11692-11700.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11692-11700
    • Mauviel, A.1    Santra, M.2    Chen, Y.Q.3    Uitto, J.4    Iozzo, R.V.5
  • 93
    • 0029780703 scopus 로고    scopus 로고
    • Identification of a bimodal regulatory element encompassing a canonical AP-1 binding site in the proximal promoter region of the human decorin gene
    • Mauviel, A., Korang, K., Santra, M., Tewari, D., Uitto, J., and Iozzo, R. V. 1996. Identification of a bimodal regulatory element encompassing a canonical AP-1 binding site in the proximal promoter region of the human decorin gene. J. Biol. Chem. 271: 24824-24829.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24824-24829
    • Mauviel, A.1    Korang, K.2    Santra, M.3    Tewari, D.4    Uitto, J.5    Iozzo, R.V.6
  • 95
    • 0024406744 scopus 로고
    • The primary structure of the core protein of the small, leucine-rich proteoglycan (PG I) from bovine articular cartilage
    • Neame, P.J., Choi, H.U., and Rosenberg, L.C. 1989. The primary structure of the core protein of the small, leucine-rich proteoglycan (PG I) from bovine articular cartilage. J. Biol. Chem. 264: 8653-8661.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8653-8661
    • Neame, P.J.1    Choi, H.U.2    Rosenberg, L.C.3
  • 96
    • 0028342664 scopus 로고
    • Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen
    • Noda, A., Ning, Y., Venable, S.F., Pereira-Smith, O.M., and Smith, J.R. 1994. Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. Exp. Cell Res. 211: 90-98.
    • (1994) Exp. Cell Res. , vol.211 , pp. 90-98
    • Noda, A.1    Ning, Y.2    Venable, S.F.3    Pereira-Smith, O.M.4    Smith, J.R.5
  • 97
    • 0024461441 scopus 로고
    • A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin)
    • Oldberg, Å., Antonsson, P., Lindblom, K., and Heinegård, D. 1989. A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin). EMBO J. 8: 2601-2604.
    • (1989) EMBO J. , vol.8 , pp. 2601-2604
    • Oldberg, Å.1    Antonsson, P.2    Lindblom, K.3    Heinegård, D.4
  • 98
    • 0029863286 scopus 로고    scopus 로고
    • Amino-terminal deletions in the decorin core protein leads to the biosynthesis of proteoglycans with shorter glycosaminoglycan chains
    • Oldberg, Å., Antonsson, P., Moses, J., and Fransson, L.-Å. 1996. Amino-terminal deletions in the decorin core protein leads to the biosynthesis of proteoglycans with shorter glycosaminoglycan chains. FEBS Lett. 386: 2932.
    • (1996) FEBS Lett. , vol.386 , pp. 2932
    • Oldberg, Å.1    Antonsson, P.2    Moses, J.3    Fransson, L.-Å.4
  • 99
    • 0029739948 scopus 로고    scopus 로고
    • Identification of stromal cell products that interact with pre-B cells
    • Oritani, K. and Kincade, P. W. 1996. Identification of stromal cell products that interact with pre-B cells. J. Cell Biol. 134: 771-781.
    • (1996) J. Cell Biol. , vol.134 , pp. 771-781
    • Oritani, K.1    Kincade, P.W.2
  • 100
    • 0023576317 scopus 로고
    • Detecting homology of distantly related proteins with consensus sequences
    • Patthy, L. 1987. Detecting homology of distantly related proteins with consensus sequences. J. Mol. Biol. 198: 567-577.
    • (1987) J. Mol. Biol. , vol.198 , pp. 567-577
    • Patthy, L.1
  • 101
    • 0026493914 scopus 로고
    • Differential regulation of biglycan and decorin by retinoic acid in bovine chondrocytes
    • Pearson, D. and Sasse, J. 1992. Differential regulation of biglycan and decorin by retinoic acid in bovine chondrocytes. J. Biol. Chem. 267: 25364-25370.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25364-25370
    • Pearson, D.1    Sasse, J.2
  • 102
    • 0003096348 scopus 로고
    • Molecular and aggregate structures of the collagens
    • (Piez, K. A. and Reddi, A. H., Eds.) New York, Elsevier
    • Piez, K. A. 1984. Molecular and aggregate structures of the collagens. In: Extracellular Matrix Biochemistry, pp. 1-39. (Piez, K. A. and Reddi, A. H., Eds.) New York, Elsevier.
    • (1984) Extracellular Matrix Biochemistry , pp. 1-39
    • Piez, K.A.1
  • 103
    • 0025200450 scopus 로고
    • Identification of the keratan sulfate attachment sites on bovine fibromodulin
    • Plaas, A. H. K., Neame, P. J., Nivens, C. M., and Reiss, L. 1990. Identification of the keratan sulfate attachment sites on bovine fibromodulin. J. Biol. Chem. 265: 20634-20640.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20634-20640
    • Plaas, A.H.K.1    Neame, P.J.2    Nivens, C.M.3    Reiss, L.4
  • 104
    • 85007664163 scopus 로고
    • Fibromodulin - A perspective on function
    • Plaas, A. H. K. 1992. Fibromodulin - a perspective on function. Trends Glycosci. Glycotechnol. 4: 445-455.
    • (1992) Trends Glycosci. Glycotechnol. , vol.4 , pp. 445-455
    • Plaas, A.H.K.1
  • 105
    • 0027365038 scopus 로고
    • Biosynthetic mechanisms for the addition of polylactosamine to chondrocyte fibromodulin
    • Plaas, A. H. K. and Wong-Palms, S. 1993. Biosynthetic mechanisms for the addition of polylactosamine to chondrocyte fibromodulin. J. Biol. Chem. 268: 26634-26644.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26634-26644
    • Plaas, A.H.K.1    Wong-Palms, S.2
  • 106
    • 0022479847 scopus 로고
    • Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues
    • Poole, A. R., Webber, C., Pidoux, I., Choi, H., and Rosenberg, L. C. 1986. Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues. J. Histochem. Cytochem. 34: 619-625.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 619-625
    • Poole, A.R.1    Webber, C.2    Pidoux, I.3    Choi, H.4    Rosenberg, L.C.5
  • 107
    • 0025042428 scopus 로고
    • Immuno-electron microscopic localization of the core protein of decorin near the d and e bands of tendon collagen fibrils by use of monoclonal antibodies
    • Pringle, G. A. and Dodd, C.M. 1990. Immuno-electron microscopic localization of the core protein of decorin near the d and e bands of tendon collagen fibrils by use of monoclonal antibodies. J. Histochem. Cytochem. 38: 1405-1411.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1405-1411
    • Pringle, G.A.1    Dodd, C.M.2
  • 108
    • 0029994951 scopus 로고    scopus 로고
    • Proteoglycans contain a 4.6 Å repeat in macular dystrophy corneas: X-ray diffraction evidence
    • Quantock, A. J., Klintworth, G. K., Schanzlin, D. J., Capel, M. S., Lenz, M. E., and Thonar, E. J. A. 1996. Proteoglycans contain a 4.6 Å repeat in macular dystrophy corneas: X-ray diffraction evidence. Biophys. J. 70: 1966-1972.
    • (1996) Biophys. J. , vol.70 , pp. 1966-1972
    • Quantock, A.J.1    Klintworth, G.K.2    Schanzlin, D.J.3    Capel, M.S.4    Lenz, M.E.5    Thonar, E.J.A.6
  • 109
    • 0027154689 scopus 로고
    • Regulation of corneal collagen fibrillogenesis in vitro by corneal keratan sulfate proteoglycan (lumican) and decorin core proteins
    • Rada, J. A., Cornuet, P. K., and Hassell, J. R. 1993. Regulation of corneal collagen fibrillogenesis in vitro by corneal keratan sulfate proteoglycan (lumican) and decorin core proteins. Exp. Eye Res. 56: 635-648.
    • (1993) Exp. Eye Res. , vol.56 , pp. 635-648
    • Rada, J.A.1    Cornuet, P.K.2    Hassell, J.R.3
  • 110
    • 0029776369 scopus 로고    scopus 로고
    • Recombinant decorin glycoforms. Purification and structure
    • Ramamurthy, P., Hocking, A. M., and McQuillan, D. J. 1996. Recombinant decorin glycoforms. Purification and structure. J. Biol. Chem. 271: 19578-19584.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19578-19584
    • Ramamurthy, P.1    Hocking, A.M.2    McQuillan, D.J.3
  • 111
    • 0027525874 scopus 로고
    • Structural properties and partial protein sequence analysis of the major dermatan sulfate proteoglycan of pigeon aorta
    • Register, T. C., Wagner, W. D., Robbins, R. A., and Lively, M. O. 1993. Structural properties and partial protein sequence analysis of the major dermatan sulfate proteoglycan of pigeon aorta. Atherosclerosis 98: 99-111.
    • (1993) Atherosclerosis , vol.98 , pp. 99-111
    • Register, T.C.1    Wagner, W.D.2    Robbins, R.A.3    Lively, M.O.4
  • 112
    • 0025736444 scopus 로고
    • Differential effect of transforming growth factor beta on proteoglycan synthesis in human embryonic lung fibroblasts
    • Romaris, M., Heredia, A., Molist, A., and Bassols, A. 1991. Differential effect of transforming growth factor beta on proteoglycan synthesis in human embryonic lung fibroblasts. Biochim. Biophys. Acta 1093: 229-233.
    • (1991) Biochim. Biophys. Acta , vol.1093 , pp. 229-233
    • Romaris, M.1    Heredia, A.2    Molist, A.3    Bassols, A.4
  • 113
    • 0028220220 scopus 로고
    • Changes in the expression of decorin and biglycan in human articular cartilage with age and regulation by TGF-β
    • Roughley, P. J., Melching, L. I., and Recklies, A. D. 1994. Changes in the expression of decorin and biglycan in human articular cartilage with age and regulation by TGF-β. Matrix Biol. 14: 51-59.
    • (1994) Matrix Biol. , vol.14 , pp. 51-59
    • Roughley, P.J.1    Melching, L.I.2    Recklies, A.D.3
  • 114
    • 0029767946 scopus 로고    scopus 로고
    • Changes with age in the structure of fibromodulin in human articular cartilage
    • Roughley, P. J., White, R .J., Csszabo, G., and Mort, J. S. 1996a. Changes with age in the structure of fibromodulin in human articular cartilage. Osteoarthitis Cartilage 4: 153-161.
    • (1996) Osteoarthitis Cartilage , vol.4 , pp. 153-161
    • Roughley, P.J.1    White, R.J.2    Csszabo, G.3    Mort, J.S.4
  • 115
    • 0029759338 scopus 로고    scopus 로고
    • Presence of pro-forms of decorin and biglycan in human articular cartilage
    • Roughley, P. J., White, R. J., and Mort, J. S. 1996b. Presence of pro-forms of decorin and biglycan in human articular cartilage. Biochem. J. 318: 779-784.
    • (1996) Biochem. J. , vol.318 , pp. 779-784
    • Roughley, P.J.1    White, R.J.2    Mort, J.S.3
  • 116
    • 0024150891 scopus 로고
    • Structure and biology of proteoglycans
    • Ruoslahti, E. 1988. Structure and biology of proteoglycans. Annu. Rev. Cell Biol. 4: 229-255.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 229-255
    • Ruoslahti, E.1
  • 117
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoslahti, E. and Yamaguchi, Y. 1991. Proteoglycans as modulators of growth factor activities. Cell 64: 867-869.
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoslahti, E.1    Yamaguchi, Y.2
  • 118
    • 0023764681 scopus 로고
    • Dermatan sulfate proteoglycan from human articular cartilage
    • Sampaio, L.O., Bayliss, M.T., Hardingham, T. E., and Muir, H. 1988. Dermatan sulfate proteoglycan from human articular cartilage. Biochem. J. 254: 757-764.
    • (1988) Biochem. J. , vol.254 , pp. 757-764
    • Sampaio, L.O.1    Bayliss, M.T.2    Hardingham, T.E.3    Muir, H.4
  • 119
    • 0028032085 scopus 로고
    • Structural and functional characterization of the human decorin gene promoter
    • Santra, M., Danielson, K. G., and Iozzo, R. V. 1994. Structural and functional characterization of the human decorin gene promoter. J. Biol. Chem. 269: 579-587.
    • (1994) J. Biol. Chem. , vol.269 , pp. 579-587
    • Santra, M.1    Danielson, K.G.2    Iozzo, R.V.3
  • 120
    • 0029088680 scopus 로고
    • De novo decorin gene expression suppresses the malignant phenotype in human colon cancer cells
    • Santra, M., Skorski, T., Calabretta, B., Lattime, E.C., and Iozzo, R.V. 1995. De novo decorin gene expression suppresses the malignant phenotype in human colon cancer cells. Proc. Natl. Acad. Sci. U.S.A. 92: 7016-7020.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7016-7020
    • Santra, M.1    Skorski, T.2    Calabretta, B.3    Lattime, E.C.4    Iozzo, R.V.5
  • 121
    • 0025813274 scopus 로고
    • Biosynthesis of small proteoglycan II (decorin) by chondrocytes and evidence for a procore protein
    • Sawhney, R. S., Hering, T. M., and Sandell, L. J. 1991. Biosynthesis of small proteoglycan II (decorin) by chondrocytes and evidence for a procore protein. J. Biol. Chem. 266: 9231-9240.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9231-9240
    • Sawhney, R.S.1    Hering, T.M.2    Sandell, L.J.3
  • 122
    • 0025954786 scopus 로고
    • Interaction of the small proteoglycan decorin with fibronectin. Involvement of the sequence NKISK of the core protein
    • Schmidt, G., Hausser, H., and Kresse, H. 1991. Interaction of the small proteoglycan decorin with fibronectin. Involvement of the sequence NKISK of the core protein. Biochem. J. 280: 411-414.
    • (1991) Biochem. J. , vol.280 , pp. 411-414
    • Schmidt, G.1    Hausser, H.2    Kresse, H.3
  • 123
    • 0028090059 scopus 로고
    • The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment and expression during organogenesis and tissue differentiation
    • Scholzen, T., Solursh, M., Suzuki, S., Reiter, R., Morgan, J. L., Buchberg, A. M., Siracusa, L. D., and Iozzo, R. V. 1994. The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment and expression during organogenesis and tissue differentiation. J. Biol. Chem. 269: 28270-28281.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28270-28281
    • Scholzen, T.1    Solursh, M.2    Suzuki, S.3    Reiter, R.4    Morgan, J.L.5    Buchberg, A.M.6    Siracusa, L.D.7    Iozzo, R.V.8
  • 124
    • 0028915521 scopus 로고
    • Decorin-type I collagen interaction. Presence of separate core protein-binding domains
    • Schönherr, E., Hausser, H., Beavan, L., and Kresse, H. 1995. Decorin-type I collagen interaction. Presence of separate core protein-binding domains. J. Biol. Chem. 270: 8877-8883.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8877-8883
    • Schönherr, E.1    Hausser, H.2    Beavan, L.3    Kresse, H.4
  • 125
    • 0019312016 scopus 로고
    • Collagen-proteoglycan interactions. Localization of proteoglycans in tendon by electron microscopy
    • Scott, J. E. 1980. Collagen-proteoglycan interactions. Localization of proteoglycans in tendon by electron microscopy. Biochem. J. 187: 887-891.
    • (1980) Biochem. J. , vol.187 , pp. 887-891
    • Scott, J.E.1
  • 126
    • 0028845761 scopus 로고
    • Extracellular matrix, supramolecular organisation and shape
    • Scott, J. E. 1995. Extracellular matrix, supramolecular organisation and shape. J. Anat. 187: 259-269.
    • (1995) J. Anat. , vol.187 , pp. 259-269
    • Scott, J.E.1
  • 127
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen
    • Scott, J. E. 1996. Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry 35: 8795-8799.
    • (1996) Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 128
    • 0019490438 scopus 로고
    • Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region
    • Scott, J. E. and Orford, C. R. 1981. Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region. Biochem. J. 197: 213-216.
    • (1981) Biochem. J. , vol.197 , pp. 213-216
    • Scott, J.E.1    Orford, C.R.2
  • 129
    • 0022491847 scopus 로고
    • A role for disulphide bridges in the protein core in the interaction of proteodermatan sulphate and collagen
    • Scott, P. G., Winterbottom, N., Dodd, C. M., Edwards, E., and Pearson, C. H. 1986. A role for disulphide bridges in the protein core in the interaction of proteodermatan sulphate and collagen. Biochem. Biophys. Res. Commun. 138: 1348-1354.
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 1348-1354
    • Scott, P.G.1    Winterbottom, N.2    Dodd, C.M.3    Edwards, E.4    Pearson, C.H.5
  • 130
    • 0001466363 scopus 로고
    • Structures of the protein cores of the small dermatan sulphate proteoglycans
    • (Scott, J. E., Ed.) London, Portland Press
    • Scott, P. G. 1993. Structures of the protein cores of the small dermatan sulphate proteoglycans. In: Dermalem Sulphate Proteoglycans, pp. 81-101. (Scott, J. E., Ed.) London, Portland Press.
    • (1993) Dermalem Sulphate Proteoglycans , pp. 81-101
    • Scott, P.G.1
  • 131
    • 0027159325 scopus 로고
    • Mapping the locations of the epitopes of five monoclonal antibodies to the core protein of dermatan sulfate proteoglycan II (decorin)
    • Scott, P. G., Dodd, C. M., and Pringle, G. A. 1993. Mapping the locations of the epitopes of five monoclonal antibodies to the core protein of dermatan sulfate proteoglycan II (decorin). J. Biol. Chem. 268: 11558-11564.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11558-11564
    • Scott, P.G.1    Dodd, C.M.2    Pringle, G.A.3
  • 132
    • 0026593299 scopus 로고
    • Proteoglycan-Lb, a small dermatan sulfate proteoglycan expressed in embryonic chick epiphyseal cartilage, is structurally related to osteoinductive factor
    • Shinomura, T. and Kimata, K. 1992. Proteoglycan-Lb, a small dermatan sulfate proteoglycan expressed in embryonic chick epiphyseal cartilage, is structurally related to osteoinductive factor. J. Biol. Chem. 267: 1265-1270.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1265-1270
    • Shinomura, T.1    Kimata, K.2
  • 133
    • 0029598740 scopus 로고
    • Intracellular membranes in the synthesis, transport, and metabolism of proteoglycans
    • Silbert, J. E. and Sugumaran, G. 1995. Intracellular membranes in the synthesis, transport, and metabolism of proteoglycans. Biochim. Biophys. Acta 1241: 371-384.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 371-384
    • Silbert, J.E.1    Sugumaran, G.2
  • 134
    • 0024330489 scopus 로고
    • Bovine pericardial proteoglycan: Biochemical, immunochemical and ultrastructural studies
    • Simionescu, D., Iozzo, R.V., and Kefalides, N. A. 1989. Bovine pericardial proteoglycan: biochemical, immunochemical and ultrastructural studies. Matrix 9: 301-310.
    • (1989) Matrix , vol.9 , pp. 301-310
    • Simionescu, D.1    Iozzo, R.V.2    Kefalides, N.A.3
  • 136
    • 0029098129 scopus 로고
    • Decorin binding sites for collagen type I are mainly located in leucine rich repeats 4-5
    • Svensson, L., Heinegård, D., and Oldberg, Å. 1995. Decorin binding sites for collagen type I are mainly located in leucine rich repeats 4-5. J. Biol. Chem. 270: 20712-20716.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20712-20716
    • Svensson, L.1    Heinegård, D.2    Oldberg, Å.3
  • 137
    • 0027301574 scopus 로고
    • Keratan sulfate and dermatan sulfate proteoglycans associate with type VI collagen in fetal rabbit cornea
    • Takahashi, T., Cho, H.-I., Kublin, C. I., and Cintron, C. 1993. Keratan sulfate and dermatan sulfate proteoglycans associate with type VI collagen in fetal rabbit cornea. J. Histochem. Cytochem. 41: 1447-1457.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1447-1457
    • Takahashi, T.1    Cho, H.-I.2    Kublin, C.I.3    Cintron, C.4
  • 138
    • 0028600614 scopus 로고
    • Bone matrix decorin binds transforming growth factor-β and enhances its bioactivity
    • Takeuchi, Y., Kodama, Y., and Matsumoto, T. 1994. Bone matrix decorin binds transforming growth factor-β and enhances its bioactivity. J. Biol. Chem. 269: 32634-32638.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32634-32638
    • Takeuchi, Y.1    Kodama, Y.2    Matsumoto, T.3
  • 139
    • 0029034178 scopus 로고
    • Expression of collagens and decorin during aortic arch artery development: Implications for matrix pattern formation
    • Thieszen, S. L. and Rosenquist, T.H. 1994. Expression of collagens and decorin during aortic arch artery development: implications for matrix pattern formation. Matrix Biol. 14:573-582.
    • (1994) Matrix Biol. , vol.14 , pp. 573-582
    • Thieszen, S.L.1    Rosenquist, T.H.2
  • 140
    • 0014697087 scopus 로고
    • Solubility of collagen fibrils formed in vitro in the presence of sulphated acid mucopolysaccharide-protein
    • Toole, B. P. 1969. Solubility of collagen fibrils formed in vitro in the presence of sulphated acid mucopolysaccharide-protein. Nature (London) 222: 872-873.
    • (1969) Nature (London) , vol.222 , pp. 872-873
    • Toole, B.P.1
  • 141
    • 0014342487 scopus 로고
    • The effect of chondroitin sulphate-protein in the formation of collagen fibrils in vitro
    • Toole, B. P. and Lowther, D. A. 1968a. The effect of chondroitin sulphate-protein in the formation of collagen fibrils in vitro. Biochem. J. 109: 857-866.
    • (1968) Biochem. J. , vol.109 , pp. 857-866
    • Toole, B.P.1    Lowther, D.A.2
  • 142
    • 0014370994 scopus 로고
    • Dermatan sulfate-protein: Isolaton from and interaction with collagen
    • Toole, B. P. and Lowther, D. A. 1968b. Dermatan sulfate-protein: isolaton from and interaction with collagen. Arch. Biochem. Biophys. 128: 567-578.
    • (1968) Arch. Biochem. Biophys. , vol.128 , pp. 567-578
    • Toole, B.P.1    Lowther, D.A.2
  • 143
    • 0027221924 scopus 로고
    • cDNA sequence for bovine biglycan (PGI) protein core
    • Torok, M. A., Evans, S. A. S., and Marcum, J. A. 1993. cDNA sequence for bovine biglycan (PGI) protein core. Biochim. Biophys. Acta 1173: 81-84.
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 81-84
    • Torok, M.A.1    Evans, S.A.S.2    Marcum, J.A.3
  • 144
    • 0029030517 scopus 로고
    • Molecular cloning of the mouse osteoglycin-encoding gene
    • Ujita, M., Shinomura, T., and Kimata, K. 1995. Molecular cloning of the mouse osteoglycin-encoding gene. Gene 158: 237-240.
    • (1995) Gene , vol.158 , pp. 237-240
    • Ujita, M.1    Shinomura, T.2    Kimata, K.3
  • 145
    • 0029931625 scopus 로고    scopus 로고
    • Transcriptional regulation of the human biglycan gene
    • Ungefroren, H. and Krull, N. B. 1996. Transcriptional regulation of the human biglycan gene. J. Biol. Chem. 271: 15787-15795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15787-15795
    • Ungefroren, H.1    Krull, N.B.2
  • 146
    • 0021715115 scopus 로고
    • Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon
    • Vogel, K.G., Paulsson, M., and Heinegård, D. 1984. Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem. J. 223: 587-597.
    • (1984) Biochem. J. , vol.223 , pp. 587-597
    • Vogel, K.G.1    Paulsson, M.2    Heinegård, D.3
  • 147
    • 0023667677 scopus 로고
    • Characterization and interactions of a fragment of the core protein of the small proteoglycan (PGII) from bovine tendon
    • Vogel, K. G., Koob, T. J., and Fisher, L. W. 1987. Characterization and interactions of a fragment of the core protein of the small proteoglycan (PGII) from bovine tendon. Biochem. Biophys. Res. Commun. 148: 658-663.
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 658-663
    • Vogel, K.G.1    Koob, T.J.2    Fisher, L.W.3
  • 148
    • 0023019961 scopus 로고
    • Comparisons of antibody reactivity and enzyme sensitivity between small proteoglycans from bovine tendon, bone and cartilage
    • Vogel, K. G. and Fisher, L. W. 1986. Comparisons of antibody reactivity and enzyme sensitivity between small proteoglycans from bovine tendon, bone and cartilage. J. Biol. Chem. 261: 11334-11340.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11334-11340
    • Vogel, K.G.1    Fisher, L.W.2
  • 149
    • 0027054738 scopus 로고
    • The effects of transforming growth factor-beta and serum on proteoglycan synthesis by tendon fibrocartilage
    • Vogel, K. G. and Hernandez, D. J. 1992. The effects of transforming growth factor-beta and serum on proteoglycan synthesis by tendon fibrocartilage. Eur. J. Cell Biol. 59: 304-313.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 304-313
    • Vogel, K.G.1    Hernandez, D.J.2
  • 150
    • 0023355097 scopus 로고
    • The effects of proteoglycans on the morphology of collagen fibrils formed in vitro
    • Vogel, K. G. and Trotter, J. A. 1987. The effects of proteoglycans on the morphology of collagen fibrils formed in vitro. Collagen Relat. Res. 7: 105-114.
    • (1987) Collagen Relat. Res. , vol.7 , pp. 105-114
    • Vogel, K.G.1    Trotter, J.A.2
  • 151
    • 0022491904 scopus 로고
    • Immunocytochemical investigation on the distribution of small chondroitin sulfate-dermatan sulfate proteoglycan in the human
    • Voss, B., Glössl, J., Cully, Z., and Kresse, H. 1986. Immunocytochemical investigation on the distribution of small chondroitin sulfate-dermatan sulfate proteoglycan in the human. J. Histochem. Cytochem. 34: 1013-1019.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1013-1019
    • Voss, B.1    Glössl, J.2    Cully, Z.3    Kresse, H.4
  • 152
    • 0029778529 scopus 로고    scopus 로고
    • Model structure of decorin and implications for collagen fibrillogenesis
    • Weber, I. T., Harrison, R. W., and Iozzo, R. V. 1996. Model structure of decorin and implications for collagen fibrillogenesis. J. Biol. Chem. 271: 31767-31770.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31767-31770
    • Weber, I.T.1    Harrison, R.W.2    Iozzo, R.V.3
  • 153
    • 0029003842 scopus 로고
    • Stimulation of sulphated glycosaminoglycan and decorin production in adult dermal fibroblasts by recombinant human interleukin-4
    • Wegrowski, Y., Paltot, V., Gillery, P., Kalis, B., Randoux, A., and Marquart, F. X. 1995a. Stimulation of sulphated glycosaminoglycan and decorin production in adult dermal fibroblasts by recombinant human interleukin-4. Biochem. J. 307: 673-678.
    • (1995) Biochem. J. , vol.307 , pp. 673-678
    • Wegrowski, Y.1    Paltot, V.2    Gillery, P.3    Kalis, B.4    Randoux, A.5    Marquart, F.X.6
  • 154
    • 0028828264 scopus 로고
    • The murine biglycan: Complete cDNA cloning, genomic organization, promoter function and expression
    • Wegrowski, Y., Pillarisetti, J., Danielson, K. G., Suzuki, S., and Iozzo, R. V. 1995b. The murine biglycan: complete cDNA cloning, genomic organization, promoter function and expression. Genomics 30: 8-17.
    • (1995) Genomics , vol.30 , pp. 8-17
    • Wegrowski, Y.1    Pillarisetti, J.2    Danielson, K.G.3    Suzuki, S.4    Iozzo, R.V.5
  • 155
    • 0025793425 scopus 로고
    • The synthesis of a family of structurally related proteoglycans in fibroblasts is differently regulated by TGF-β
    • Westergren-Thorsson, G., Antonsson, P., Malmström, A., Heinegård, D., and Oldberg, Å. 1991. The synthesis of a family of structurally related proteoglycans in fibroblasts is differently regulated by TGF-β. Matrix 11: 177-183.
    • (1991) Matrix , vol.11 , pp. 177-183
    • Westergren-Thorsson, G.1    Antonsson, P.2    Malmström, A.3    Heinegård, D.4    Oldberg, Å.5
  • 156
    • 0027483199 scopus 로고
    • Interaction of heparin cofactor II with biglycan and decorin
    • Whinna, H. C., Choi, H. U., Rosenberg, L. C., and Church, F. C. 1993. Interaction of heparin cofactor II with biglycan and decorin. J. Biol. Chem. 268: 3920-3924.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3920-3924
    • Whinna, H.C.1    Choi, H.U.2    Rosenberg, L.C.3    Church, F.C.4
  • 157
    • 0026940259 scopus 로고
    • The role of proteoglycans in cell adhesion, migration and proliferation
    • Wight, T. N., Kinsella, M. G., and Qwarnström, E. A. 1992. The role of proteoglycans in cell adhesion, migration and proliferation. Curr. Opin. Cell Biol. 4: 793-801.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 793-801
    • Wight, T.N.1    Kinsella, M.G.2    Qwarnström, E.A.3
  • 158
    • 0026473155 scopus 로고
    • Interactions between thrombospondin and the small proteoglycan decorin: Interference with cell attachment
    • Winnemöller, M., Schön, P., Vischer, P., and Kresse, H. 1992. Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment. Eur. J. Cell Biol. 59: 47-55.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 47-55
    • Winnemöller, M.1    Schön, P.2    Vischer, P.3    Kresse, H.4
  • 159
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-β by the proteoglycan decorin
    • Yamaguchi, Y., Mann, D. M., and Ruoslahti, E. 1990. Negative regulation of transforming growth factor-β by the proteoglycan decorin. Nature (London) 346: 281-284.
    • (1990) Nature (London) , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 160
    • 0024290698 scopus 로고
    • Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation
    • Yamaguchi, Y. and Ruoslahti, E. 1988. Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation. Nature (London) 336: 244-246.
    • (1988) Nature (London) , vol.336 , pp. 244-246
    • Yamaguchi, Y.1    Ruoslahti, E.2
  • 161
    • 0029039714 scopus 로고
    • Distribution of biglycan and its propeptide form in rat and bovine aortic tissue
    • Yeo, T. K., Torok, M. A., Kraus, H. L., Evans, S. A., Zhou, Y., and Marcum, J. A. 1995. Distribution of biglycan and its propeptide form in rat and bovine aortic tissue. J. Vasc. Res. 32: 175-182.
    • (1995) J. Vasc. Res. , vol.32 , pp. 175-182
    • Yeo, T.K.1    Torok, M.A.2    Kraus, H.L.3    Evans, S.A.4    Zhou, Y.5    Marcum, J.A.6
  • 162


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.