메뉴 건너뛰기




Volumn 55, Issue , 2016, Pages 7-21

Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions

Author keywords

Angiogenesis; Autophagy; Binding partners; Decorin; Extracellular matrix; Proteoglycan; Tumorigenesis

Indexed keywords

BINDING PROTEIN; DECORIN; ENZYME; GROWTH FACTOR; LIGAND; MEMBRANE PROTEIN; PROTEIN TYROSINE KINASE; PROTEINASE; COLLAGEN; GLYCOSAMINOGLYCAN; PROTEOGLYCAN;

EID: 84992187693     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2016.09.009     Document Type: Review
Times cited : (165)

References (179)
  • 1
    • 0030986608 scopus 로고    scopus 로고
    • The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth
    • [1] Iozzo, R.V., The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth. Crit. Rev. Biochem. Mol. Biol. 32 (1997), 141–174.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 141-174
    • Iozzo, R.V.1
  • 2
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • [2] Iozzo, R.V., Schaefer, L., Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans. FEBS J. 277 (2010), 3864–3875.
    • (2010) FEBS J. , vol.277 , pp. 3864-3875
    • Iozzo, R.V.1    Schaefer, L.2
  • 3
    • 79957605232 scopus 로고    scopus 로고
    • Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
    • [3] Iozzo, R.V., Sanderson, R.D., Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J. Cell. Mol. Med. 15 (2011), 1013–1031.
    • (2011) J. Cell. Mol. Med. , vol.15 , pp. 1013-1031
    • Iozzo, R.V.1    Sanderson, R.D.2
  • 5
    • 84939968330 scopus 로고    scopus 로고
    • Proteoglycan form and function: a comprehensive nomenclature of proteoglycans
    • [5] Iozzo, R.V., Schaefer, L., Proteoglycan form and function: a comprehensive nomenclature of proteoglycans. Matrix Biol. 42 (2015), 11–55.
    • (2015) Matrix Biol. , vol.42 , pp. 11-55
    • Iozzo, R.V.1    Schaefer, L.2
  • 6
    • 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
    • [6] Danielson, K.G., Fazzio, A., Cohen, I., Cannizzaro, L.A., Eichstetter, I., Iozzo, R.V., 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 (1993), 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
  • 8
    • 0141763811 scopus 로고    scopus 로고
    • The role of decorin in collagen fibrillogenesis and skin homeostasis
    • [8] Reed, C.C., Iozzo, R.V., The role of decorin in collagen fibrillogenesis and skin homeostasis. Glycoconj. J. 19 (2002), 249–255.
    • (2002) Glycoconj. J. , vol.19 , pp. 249-255
    • Reed, C.C.1    Iozzo, R.V.2
  • 9
    • 34547796856 scopus 로고    scopus 로고
    • The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis
    • [9] Rühland, C., Schönherr, E., Robenek, H., Hansen, U., Iozzo, R.V., Bruckner, P., et al. The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis. FEBS J. 274 (2007), 4246–4255.
    • (2007) FEBS J. , vol.274 , pp. 4246-4255
    • Rühland, C.1    Schönherr, E.2    Robenek, H.3    Hansen, U.4    Iozzo, R.V.5    Bruckner, P.6
  • 10
    • 3843060124 scopus 로고    scopus 로고
    • Investigating tendon fascicle structure–function relationship in a transgenic age mouse model using multiple regression models
    • [10] Robinson, P.S., Lin, T.W., Jawad, A.F., Iozzo, R.V., Soslowsky, L.J., Investigating tendon fascicle structure–function relationship in a transgenic age mouse model using multiple regression models. Ann. Biomed. Eng. 32 (2004), 924–931.
    • (2004) Ann. Biomed. Eng. , vol.32 , pp. 924-931
    • Robinson, P.S.1    Lin, T.W.2    Jawad, A.F.3    Iozzo, R.V.4    Soslowsky, L.J.5
  • 11
    • 73149102043 scopus 로고    scopus 로고
    • Collagen fibril organization in the pregnant endometrium of decorin-deficient mice
    • [11] Sanches, J.C.T., Jones, C.J.P., Aplin, J.D., Iozzo, R.V., Zorn, T.M.T., Oliveira, S.F., Collagen fibril organization in the pregnant endometrium of decorin-deficient mice. J. Anat. 216 (2010), 144–155.
    • (2010) J. Anat. , vol.216 , pp. 144-155
    • Sanches, J.C.T.1    Jones, C.J.P.2    Aplin, J.D.3    Iozzo, R.V.4    Zorn, T.M.T.5    Oliveira, S.F.6
  • 12
    • 0029778529 scopus 로고    scopus 로고
    • Model structure of decorin and implications for collagen fibrillogenesis
    • [12] Weber, I.T., Harrison, R.W., Iozzo, R.V., Model structure of decorin and implications for collagen fibrillogenesis. J. Biol. Chem. 271 (1996), 31767–31770.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31767-31770
    • Weber, I.T.1    Harrison, R.W.2    Iozzo, R.V.3
  • 13
    • 84901394906 scopus 로고    scopus 로고
    • A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function
    • [13] Nikolovska, K., Renke, J.K., Jungmann, O., Grobe, K., Iozzo, R.V., Zamfir, A.D., et al. A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function. Matrix Biol. 35 (2014), 91–102.
    • (2014) Matrix Biol. , vol.35 , pp. 91-102
    • Nikolovska, K.1    Renke, J.K.2    Jungmann, O.3    Grobe, K.4    Iozzo, R.V.5    Zamfir, A.D.6
  • 14
    • 84901391891 scopus 로고    scopus 로고
    • Interclass small leucine-rich repeat proteoglycan interactions regulate collagen fibrillogenesis and corneal stromal assembly
    • [14] Chen, S., Young, M.F., Chakravarti, S., Birk, D.E., Interclass small leucine-rich repeat proteoglycan interactions regulate collagen fibrillogenesis and corneal stromal assembly. Matrix Biol. 35 (2014), 103–111.
    • (2014) Matrix Biol. , vol.35 , pp. 103-111
    • Chen, S.1    Young, M.F.2    Chakravarti, S.3    Birk, D.E.4
  • 15
    • 84901453190 scopus 로고    scopus 로고
    • Biglycan and decorin differentially regulate signaling in the fetal membranes
    • [15] Wu, Z., Horgan, C.E., Carr, O., Owens, R.T., Iozzo, R.V., Lechner, B.E., Biglycan and decorin differentially regulate signaling in the fetal membranes. Matrix Biol. 35 (2014), 266–275.
    • (2014) Matrix Biol. , vol.35 , pp. 266-275
    • Wu, Z.1    Horgan, C.E.2    Carr, O.3    Owens, R.T.4    Iozzo, R.V.5    Lechner, B.E.6
  • 18
    • 84857485828 scopus 로고    scopus 로고
    • The canonical Wnt pathway shapes niches supportive of hematopoietic stem/progenitor cells
    • [18] Ichii, M., Frank, M.B., Iozzo, R.V., Kincade, P.W., The canonical Wnt pathway shapes niches supportive of hematopoietic stem/progenitor cells. Blood 119 (2012), 1683–1692.
    • (2012) Blood , vol.119 , pp. 1683-1692
    • Ichii, M.1    Frank, M.B.2    Iozzo, R.V.3    Kincade, P.W.4
  • 19
    • 84930181202 scopus 로고    scopus 로고
    • Pivotal role for decorin in angiogenesis
    • [19] Järveläinen, H., Sainio, A., Wight, T.N., Pivotal role for decorin in angiogenesis. Matrix Biol. 43 (2015), 15–26.
    • (2015) Matrix Biol. , vol.43 , pp. 15-26
    • Järveläinen, H.1    Sainio, A.2    Wight, T.N.3
  • 20
    • 84857308088 scopus 로고    scopus 로고
    • Decorin antagonizes the angiogenic network. Concurrent inhibition of Met, hypoxia inducible factor-1α and vascular endothelial growth factor a and induction of thrombospondin-1 and TIMP3
    • [20] Neill, T., Painter, H., Buraschi, S., Owens, R.T., Lisanti, M.P., Schaefer, L., et al. Decorin antagonizes the angiogenic network. Concurrent inhibition of Met, hypoxia inducible factor-1α and vascular endothelial growth factor a and induction of thrombospondin-1 and TIMP3. J. Biol. Chem. 287 (2012), 5492–5506.
    • (2012) J. Biol. Chem. , vol.287 , pp. 5492-5506
    • Neill, T.1    Painter, H.2    Buraschi, S.3    Owens, R.T.4    Lisanti, M.P.5    Schaefer, L.6
  • 22
    • 84877703267 scopus 로고    scopus 로고
    • Biological interplay between proteoglycans and their innate immune receptors in inflammation
    • [22] Frey, T., Schroeder, N., Manon-Jensen, T., Iozzo, R.V., Schaefer, L., Biological interplay between proteoglycans and their innate immune receptors in inflammation. FEBS J. 280 (2013), 2165–2179.
    • (2013) FEBS J. , vol.280 , pp. 2165-2179
    • Frey, T.1    Schroeder, N.2    Manon-Jensen, T.3    Iozzo, R.V.4    Schaefer, L.5
  • 23
    • 84877113971 scopus 로고    scopus 로고
    • Decorin potentiates interferon-gamma activity in a model of allergic inflammation
    • [23] Bocian, C., Urbanowitz, A.K., Owens, R.T., Iozzo, R.V., Gotte, M., Seidler, D.G., Decorin potentiates interferon-gamma activity in a model of allergic inflammation. J. Biol. Chem. 288 (2013), 12699–12711.
    • (2013) J. Biol. Chem. , vol.288 , pp. 12699-12711
    • Bocian, C.1    Urbanowitz, A.K.2    Owens, R.T.3    Iozzo, R.V.4    Gotte, M.5    Seidler, D.G.6
  • 24
    • 84937023699 scopus 로고    scopus 로고
    • Deficiency of decorin induces expression of Foxp3 in CD4(+) CD25(+) T cells in a murine model of allergic asthma
    • [24] Borges, M.C., Narayanan, V., Iozzo, R.V., Ludwig, M.S., Deficiency of decorin induces expression of Foxp3 in CD4(+) CD25(+) T cells in a murine model of allergic asthma. Respirology 20 (2015), 904–911.
    • (2015) Respirology , vol.20 , pp. 904-911
    • Borges, M.C.1    Narayanan, V.2    Iozzo, R.V.3    Ludwig, M.S.4
  • 25
    • 36348995969 scopus 로고    scopus 로고
    • Decorin deficiency enhances progressive nephropathy in diabetic mice
    • [25] Williams, K.J., Qiu, G., Usui, H.K., Dunn, S.R., McCue, P., Bottinger, E., et al. Decorin deficiency enhances progressive nephropathy in diabetic mice. Am. J. Pathol. 171 (2007), 1441–1450.
    • (2007) Am. J. Pathol. , vol.171 , pp. 1441-1450
    • Williams, K.J.1    Qiu, G.2    Usui, H.K.3    Dunn, S.R.4    McCue, P.5    Bottinger, E.6
  • 26
    • 84864796944 scopus 로고    scopus 로고
    • Decorin-TGFβ axis in hepatic fibrosis and cirrhosis
    • [26] Baghy, K., Iozzo, R.V., Kovalszky, I., Decorin-TGFβ axis in hepatic fibrosis and cirrhosis. J. Histochem. Cytochem. 60 (2012), 262–268.
    • (2012) J. Histochem. Cytochem. , vol.60 , pp. 262-268
    • Baghy, K.1    Iozzo, R.V.2    Kovalszky, I.3
  • 28
    • 84947795871 scopus 로고    scopus 로고
    • Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy
    • [28] Gubbiotti, M.A., Neill, T., Frey, H., Schaefer, L., Iozzo, R.V., Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy. Matrix Biol. 48 (2015), 14–25.
    • (2015) Matrix Biol. , vol.48 , pp. 14-25
    • Gubbiotti, M.A.1    Neill, T.2    Frey, H.3    Schaefer, L.4    Iozzo, R.V.5
  • 29
    • 84885664893 scopus 로고    scopus 로고
    • Decorin has an appetite for endothelial cell autophagy
    • [29] Neill, T., Torres, A.T., Buraschi, S., Iozzo, R.V., Decorin has an appetite for endothelial cell autophagy. Autophagy 9 (2013), 1626–1628.
    • (2013) Autophagy , vol.9 , pp. 1626-1628
    • Neill, T.1    Torres, A.T.2    Buraschi, S.3    Iozzo, R.V.4
  • 31
    • 84947728400 scopus 로고    scopus 로고
    • Proteoglycans regulate autophagy via outside-in signaling: an emerging new concept
    • [31] Gubbiotti, M.A., Iozzo, R.V., Proteoglycans regulate autophagy via outside-in signaling: an emerging new concept. Matrix Biol. 48 (2015), 6–13.
    • (2015) Matrix Biol. , vol.48 , pp. 6-13
    • Gubbiotti, M.A.1    Iozzo, R.V.2
  • 32
    • 84894342780 scopus 로고    scopus 로고
    • Decorin activates AMPK, an energy sensor kinase, to induce autophagy in endothelial cells
    • [32] Goyal, A., Neill, T., Owens, R.T., Schaefer, L., Iozzo, R.V., Decorin activates AMPK, an energy sensor kinase, to induce autophagy in endothelial cells. Matrix Biol. 34 (2014), 46–54.
    • (2014) Matrix Biol. , vol.34 , pp. 46-54
    • Goyal, A.1    Neill, T.2    Owens, R.T.3    Schaefer, L.4    Iozzo, R.V.5
  • 33
    • 84860253721 scopus 로고    scopus 로고
    • Small leucine rich proteoglycan family regulates multiple signalling pathways in neural development and maintenance
    • [33] Dellett, M., Hu, W., Papadaki, V., Ohnuma, S., Small leucine rich proteoglycan family regulates multiple signalling pathways in neural development and maintenance. Develop. Growth Differ. 54 (2012), 327–340.
    • (2012) Develop. Growth Differ. , vol.54 , pp. 327-340
    • Dellett, M.1    Hu, W.2    Papadaki, V.3    Ohnuma, S.4
  • 34
    • 78650674666 scopus 로고    scopus 로고
    • Decorin antagonizes met receptor activity and downregulates β-catenin and Myc levels
    • [34] Buraschi, S., Pal, N., Tyler-Rubinstein, N., Owens, R.T., Neill, T., Iozzo, R.V., Decorin antagonizes met receptor activity and downregulates β-catenin and Myc levels. J. Biol. Chem. 285 (2010), 42075–42085.
    • (2010) J. Biol. Chem. , vol.285 , pp. 42075-42085
    • Buraschi, S.1    Pal, N.2    Tyler-Rubinstein, N.3    Owens, R.T.4    Neill, T.5    Iozzo, R.V.6
  • 35
    • 0034693263 scopus 로고    scopus 로고
    • Sustained down-regulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo
    • [35] Csordás, G., Santra, M., Reed, C.C., Eichstetter, I., McQuillan, D.J., Gross, D., et al. Sustained down-regulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo. J. Biol. Chem. 275 (2000), 32879–32887.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32879-32887
    • Csordás, G.1    Santra, M.2    Reed, C.C.3    Eichstetter, I.4    McQuillan, D.J.5    Gross, D.6
  • 37
    • 0033582415 scopus 로고    scopus 로고
    • Decorin is a biological ligand for the epidermal growth factor receptor
    • [37] Iozzo, R.V., Moscatello, D., McQuillan, D.J., Eichstetter, I., Decorin is a biological ligand for the epidermal growth factor receptor. J. Biol. Chem. 274 (1999), 4489–4492.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4489-4492
    • Iozzo, R.V.1    Moscatello, D.2    McQuillan, D.J.3    Eichstetter, I.4
  • 38
    • 37249003185 scopus 로고    scopus 로고
    • Decorin-transforming growth factor-ß interaction regulates matrix organization and mechanical characteristics of three-dimensional collagen matrices
    • [38] Ferdous, Z., Wei, V.M., Iozzo, R.V., Höök, M., Grande-Allen, K.J., Decorin-transforming growth factor-ß interaction regulates matrix organization and mechanical characteristics of three-dimensional collagen matrices. J. Biol. Chem. 282 (2007), 35887–35898.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35887-35898
    • Ferdous, Z.1    Wei, V.M.2    Iozzo, R.V.3    Höök, M.4    Grande-Allen, K.J.5
  • 39
    • 84949870620 scopus 로고    scopus 로고
    • Decorin: a growth factor antagonist for tumor growth inhibition
    • [39] Jarvinen, T.A., Prince, S., Decorin: a growth factor antagonist for tumor growth inhibition. Biomed. Res. Int., 2015, 2015, 654765.
    • (2015) Biomed. Res. Int. , vol.2015 , pp. 654765
    • Jarvinen, T.A.1    Prince, S.2
  • 40
    • 0033732919 scopus 로고    scopus 로고
    • Influence of decorin expression on transforming growth factor-beta-mediated collagen gel retraction and biglycan induction
    • [40] Markmann, A., Hausser, H., Schonherr, E., Kresse, H., Influence of decorin expression on transforming growth factor-beta-mediated collagen gel retraction and biglycan induction. Matrix Biol. 19 (2000), 631–636.
    • (2000) Matrix Biol. , vol.19 , pp. 631-636
    • Markmann, A.1    Hausser, H.2    Schonherr, E.3    Kresse, H.4
  • 41
    • 79959865250 scopus 로고    scopus 로고
    • Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity
    • [41] Vial, C., Gutierrez, J., Santander, C., Cabrera, D., Brandan, E., Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity. J. Biol. Chem. 286 (2011), 24242–24252.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24242-24252
    • Vial, C.1    Gutierrez, J.2    Santander, C.3    Cabrera, D.4    Brandan, E.5
  • 42
    • 84877700624 scopus 로고    scopus 로고
    • Decorin interferes with platelet-derived growth factor receptor signaling in experimental hepatocarcinogenesis
    • [42] Baghy, K., Horváth, Z., Regõs, E., Kiss, K., Schaff, Z., Iozzo, R.V., et al. Decorin interferes with platelet-derived growth factor receptor signaling in experimental hepatocarcinogenesis. FEBS J. 280 (2013), 2150–2164.
    • (2013) FEBS J. , vol.280 , pp. 2150-2164
    • Baghy, K.1    Horváth, Z.2    Regõs, E.3    Kiss, K.4    Schaff, Z.5    Iozzo, R.V.6
  • 45
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen
    • [45] Scott, J.E., Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry 35 (1996), 8795–8799.
    • (1996) Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 46
    • 8144221077 scopus 로고    scopus 로고
    • Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
    • [46] Scott, P.G., McEwan, P.A., Dodd, C.M., Bergmann, E.M., Bishop, P.N., Bella, J., Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 15633–15638.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15633-15638
    • Scott, P.G.1    McEwan, P.A.2    Dodd, C.M.3    Bergmann, E.M.4    Bishop, P.N.5    Bella, J.6
  • 47
    • 0029098129 scopus 로고
    • Decorin binding sites for collagen type I are mainly located in leucine rich repeats 4–5
    • [47] Svensson, L., Heinegård, D., Oldberg, Å., Decorin binding sites for collagen type I are mainly located in leucine rich repeats 4–5. J. Biol. Chem. 270 (1995), 20712–20716.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20712-20716
    • Svensson, L.1    Heinegård, D.2    Oldberg, Å.3
  • 48
    • 79961009000 scopus 로고    scopus 로고
    • Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast
    • [48] Khan, G.A., Girish, G.V., Lala, N., DiGuglielmo, G.M., Lala, P.K., Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast. Mol. Endocrinol. 25 (2011), 1431–1443.
    • (2011) Mol. Endocrinol. , vol.25 , pp. 1431-1443
    • Khan, G.A.1    Girish, G.V.2    Lala, N.3    DiGuglielmo, G.M.4    Lala, P.K.5
  • 49
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping with but distinct from the EGF-binding epitope
    • [49] Santra, M., Reed, C.C., Iozzo, R.V., Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping with but distinct from the EGF-binding epitope. J. Biol. Chem. 277 (2002), 35671–35681.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 50
    • 84890282586 scopus 로고    scopus 로고
    • The concave face of decorin mediates reversible dimerization and collagen binding
    • [50] Islam, M., Gor, J., Perkins, S.J., Ishikawa, Y., Bãchinger, H.S., Hohenester, E., The concave face of decorin mediates reversible dimerization and collagen binding. J. Biol. Chem. 288 (2013), 35526–35533.
    • (2013) J. Biol. Chem. , vol.288 , pp. 35526-35533
    • Islam, M.1    Gor, J.2    Perkins, S.J.3    Ishikawa, Y.4    Bãchinger, H.S.5    Hohenester, E.6
  • 53
    • 81355127411 scopus 로고    scopus 로고
    • A novel mutation of the decorin gene identified in a Korean family with congenial hereditary stromal dystrophy
    • [53] Kim, J.-H., Ko, J.M., Lee, I., Kim, J.Y., Kim, M.J., Tchah, H., A novel mutation of the decorin gene identified in a Korean family with congenial hereditary stromal dystrophy. Cornea 30 (2011), 1473–1477.
    • (2011) Cornea , vol.30 , pp. 1473-1477
    • Kim, J.-H.1    Ko, J.M.2    Lee, I.3    Kim, J.Y.4    Kim, M.J.5    Tchah, H.6
  • 54
    • 33748850603 scopus 로고    scopus 로고
    • A second decorin frame shift mutation in a family with congenital stromal corneal dystrophy
    • [54] Rødahl, E., Van Ginderdeuren, R., Knappskog, P.M., Bredrup, C., Boman, H., A second decorin frame shift mutation in a family with congenital stromal corneal dystrophy. Am. J. Opthalmol. 142 (2006), 520–521.
    • (2006) Am. J. Opthalmol. , vol.142 , pp. 520-521
    • Rødahl, E.1    Van Ginderdeuren, R.2    Knappskog, P.M.3    Bredrup, C.4    Boman, H.5
  • 55
    • 80055005154 scopus 로고    scopus 로고
    • Pathophysiological mechanisms of autosomal dominant congenital stromal corneal dystrophy. C-terminal-truncated decorin results in abnormal matrix assembly and altered expression of small leucine-rich proteoglycans
    • [55] Chen, S., Sun, M., Meng, X., Iozzo, R.V., Kao, W.W.Y., Birk, D.E., Pathophysiological mechanisms of autosomal dominant congenital stromal corneal dystrophy. C-terminal-truncated decorin results in abnormal matrix assembly and altered expression of small leucine-rich proteoglycans. Am. J. Pathol. 179 (2011), 2409–2419.
    • (2011) Am. J. Pathol. , vol.179 , pp. 2409-2419
    • Chen, S.1    Sun, M.2    Meng, X.3    Iozzo, R.V.4    Kao, W.W.Y.5    Birk, D.E.6
  • 56
    • 0025285463 scopus 로고
    • Non-uniform influence of transforming growth factor-β on the biosynthesis of different forms of small chondroitin sulphate/dermatan sulphate proteoglycan
    • [56] Breuer, B., Schmidt, G., Kresse, H., Non-uniform influence of transforming growth factor-β on the biosynthesis of different forms of small chondroitin sulphate/dermatan sulphate proteoglycan. Biochem. J. 269 (1990), 551–554.
    • (1990) Biochem. J. , vol.269 , pp. 551-554
    • Breuer, B.1    Schmidt, G.2    Kresse, H.3
  • 57
    • 84939616757 scopus 로고    scopus 로고
    • Development of congenital stromal corneal dystrophy is dependent on export and extracellular deposition of truncated decorin
    • [57] Mellgren, A.E., Bruland, O., Vedeler, A., Saraste, J., Schonheit, J., Bredrup, C., et al. Development of congenital stromal corneal dystrophy is dependent on export and extracellular deposition of truncated decorin. Invest. Ophthalmol. Vis. Sci. 56 (2015), 2909–2915.
    • (2015) Invest. Ophthalmol. Vis. Sci. , vol.56 , pp. 2909-2915
    • Mellgren, A.E.1    Bruland, O.2    Vedeler, A.3    Saraste, J.4    Schonheit, J.5    Bredrup, C.6
  • 58
    • 84958793759 scopus 로고    scopus 로고
    • Role of decorin core protein in collagen organisation in congenital stromal corneal dystrophy (CSCD)
    • [58] Kamma-Lorger, C.S., Pinali, C., Martinez, J.C., Harris, J., Young, R.D., Bredrup, C., et al. Role of decorin core protein in collagen organisation in congenital stromal corneal dystrophy (CSCD). PLoS One, 11, 2016, e0147948.
    • (2016) PLoS One , vol.11 , pp. e0147948
    • Kamma-Lorger, C.S.1    Pinali, C.2    Martinez, J.C.3    Harris, J.4    Young, R.D.5    Bredrup, C.6
  • 59
    • 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
    • [59] Adany, R., Heimer, R., Caterson, B., Sorrell, J.M., Iozzo, R.V., 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 (1990), 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
  • 60
    • 0024150891 scopus 로고
    • Structure and biology of proteoglycans
    • [60] Ruoslahti, E., Structure and biology of proteoglycans. Annu. Rev. Cell Biol. 4 (1988), 229–255.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 229-255
    • Ruoslahti, E.1
  • 61
    • 0007336718 scopus 로고
    • Dermatan Sulfate Proteoglycans
    • Portland Press London
    • [61] Scott, J.E., Dermatan Sulfate Proteoglycans. 1993, Portland Press, London.
    • (1993)
    • Scott, J.E.1
  • 62
    • 0019490438 scopus 로고
    • Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region
    • [62] Scott, J.E., Orford, C.R., Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region. Biochem. J. 197 (1981), 213–216.
    • (1981) Biochem. J. , vol.197 , pp. 213-216
    • Scott, J.E.1    Orford, C.R.2
  • 63
    • 0032525937 scopus 로고    scopus 로고
    • Structural requirements for fibromodulin binding to collagen and the control of type I collagen fibrillogenesis. Critical roles for disulphide bonding and the C-terminal region
    • [63] Font, B., Eichenberger, D., Goldschmidt, D., Boutillon, M.-M., Hulmes, D.J.S., Structural requirements for fibromodulin binding to collagen and the control of type I collagen fibrillogenesis. Critical roles for disulphide bonding and the C-terminal region. Eur. J. Biochem. 254 (1998), 580–587.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 580-587
    • Font, B.1    Eichenberger, D.2    Goldschmidt, D.3    Boutillon, M.-M.4    Hulmes, D.J.S.5
  • 64
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • [64] Danielson, K.G., Baribault, H., Holmes, D.F., Graham, H., Kadler, K.E., Iozzo, R.V., Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 136 (1997), 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
  • 66
    • 4344595995 scopus 로고    scopus 로고
    • Differential interactions of decorin and decorin mutants with type I and type VI collagens
    • [66] Nareyeck, G., Seidler, D.G., Troyer, D., Rauterberg, J., Krese, H., Schönherr, E., Differential interactions of decorin and decorin mutants with type I and type VI collagens. Eur. J. Biochem. 271 (2004), 3389–3398.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3389-3398
    • Nareyeck, G.1    Seidler, D.G.2    Troyer, D.3    Rauterberg, J.4    Krese, H.5    Schönherr, E.6
  • 68
    • 0030297999 scopus 로고    scopus 로고
    • Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin
    • [68] Font, B., Eichenberger, D., Rosenberg, L.M., der Rest, M.v., Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin. Matrix Biol. 15 (1996), 341–348.
    • (1996) Matrix Biol. , vol.15 , pp. 341-348
    • Font, B.1    Eichenberger, D.2    Rosenberg, L.M.3    der Rest, M.V.4
  • 69
    • 0021715115 scopus 로고
    • Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon
    • [69] Vogel, K.G., Paulsson, M., Heinegård, D., Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem. J. 223 (1984), 587–597.
    • (1984) Biochem. J. , vol.223 , pp. 587-597
    • Vogel, K.G.1    Paulsson, M.2    Heinegård, D.3
  • 70
    • 0029776369 scopus 로고    scopus 로고
    • Recombinant decorin glycoforms. Purification and structure
    • [70] Ramamurthy, P., Hocking, A.M., McQuillan, D.J., Recombinant decorin glycoforms. Purification and structure. J. Biol. Chem. 271 (1996), 19578–19584.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19578-19584
    • Ramamurthy, P.1    Hocking, A.M.2    McQuillan, D.J.3
  • 71
    • 39049160569 scopus 로고    scopus 로고
    • Influence of collagen-fibril-based coatings containing decorin and biglycan on osteoblast behavior
    • [71] Douglas, T., Hempel, U., Mietrach, C., Viola, M., Vigetti, D., Heinemann, S., et al. Influence of collagen-fibril-based coatings containing decorin and biglycan on osteoblast behavior. J. Biomed. Mater. Res. 84A (2008), 805–816.
    • (2008) J. Biomed. Mater. Res. , vol.84A , pp. 805-816
    • Douglas, T.1    Hempel, U.2    Mietrach, C.3    Viola, M.4    Vigetti, D.5    Heinemann, S.6
  • 72
    • 0141621124 scopus 로고    scopus 로고
    • Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan
    • [72] Wiberg, C., Klatt, A.R., Wagener, R., Paulsson, M., Bateman, J.F., Heinegård, D., et al. Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan. J. Biol. Chem. 278 (2003), 37698–37704.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37698-37704
    • Wiberg, C.1    Klatt, A.R.2    Wagener, R.3    Paulsson, M.4    Bateman, J.F.5    Heinegård, D.6
  • 73
    • 26944490699 scopus 로고    scopus 로고
    • Matrilin-3 mutations that cause chondrodysplasias interfere with protein trafficking while a mutation associated with hand osteoarthritis does not
    • [73] Otten, C., Wagener, R., Paulsson, M., Zaucke, F., Matrilin-3 mutations that cause chondrodysplasias interfere with protein trafficking while a mutation associated with hand osteoarthritis does not. J. Med. Genet. 42 (2005), 774–779.
    • (2005) J. Med. Genet. , vol.42 , pp. 774-779
    • Otten, C.1    Wagener, R.2    Paulsson, M.3    Zaucke, F.4
  • 74
    • 84873262892 scopus 로고    scopus 로고
    • Dermatopontin promotes adhesion, spreading and migration of cardiac fibroblasts in vitro
    • [74] Liu, X., Meng, L., Shi, Q., Liu, S., Cui, C., Hu, S., et al. Dermatopontin promotes adhesion, spreading and migration of cardiac fibroblasts in vitro. Matrix Biol. 32 (2013), 23–31.
    • (2013) Matrix Biol. , vol.32 , pp. 23-31
    • Liu, X.1    Meng, L.2    Shi, Q.3    Liu, S.4    Cui, C.5    Hu, S.6
  • 75
    • 18544373396 scopus 로고    scopus 로고
    • Targeted disruption of dermatopontin causes abnormal collagen fibrillogenesis
    • [75] Takeda, U., Utani, A., Wu, J., Adachi, E., Koseki, H., Taniguchi, M., et al. Targeted disruption of dermatopontin causes abnormal collagen fibrillogenesis. J. Invest. Dermatol. 119 (2002), 678–683.
    • (2002) J. Invest. Dermatol. , vol.119 , pp. 678-683
    • Takeda, U.1    Utani, A.2    Wu, J.3    Adachi, E.4    Koseki, H.5    Taniguchi, M.6
  • 76
    • 0030843025 scopus 로고    scopus 로고
    • Tenascin-X deficiency is associated with Ehlers-Danlos syndrome
    • [76] Burch, G.H., Gong, Y., Liu, W., Dettman, R.W., Curry, C.J., Smith, L., et al. Tenascin-X deficiency is associated with Ehlers-Danlos syndrome. Nat. Genet. 17 (1997), 104–108.
    • (1997) Nat. Genet. , vol.17 , pp. 104-108
    • Burch, G.H.1    Gong, Y.2    Liu, W.3    Dettman, R.W.4    Curry, C.J.5    Smith, L.6
  • 79
    • 0034111432 scopus 로고    scopus 로고
    • The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin
    • [79] Trask, B.C., Trask, T.M., Broekelmann, T., Mecham, R.P., The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin. Mol. Biol. Cell 11 (2000), 1499–1507.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1499-1507
    • Trask, B.C.1    Trask, T.M.2    Broekelmann, T.3    Mecham, R.P.4
  • 80
    • 84943665548 scopus 로고    scopus 로고
    • The microfibril-associated glycoproteins (MAGPs) and the microfibrillar niche
    • [80] Mecham, R.P., Gibson, M.A., The microfibril-associated glycoproteins (MAGPs) and the microfibrillar niche. Matrix Biol. 47 (2015), 13–33.
    • (2015) Matrix Biol. , vol.47 , pp. 13-33
    • Mecham, R.P.1    Gibson, M.A.2
  • 81
    • 84943665692 scopus 로고    scopus 로고
    • The fibrillin microfibril scaffold: a niche for growth factors and mechanosensation?
    • [81] Sengle, G., Sakai, L.Y., The fibrillin microfibril scaffold: a niche for growth factors and mechanosensation?. Matrix Biol. 47 (2015), 3–12.
    • (2015) Matrix Biol. , vol.47 , pp. 3-12
    • Sengle, G.1    Sakai, L.Y.2
  • 82
    • 84943661523 scopus 로고    scopus 로고
    • ADAMTS proteins as modulators of microfibril formation and function
    • [82] Hubmacher, D., Apte, S.S., ADAMTS proteins as modulators of microfibril formation and function. Matrix Biol. 47 (2015), 34–43.
    • (2015) Matrix Biol. , vol.47 , pp. 34-43
    • Hubmacher, D.1    Apte, S.S.2
  • 85
    • 84943817650 scopus 로고    scopus 로고
    • The extracellular matrix and transforming growth factor-beta1: tale of a strained relationship
    • [85] Hinz, B., The extracellular matrix and transforming growth factor-beta1: tale of a strained relationship. Matrix Biol. 47 (2015), 54–65.
    • (2015) Matrix Biol. , vol.47 , pp. 54-65
    • Hinz, B.1
  • 86
    • 0037040270 scopus 로고    scopus 로고
    • Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1
    • [86] Reinboth, B., Hanssen, E., Cleary, E.G., Gibson, M.A., Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1. J. Biol. Chem. 277 (2002), 3950–3957.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3950-3957
    • Reinboth, B.1    Hanssen, E.2    Cleary, E.G.3    Gibson, M.A.4
  • 87
    • 0025954786 scopus 로고
    • Interaction of the small proteoglycan decorin with fibronectin. Involvement of the sequence NKISK of the core protein
    • [87] Schmidt, G., Hausser, H., Kresse, H., Interaction of the small proteoglycan decorin with fibronectin. Involvement of the sequence NKISK of the core protein. Biochem. J. 280 (1991), 411–414.
    • (1991) Biochem. J. , vol.280 , pp. 411-414
    • Schmidt, G.1    Hausser, H.2    Kresse, H.3
  • 88
    • 0025892331 scopus 로고
    • Influence of decorin on fibroblast adhesion to fibronectin
    • [88] Winnemöller, M., Schmidt, G., Kresse, H., Influence of decorin on fibroblast adhesion to fibronectin. Eur. J. Cell Biol. 54 (1991), 10–17.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 10-17
    • Winnemöller, M.1    Schmidt, G.2    Kresse, H.3
  • 89
    • 0026473155 scopus 로고
    • Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment
    • [89] Winnemöller, M., Schön, P., Vischer, P., Kresse, H., Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment. Eur. J. Cell Biol. 59 (1992), 47–55.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 47-55
    • Winnemöller, M.1    Schön, P.2    Vischer, P.3    Kresse, H.4
  • 91
    • 84857790767 scopus 로고    scopus 로고
    • Thrombospondins in physiology and disease: new tricks for old dogs
    • [91] Murphy-Ullrich, J.E., Iozzo, R.V., Thrombospondins in physiology and disease: new tricks for old dogs. Matrix Biol. 31 (2012), 152–154.
    • (2012) Matrix Biol. , vol.31 , pp. 152-154
    • Murphy-Ullrich, J.E.1    Iozzo, R.V.2
  • 92
    • 84908350153 scopus 로고    scopus 로고
    • Revisiting the matricellular concept
    • [92] Murphy-Ullrich, J.E., Sage, E.H., Revisiting the matricellular concept. Matrix Biol. 37 (2014), 1–14.
    • (2014) Matrix Biol. , vol.37 , pp. 1-14
    • Murphy-Ullrich, J.E.1    Sage, E.H.2
  • 94
    • 84908347357 scopus 로고    scopus 로고
    • Current understanding of the thrombospondin-1 interactome
    • [94] Resovi, A., Pinessi, D., Chiorino, G., Taraboletti, G., Current understanding of the thrombospondin-1 interactome. Matrix Biol. 37 (2014), 83–91.
    • (2014) Matrix Biol. , vol.37 , pp. 83-91
    • Resovi, A.1    Pinessi, D.2    Chiorino, G.3    Taraboletti, G.4
  • 95
    • 84908329397 scopus 로고    scopus 로고
    • Thrombospondin-1 and CD47 regulation of cardiac, pulmonary and vascular responses in health and disease
    • [95] Rogers, N.M., Sharifi-Sanjani, M., Csanyi, G., Pagano, P.J., Isenberg, J.S., Thrombospondin-1 and CD47 regulation of cardiac, pulmonary and vascular responses in health and disease. Matrix Biol. 37 (2014), 92–101.
    • (2014) Matrix Biol. , vol.37 , pp. 92-101
    • Rogers, N.M.1    Sharifi-Sanjani, M.2    Csanyi, G.3    Pagano, P.J.4    Isenberg, J.S.5
  • 96
    • 84908338414 scopus 로고    scopus 로고
    • Members of the thrombospondin gene family bind stromal interaction molecule 1 and regulate calcium channel activity
    • [96] Duquette, M., Nadler, M., Okuhara, D., Thompson, J., Shuttleworth, T., Lawler, J., Members of the thrombospondin gene family bind stromal interaction molecule 1 and regulate calcium channel activity. Matrix Biol. 37 (2014), 15–24.
    • (2014) Matrix Biol. , vol.37 , pp. 15-24
    • Duquette, M.1    Nadler, M.2    Okuhara, D.3    Thompson, J.4    Shuttleworth, T.5    Lawler, J.6
  • 97
    • 84908323775 scopus 로고    scopus 로고
    • Invoking the power of thrombospondins: regulation of thrombospondins expression
    • [97] Stenina-Adognravi, O., Invoking the power of thrombospondins: regulation of thrombospondins expression. Matrix Biol. 37 (2014), 69–82.
    • (2014) Matrix Biol. , vol.37 , pp. 69-82
    • Stenina-Adognravi, O.1
  • 98
    • 84958078660 scopus 로고    scopus 로고
    • WISP1 mediates IL-6-dependent proliferation in primary human lung fibroblasts
    • [98] Klee, S., Lehmann, M., Wagner, D.E., Baarsma, H.A., Konigshoff, M., WISP1 mediates IL-6-dependent proliferation in primary human lung fibroblasts. Sci. Rep., 6, 2016, 20547.
    • (2016) Sci. Rep. , vol.6 , pp. 20547
    • Klee, S.1    Lehmann, M.2    Wagner, D.E.3    Baarsma, H.A.4    Konigshoff, M.5
  • 99
    • 0035861577 scopus 로고    scopus 로고
    • WISP-1 binds to decorin and biglycan
    • [99] Desnoyers, L., Arnott, D., Pennica, D., WISP-1 binds to decorin and biglycan. J. Biol. Chem. 276 (2001), 47599–47607.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47599-47607
    • Desnoyers, L.1    Arnott, D.2    Pennica, D.3
  • 100
    • 0033837901 scopus 로고    scopus 로고
    • Identification and immunolocalization of decorin, versican, perlecan, nidogen and chondroitin sulfate proteoglycans in bovine small-antral ovarian follicles
    • [100] McArthur, M.E., Irving-Rodgers, H.F., Byer, S., Rodgers, R.J., Identification and immunolocalization of decorin, versican, perlecan, nidogen and chondroitin sulfate proteoglycans in bovine small-antral ovarian follicles. Biol. Reprod. 63 (2000), 913–924.
    • (2000) Biol. Reprod. , vol.63 , pp. 913-924
    • McArthur, M.E.1    Irving-Rodgers, H.F.2    Byer, S.3    Rodgers, R.J.4
  • 101
    • 84901418809 scopus 로고    scopus 로고
    • Versican and the control of inflammation
    • [101] Wight, T.N., Kang, I., Merrilees, M.J., Versican and the control of inflammation. Matrix Biol. 35 (2014), 152–161.
    • (2014) Matrix Biol. , vol.35 , pp. 152-161
    • Wight, T.N.1    Kang, I.2    Merrilees, M.J.3
  • 103
    • 84901459609 scopus 로고    scopus 로고
    • Reprint of: a rapid increase in macrophage-derived versican and hyaluronan in infectious lung disease
    • [103] Chang, M.Y., Tanino, Y., Vidova, V., Kinsella, M.G., Chan, C.K., Johnson, P.Y., et al. Reprint of: a rapid increase in macrophage-derived versican and hyaluronan in infectious lung disease. Matrix Biol. 35 (2014), 162–173.
    • (2014) Matrix Biol. , vol.35 , pp. 162-173
    • Chang, M.Y.1    Tanino, Y.2    Vidova, V.3    Kinsella, M.G.4    Chan, C.K.5    Johnson, P.Y.6
  • 104
    • 84947870176 scopus 로고    scopus 로고
    • Perlecan inhibits autophagy to maintain muscle homeostasis in mouse soleus muscle
    • [104] Ning, L., Xu, Z., Furuya, N., Nonaka, R., Yamada, Y., Arikawa-Hirasawa, E., Perlecan inhibits autophagy to maintain muscle homeostasis in mouse soleus muscle. Matrix Biol. 48 (2015), 26–35.
    • (2015) Matrix Biol. , vol.48 , pp. 26-35
    • Ning, L.1    Xu, Z.2    Furuya, N.3    Nonaka, R.4    Yamada, Y.5    Arikawa-Hirasawa, E.6
  • 105
    • 84909966044 scopus 로고    scopus 로고
    • Matrilysin/matrix metalloproteinase-7(MMP7) cleavage of perlecan/HSPG2 creates a molecular switch to alter prostate cancer cell behavior
    • [105] Grindel, B.J., Martinez, J.R., Pennington, C.L., Muldoon, M., Stave, J., Chung, L.W., et al. Matrilysin/matrix metalloproteinase-7(MMP7) cleavage of perlecan/HSPG2 creates a molecular switch to alter prostate cancer cell behavior. Matrix Biol. 36 (2014), 64–76.
    • (2014) Matrix Biol. , vol.36 , pp. 64-76
    • Grindel, B.J.1    Martinez, J.R.2    Pennington, C.L.3    Muldoon, M.4    Stave, J.5    Chung, L.W.6
  • 106
    • 84901390292 scopus 로고    scopus 로고
    • The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling
    • [106] Lord, M.S., Chuang, C.Y., Melrose, J., Davies, M.J., Iozzo, R.V., Whitelock, J.M., The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling. Matrix Biol. 35 (2014), 112–122.
    • (2014) Matrix Biol. , vol.35 , pp. 112-122
    • Lord, M.S.1    Chuang, C.Y.2    Melrose, J.3    Davies, M.J.4    Iozzo, R.V.5    Whitelock, J.M.6
  • 107
    • 84900304808 scopus 로고    scopus 로고
    • Border patrol:insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue borders
    • [107] Farach-Carson, M.C., Warren, C.R., Harrington, D.A., Carson, D.D., Border patrol:insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue borders. Matrix Biol. 34 (2014), 64–79.
    • (2014) Matrix Biol. , vol.34 , pp. 64-79
    • Farach-Carson, M.C.1    Warren, C.R.2    Harrington, D.A.3    Carson, D.D.4
  • 109
    • 0029117215 scopus 로고
    • Adherence of Borrelia burgdorferi to the proteoglycan decorin
    • [109] Guo, B., Norris, S., Rosenberg, L.C., Höök, M., Adherence of Borrelia burgdorferi to the proteoglycan decorin. Infect. Immun. 63 (1995), 3467–3472.
    • (1995) Infect. Immun. , vol.63 , pp. 3467-3472
    • Guo, B.1    Norris, S.2    Rosenberg, L.C.3    Höök, M.4
  • 110
    • 40749130867 scopus 로고    scopus 로고
    • Both decorin-binding proteins A and B are critical for the overall virulence of Borrelia burgdorferi
    • [110] Shi, Y., Xu, Q., McShan, K., Liang, F.T., Both decorin-binding proteins A and B are critical for the overall virulence of Borrelia burgdorferi. Infect. Immun. 76 (2008), 1239–1246.
    • (2008) Infect. Immun. , vol.76 , pp. 1239-1246
    • Shi, Y.1    Xu, Q.2    McShan, K.3    Liang, F.T.4
  • 111
    • 0032518407 scopus 로고    scopus 로고
    • Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor
    • [111] Moscatello, D.K., Santra, M., Mann, D.M., McQuillan, D.J., Wong, A.J., Iozzo, R.V., Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor. J. Clin. Invest. 101 (1998), 406–412.
    • (1998) J. Clin. Invest. , vol.101 , pp. 406-412
    • Moscatello, D.K.1    Santra, M.2    Mann, D.M.3    McQuillan, D.J.4    Wong, A.J.5    Iozzo, R.V.6
  • 112
    • 25444503249 scopus 로고    scopus 로고
    • Decorin evokes protracted internalization and degradation of the EGF receptor via caveolar endocytosis
    • [112] Zhu, J.-X., Goldoni, S., Bix, G., Owens, R.A., McQuillan, D., Reed, C.C., et al. Decorin evokes protracted internalization and degradation of the EGF receptor via caveolar endocytosis. J. Biol. Chem. 280 (2005), 32468–32479.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32468-32479
    • Zhu, J.-X.1    Goldoni, S.2    Bix, G.3    Owens, R.A.4    McQuillan, D.5    Reed, C.C.6
  • 114
    • 57349175862 scopus 로고    scopus 로고
    • Tumor microenvironment: modulation by decorin and related molecules harboring leucine-rich tandem motifs
    • [114] Goldoni, S., Iozzo, R.V., Tumor microenvironment: modulation by decorin and related molecules harboring leucine-rich tandem motifs. Int. J. Cancer 123 (2008), 2473–2479.
    • (2008) Int. J. Cancer , vol.123 , pp. 2473-2479
    • Goldoni, S.1    Iozzo, R.V.2
  • 115
    • 84894479646 scopus 로고    scopus 로고
    • Decorin induces mitophagy in breast carcinoma cells via peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) and mitostatin
    • [115] Neill, T., Torres, A., Buraschi, S., Owens, R.T., Hoek, J., Baffa, R., et al. Decorin induces mitophagy in breast carcinoma cells via peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α) and mitostatin. J. Biol. Chem. 289 (2014), 4952–4968.
    • (2014) J. Biol. Chem. , vol.289 , pp. 4952-4968
    • Neill, T.1    Torres, A.2    Buraschi, S.3    Owens, R.T.4    Hoek, J.5    Baffa, R.6
  • 116
    • 80053402608 scopus 로고    scopus 로고
    • Decorin antagonizes IGF receptor I (IGF-IR) function by interfering with IGF-IR activity and attenuating downstream signaling
    • [116] Iozzo, R.V., Buraschi, S., Genua, M., Xu, S.-Q., Solomides, C.C., Peiper, S.C., et al. Decorin antagonizes IGF receptor I (IGF-IR) function by interfering with IGF-IR activity and attenuating downstream signaling. J. Biol. Chem. 286 (2011), 34712–34721.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34712-34721
    • Iozzo, R.V.1    Buraschi, S.2    Genua, M.3    Xu, S.-Q.4    Solomides, C.C.5    Peiper, S.C.6
  • 117
    • 84901451484 scopus 로고    scopus 로고
    • Decorin differentially modulates the activity of insulin receptor isoform A ligands
    • [117] Morcavallo, A., Buraschi, S., Xu, S.-Q., Belfiore, A., Schaefer, L., Iozzo, R.V., et al. Decorin differentially modulates the activity of insulin receptor isoform A ligands. Matrix Biol. 35 (2014), 82–90.
    • (2014) Matrix Biol. , vol.35 , pp. 82-90
    • Morcavallo, A.1    Buraschi, S.2    Xu, S.-Q.3    Belfiore, A.4    Schaefer, L.5    Iozzo, R.V.6
  • 118
    • 84877716242 scopus 로고    scopus 로고
    • Dichotomy of decorin activity on the insulin-like growth factor-I system
    • [118] Morrione, A., Neill, T., Iozzo, R.V., Dichotomy of decorin activity on the insulin-like growth factor-I system. FEBS J. 280 (2013), 2138–2149.
    • (2013) FEBS J. , vol.280 , pp. 2138-2149
    • Morrione, A.1    Neill, T.2    Iozzo, R.V.3
  • 119
    • 84869416110 scopus 로고    scopus 로고
    • Mechanisms in decorin regulation of vascular endothelial growth factor-induced human trophoblast migration and acquisition of endothelial phenotype
    • [119] Lala, N., Gannareddy, V.G., Cloutier-Bosworth, A., Lala, P.K., Mechanisms in decorin regulation of vascular endothelial growth factor-induced human trophoblast migration and acquisition of endothelial phenotype. Biol. Reprod. 87:59 (2012), 1–14.
    • (2012) Biol. Reprod. , vol.87 , Issue.59 , pp. 1-14
    • Lala, N.1    Gannareddy, V.G.2    Cloutier-Bosworth, A.3    Lala, P.K.4
  • 120
    • 84861871896 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation
    • [120] Moreth, K., Iozzo, R.V., Schaefer, L., Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation. Cell Cycle 11 (2012), 2084–2091.
    • (2012) Cell Cycle , vol.11 , pp. 2084-2091
    • Moreth, K.1    Iozzo, R.V.2    Schaefer, L.3
  • 121
    • 84858450953 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation
    • [121] Schaefer, L., Iozzo, R.V., Small leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation. Curr. Opin. Genet. Dev. 22 (2012), 56–57.
    • (2012) Curr. Opin. Genet. Dev. , vol.22 , pp. 56-57
    • Schaefer, L.1    Iozzo, R.V.2
  • 122
    • 0037470088 scopus 로고    scopus 로고
    • The class A scavenger receptor binds to proteoglycans and mediates adhesion of macrophages to the extracellular matrix
    • [122] Santiago-García, J., Kodama, T., Pitas, R.E., The class A scavenger receptor binds to proteoglycans and mediates adhesion of macrophages to the extracellular matrix. J. Biol. Chem. 278 (2003), 6942–6946.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6942-6946
    • Santiago-García, J.1    Kodama, T.2    Pitas, R.E.3
  • 124
    • 84970015911 scopus 로고    scopus 로고
    • Biglycan potentially regulates angiogenesis during fracture repair by altering expression and function of endostatin
    • [124] Myren, M., Kirby, D.J., Noonan, M.L., Maeda, A., Owens, R.T., Ricard-Blum, S., et al. Biglycan potentially regulates angiogenesis during fracture repair by altering expression and function of endostatin. Matrix Biol. 52-54 (2016), 141–150.
    • (2016) Matrix Biol. , vol.52-54 , pp. 141-150
    • Myren, M.1    Kirby, D.J.2    Noonan, M.L.3    Maeda, A.4    Owens, R.T.5    Ricard-Blum, S.6
  • 125
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin
    • [125] Brandan, E., Retamal, C., Cabello-Verrugio, C., Marzolo, M.-P., The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin. J. Biol. Chem. 281 (2006), 31562–31571.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31562-31571
    • Brandan, E.1    Retamal, C.2    Cabello-Verrugio, C.3    Marzolo, M.-P.4
  • 126
    • 34547131835 scopus 로고    scopus 로고
    • A novel modulatory mechanism of transforming growth factor-β signaling through decorin and LRP-1
    • [126] Cabello-Verrugio, C., Brandan, E., A novel modulatory mechanism of transforming growth factor-β signaling through decorin and LRP-1. J. Biol. Chem. 282 (2007), 18842–18850.
    • (2007) J. Biol. Chem. , vol.282 , pp. 18842-18850
    • Cabello-Verrugio, C.1    Brandan, E.2
  • 127
    • 84857479041 scopus 로고    scopus 로고
    • The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-beta-dependent signaling, and inhibits TGF-beta-dependent fibrotic response in skeletal muscles
    • [127] Cabello-Verrugio, C., Santander, C., Cofre, C., Acuna, M.J., Melo, F., Brandan, E., The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-beta-dependent signaling, and inhibits TGF-beta-dependent fibrotic response in skeletal muscles. J. Biol. Chem. 287 (2012), 6773–6787.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6773-6787
    • Cabello-Verrugio, C.1    Santander, C.2    Cofre, C.3    Acuna, M.J.4    Melo, F.5    Brandan, E.6
  • 128
    • 56949083199 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy
    • [128] Brandan, E., Cabello-Verrugio, C., Vial, C., Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy. Matrix Biol. 27 (2008), 700–708.
    • (2008) Matrix Biol. , vol.27 , pp. 700-708
    • Brandan, E.1    Cabello-Verrugio, C.2    Vial, C.3
  • 129
    • 84870690407 scopus 로고    scopus 로고
    • The dermatan sulfate proteoglycan decorin modulates α2β1 integrin and vimentin intermediate filament system during collagen synthesis
    • [129] Jungmann, O., Nikolovska, K., Stock, C., Schulz, J.-N., Eckes, B., Riethmüller, C., et al. The dermatan sulfate proteoglycan decorin modulates α2β1 integrin and vimentin intermediate filament system during collagen synthesis. PLoS One, 7, 2012, e50809.
    • (2012) PLoS One , vol.7 , pp. e50809
    • Jungmann, O.1    Nikolovska, K.2    Stock, C.3    Schulz, J.-N.4    Eckes, B.5    Riethmüller, C.6
  • 130
    • 0032763725 scopus 로고    scopus 로고
    • Functional domains present in the mycobacterial hemagglutinin, HBHA
    • [130] Delogu, G., Brennan, M.J., Functional domains present in the mycobacterial hemagglutinin, HBHA. J. Bacteriol. 181 (1999), 7464–7469.
    • (1999) J. Bacteriol. , vol.181 , pp. 7464-7469
    • Delogu, G.1    Brennan, M.J.2
  • 131
    • 0028600614 scopus 로고
    • Bone matrix decorin binds transforming growth factor-β and enhances its bioactivity
    • [131] Takeuchi, Y., Kodama, Y., Matsumoto, T., Bone matrix decorin binds transforming growth factor-β and enhances its bioactivity. J. Biol. Chem. 269 (1994), 32634–32638.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32634-32638
    • Takeuchi, Y.1    Kodama, Y.2    Matsumoto, T.3
  • 132
    • 0034979153 scopus 로고    scopus 로고
    • Proteoblycans decorin and biglycan differentially modulate TGF-β-mediated fibrotic responses in the lung
    • [132] Kolb, M., Margetts, P.J., Sime, P.J., Gauldie, J., Proteoblycans decorin and biglycan differentially modulate TGF-β-mediated fibrotic responses in the lung. Am. J. Physiol. Lung Cell. Mol. Physiol. 280 (2001), L1327–L1334.
    • (2001) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.280 , pp. L1327-L1334
    • Kolb, M.1    Margetts, P.J.2    Sime, P.J.3    Gauldie, J.4
  • 134
    • 0029056591 scopus 로고
    • Transcriptional regulation of decorin gene expression. Induction by quiescence and repression by tumor necrosis factor-α
    • [134] Mauviel, A., Santra, M., Chen, Y.Q., Uitto, J., Iozzo, R.V., Transcriptional regulation of decorin gene expression. Induction by quiescence and repression by tumor necrosis factor-α. J. Biol. Chem. 270 (1995), 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
  • 135
    • 8444243360 scopus 로고    scopus 로고
    • Regulation of muscle mass by myostatin
    • [135] Lee, S.-J., Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol. 20 (2004), 61–86.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 61-86
    • Lee, S.-J.1
  • 137
    • 84875779325 scopus 로고    scopus 로고
    • CTGF is a central mediator of tissue remodeling and fibrosis and its inhibition can reverse the process of fibrosis
    • [137] Lipson, K.E., Wong, C., Teng, Y., Spong, S., CTGF is a central mediator of tissue remodeling and fibrosis and its inhibition can reverse the process of fibrosis. Fibrogenesis Tissue Repair, 5, 2012, S24.
    • (2012) Fibrogenesis Tissue Repair , vol.5 , pp. S24
    • Lipson, K.E.1    Wong, C.2    Teng, Y.3    Spong, S.4
  • 138
    • 84949267354 scopus 로고    scopus 로고
    • Oncogenic activin C interacts with decorin in colorectal cancer in vivo and in vitro
    • [138] Bi, X., Xia, X., Fan, D., Mu, T., Zhang, Q., Iozzo, R.V., et al. Oncogenic activin C interacts with decorin in colorectal cancer in vivo and in vitro. Mol. Carcinog., 2015.
    • (2015) Mol. Carcinog.
    • Bi, X.1    Xia, X.2    Fan, D.3    Mu, T.4    Zhang, Q.5    Iozzo, R.V.6
  • 139
    • 0037163862 scopus 로고    scopus 로고
    • Tumor necrosis factor-α interacts with biglycan and decorin
    • [139] Tufvesson, E., Westergren-Thorsson, G., Tumor necrosis factor-α interacts with biglycan and decorin. FEBS Lett. 530 (2002), 124–128.
    • (2002) FEBS Lett. , vol.530 , pp. 124-128
    • Tufvesson, E.1    Westergren-Thorsson, G.2
  • 141
  • 142
    • 58149350127 scopus 로고    scopus 로고
    • Decorin and its galactosaminoglycan chain: extracellular regulator of cellular function?
    • [142] Seidler, D.G., Dreier, R., Decorin and its galactosaminoglycan chain: extracellular regulator of cellular function?. IUBMB Life 60 (2008), 729–733.
    • (2008) IUBMB Life , vol.60 , pp. 729-733
    • Seidler, D.G.1    Dreier, R.2
  • 143
    • 84930764947 scopus 로고    scopus 로고
    • Matrix remodeling by MMPs during wound repair
    • [143] Rohani, M.G., Parks, W.C., Matrix remodeling by MMPs during wound repair. Matrix Biol. 44-46 (2015), 113–121.
    • (2015) Matrix Biol. , vol.44-46 , pp. 113-121
    • Rohani, M.G.1    Parks, W.C.2
  • 144
    • 84930752520 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases: their functions and regulations
    • [144] Itoh, Y., Membrane-type matrix metalloproteinases: their functions and regulations. Matrix Biol. 44-46 (2015), 207–223.
    • (2015) Matrix Biol. , vol.44-46 , pp. 207-223
    • Itoh, Y.1
  • 145
    • 84930764392 scopus 로고    scopus 로고
    • Tumor angiogenesis: MMP-mediated induction of intravasation- and metastasis-sustaining neovasculature
    • [145] Deryugina, E.I., Quigley, J.P., Tumor angiogenesis: MMP-mediated induction of intravasation- and metastasis-sustaining neovasculature. Matrix Biol. 44-46 (2015), 94–112.
    • (2015) Matrix Biol. , vol.44-46 , pp. 94-112
    • Deryugina, E.I.1    Quigley, J.P.2
  • 146
    • 84930757646 scopus 로고    scopus 로고
    • Multilevel regulation of matrix metalloproteinases in tissue homeostasis indicates their molecular specificity in vivo
    • [146] Gaffney, J., Solomonov, I., Zehorai, E., Sagi, I., Multilevel regulation of matrix metalloproteinases in tissue homeostasis indicates their molecular specificity in vivo. Matrix Biol. 44-46 (2015), 191–199.
    • (2015) Matrix Biol. , vol.44-46 , pp. 191-199
    • Gaffney, J.1    Solomonov, I.2    Zehorai, E.3    Sagi, I.4
  • 147
    • 0030958072 scopus 로고    scopus 로고
    • Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release
    • [147] Imai, K., Hiramatsu, A., Fukushima, D., Pierschbacher, M.D., Okada, Y., Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem. J. 322:Pt 3 (1997), 809–814.
    • (1997) Biochem. J. , vol.322 , pp. 809-814
    • Imai, K.1    Hiramatsu, A.2    Fukushima, D.3    Pierschbacher, M.D.4    Okada, Y.5
  • 148
    • 84930753614 scopus 로고    scopus 로고
    • Matrix metalloproteinases in liver injury, repair and fibrosis
    • [148] Duarte, S., Baber, J., Fujii, T., Coito, A.J., Matrix metalloproteinases in liver injury, repair and fibrosis. Matrix Biol. 44-46 (2015), 147–156.
    • (2015) Matrix Biol. , vol.44-46 , pp. 147-156
    • Duarte, S.1    Baber, J.2    Fujii, T.3    Coito, A.J.4
  • 149
    • 73949158120 scopus 로고    scopus 로고
    • Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1)
    • [149] von Marschall, Z., Fisher, L.W., Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1). Biochem. Biophys. Res. Comm. 391 (2010), 1374–1378.
    • (2010) Biochem. Biophys. Res. Comm. , vol.391 , pp. 1374-1378
    • von Marschall, Z.1    Fisher, L.W.2
  • 150
    • 84930765783 scopus 로고    scopus 로고
    • BMP-1/tolloid-like proteinases synchronize matrix assembly with growth factor activation to promote morphogenesis and tissue remodeling
    • [150] Vadon-Le Goff, S., Hulmes, D.J., Moali, C., BMP-1/tolloid-like proteinases synchronize matrix assembly with growth factor activation to promote morphogenesis and tissue remodeling. Matrix Biol. 44-46 (2015), 14–23.
    • (2015) Matrix Biol. , vol.44-46 , pp. 14-23
    • Vadon-Le Goff, S.1    Hulmes, D.J.2    Moali, C.3
  • 151
    • 0034737779 scopus 로고    scopus 로고
    • Molecular basis for the association of group IIA phospholipase A(2) and decorin in human atherosclerotic lesions
    • [151] Sartipy, P., Johansen, B., Gasvik, K., Hurt-Camejo, E., Molecular basis for the association of group IIA phospholipase A(2) and decorin in human atherosclerotic lesions. Circ. Res. 86 (2000), 707–714.
    • (2000) Circ. Res. , vol.86 , pp. 707-714
    • Sartipy, P.1    Johansen, B.2    Gasvik, K.3    Hurt-Camejo, E.4
  • 152
    • 66349090778 scopus 로고    scopus 로고
    • Phospholipase A2 structure/function, mechanism, and signaling
    • [152] Burke, J.E., Dennis, E.A., Phospholipase A2 structure/function, mechanism, and signaling. J. Lipid Res. 50:Suppl (2009), S237–S242.
    • (2009) J. Lipid Res. , vol.50 , pp. S237-S242
    • Burke, J.E.1    Dennis, E.A.2
  • 153
    • 0036721028 scopus 로고    scopus 로고
    • The small proteoglycan decorin supports adhesion and activation of human platelets
    • [153] Guidetti, G., Bertoni, A., Viola, M., Tira, E., Balduini, C., Torti, M., The small proteoglycan decorin supports adhesion and activation of human platelets. Blood 100 (2002), 1707–1714.
    • (2002) Blood , vol.100 , pp. 1707-1714
    • Guidetti, G.1    Bertoni, A.2    Viola, M.3    Tira, E.4    Balduini, C.5    Torti, M.6
  • 154
    • 51349164922 scopus 로고    scopus 로고
    • Function of von Willebrand factor in haemostasis and thrombosis
    • [154] Reininger, A.J., Function of von Willebrand factor in haemostasis and thrombosis. Haemophilia 14:Suppl 5 (2008), 11–26.
    • (2008) Haemophilia , vol.14 , pp. 11-26
    • Reininger, A.J.1
  • 157
    • 33846002042 scopus 로고    scopus 로고
    • Decorin modulates fibrin assembly and structure
    • [157] Dugan, T.A., Yang, V.W.C., McQuillan, D.J., Höök, M., Decorin modulates fibrin assembly and structure. J. Biol. Chem. 281 (2006), 38208–38216.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38208-38216
    • Dugan, T.A.1    Yang, V.W.C.2    McQuillan, D.J.3    Höök, M.4
  • 158
    • 0026048441 scopus 로고
    • Molecular basis of apolipoprotein (a) isoform size heterogeneity as revealed by pulsed-field gel electrophoresis
    • [158] Lackner, C., Boerwinkle, E., Leffert, C.C., Rahmig, T., Hobbs, H.H., Molecular basis of apolipoprotein (a) isoform size heterogeneity as revealed by pulsed-field gel electrophoresis. J. Clin. Invest. 87 (1991), 2153–2161.
    • (1991) J. Clin. Invest. , vol.87 , pp. 2153-2161
    • Lackner, C.1    Boerwinkle, E.2    Leffert, C.C.3    Rahmig, T.4    Hobbs, H.H.5
  • 159
    • 0032508573 scopus 로고    scopus 로고
    • Apolipoprotein(a) binds via its C-terminal domain to the protein core of the proteoglycan decorin. Implications for the retention of lipoprotein(a) in atherosclerotic lesions
    • [159] Klezovitch, O., Edelstein, C., Zhu, L., Scanu, A.M., Apolipoprotein(a) binds via its C-terminal domain to the protein core of the proteoglycan decorin. Implications for the retention of lipoprotein(a) in atherosclerotic lesions. J. Biol. Chem. 273 (1998), 23856–23865.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23856-23865
    • Klezovitch, O.1    Edelstein, C.2    Zhu, L.3    Scanu, A.M.4
  • 160
    • 0033117090 scopus 로고    scopus 로고
    • Decorin links low-density lipoproteins (LDL) to collagen: a novel mechanism for retention of LDL in the atherosclerotic plaque
    • [160] Kovanen, P.T., Pentikäinen, M.O., Decorin links low-density lipoproteins (LDL) to collagen: a novel mechanism for retention of LDL in the atherosclerotic plaque. Trends Cardiovasc. Med. 9 (1999), 86–91.
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 86-91
    • Kovanen, P.T.1    Pentikäinen, M.O.2
  • 161
    • 0030950781 scopus 로고    scopus 로고
    • The proteoglycan decorin links low density lipoproteins with collagen type I
    • [161] Pentikäinen, M.O., öörni, K., Lassila, R., Kovanen, P.T., The proteoglycan decorin links low density lipoproteins with collagen type I. J. Biol. Chem. 272 (1997), 7633–7638.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7633-7638
    • Pentikäinen, M.O.1    öörni, K.2    Lassila, R.3    Kovanen, P.T.4
  • 163
    • 33750304277 scopus 로고    scopus 로고
    • Actin-binding protein filamin A is displayed on the surface of human neuroblastoma cells
    • [163] Bachmann, A.S., Howard, J.P., Vogel, C.W., Actin-binding protein filamin A is displayed on the surface of human neuroblastoma cells. Cancer Sci. 97 (2006), 1359–1365.
    • (2006) Cancer Sci. , vol.97 , pp. 1359-1365
    • Bachmann, A.S.1    Howard, J.P.2    Vogel, C.W.3
  • 164
    • 79960010914 scopus 로고    scopus 로고
    • An isoform of decorin is a resistin receptor on the surface of adipose progenitor cells
    • [164] Daquinag, A.C., Zhang, Y., Amaya-Manzanares, F., Simmons, P.J., Kolonin, M.G., An isoform of decorin is a resistin receptor on the surface of adipose progenitor cells. Cell Stem Cell 9 (2011), 74–86.
    • (2011) Cell Stem Cell , vol.9 , pp. 74-86
    • Daquinag, A.C.1    Zhang, Y.2    Amaya-Manzanares, F.3    Simmons, P.J.4    Kolonin, M.G.5
  • 165
    • 0038152797 scopus 로고    scopus 로고
    • Identification and characterization of a novel interaction between pulmonary surfactant protein D and decorin
    • [165] Nadesalingam, J., Bernal, A.L., Dodds, A.W., Willis, A.C., Mahoney, D.J., Day, A.J., et al. Identification and characterization of a novel interaction between pulmonary surfactant protein D and decorin. J. Biol. Chem. 278 (2003), 25678–25687.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25678-25687
    • Nadesalingam, J.1    Bernal, A.L.2    Dodds, A.W.3    Willis, A.C.4    Mahoney, D.J.5    Day, A.J.6
  • 166
    • 0026463907 scopus 로고
    • The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex
    • [166] Krumdieck, R., Höök, M., Rosenberg, L.C., Volanakis, J.E., The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex. J. Immunol. 149 (1992), 3695–3701.
    • (1992) J. Immunol. , vol.149 , pp. 3695-3701
    • Krumdieck, R.1    Höök, M.2    Rosenberg, L.C.3    Volanakis, J.E.4
  • 167
    • 0036931513 scopus 로고    scopus 로고
    • The interaction of recombinant decorin with α2HS-glycoprotein-implications for structural and functional investigations
    • [167] Sugars, R.V., Waddington, R.J., Embery, G., The interaction of recombinant decorin with α2HS-glycoprotein-implications for structural and functional investigations. Protein Expr. Purif. 25 (2002), 180–188.
    • (2002) Protein Expr. Purif. , vol.25 , pp. 180-188
    • Sugars, R.V.1    Waddington, R.J.2    Embery, G.3
  • 168
  • 169
    • 84938635144 scopus 로고    scopus 로고
    • Decoding the matrix: instructive roles of proteoglycan receptors
    • [169] Neill, T., Schaefer, L., Iozzo, R.V., Decoding the matrix: instructive roles of proteoglycan receptors. Biochemistry 54 (2015), 4583–4598.
    • (2015) Biochemistry , vol.54 , pp. 4583-4598
    • Neill, T.1    Schaefer, L.2    Iozzo, R.V.3
  • 170
    • 84864138010 scopus 로고    scopus 로고
    • Decorin, a guardian from the matrix
    • [170] Neill, T., Schaefer, L., Iozzo, R.V., Decorin, a guardian from the matrix. Am. J. Pathol. 181 (2012), 380–387.
    • (2012) Am. J. Pathol. , vol.181 , pp. 380-387
    • Neill, T.1    Schaefer, L.2    Iozzo, R.V.3
  • 171
    • 84927546643 scopus 로고    scopus 로고
    • Insights into the key roles of proteoglycans in breast cancer biology and translational medicine
    • [171] Theocharis, A.D., Skandalis, S.S., Neill, T., Multhaupt, H.A., Hubo, M., Frey, H., et al. Insights into the key roles of proteoglycans in breast cancer biology and translational medicine. Biochim. Biophys. Acta 1855 (2015), 276–300.
    • (2015) Biochim. Biophys. Acta , vol.1855 , pp. 276-300
    • Theocharis, A.D.1    Skandalis, S.S.2    Neill, T.3    Multhaupt, H.A.4    Hubo, M.5    Frey, H.6
  • 172
    • 84924628052 scopus 로고    scopus 로고
    • The systemic delivery of an oncolytic adenovirus expressing decorin inhibits bone metastasis in a mouse model of human prostate cancer
    • [172] Xu, W., Neill, T., Yang, Y., Hu, Z., Cleveland, E., Wu, Y., et al. The systemic delivery of an oncolytic adenovirus expressing decorin inhibits bone metastasis in a mouse model of human prostate cancer. Gene Ther. 22 (2015), 31–40.
    • (2015) Gene Ther. , vol.22 , pp. 31-40
    • Xu, W.1    Neill, T.2    Yang, Y.3    Hu, Z.4    Cleveland, E.5    Wu, Y.6
  • 173
    • 84949886842 scopus 로고    scopus 로고
    • Systemic delivery of an oncolytic adenovirus expressing decorin for the treatment of breast cancer bone metastases
    • [173] Yang, Y., Xu, W.W., Neill, T., Hu, Z., Wang, C.H., Xiao, X., et al. Systemic delivery of an oncolytic adenovirus expressing decorin for the treatment of breast cancer bone metastases. Hum. Gene Ther. 26 (2015), 813–825.
    • (2015) Hum. Gene Ther. , vol.26 , pp. 813-825
    • Yang, Y.1    Xu, W.W.2    Neill, T.3    Hu, Z.4    Wang, C.H.5    Xiao, X.6
  • 175
    • 49349109705 scopus 로고    scopus 로고
    • Genetic deficiency of decorin causes intestinal tumor formation through disruption of intestinal cell maturation
    • [175] Bi, X., Tong, C., Dokendorff, A., Banroft, L., Gallagher, L., Guzman-Hartman, G., et al. Genetic deficiency of decorin causes intestinal tumor formation through disruption of intestinal cell maturation. Carcinogenesis 29 (2008), 1435–1440.
    • (2008) Carcinogenesis , vol.29 , pp. 1435-1440
    • Bi, X.1    Tong, C.2    Dokendorff, A.3    Banroft, L.4    Gallagher, L.5    Guzman-Hartman, G.6
  • 176
    • 84863012228 scopus 로고    scopus 로고
    • Decorin-mediated inhibition of colorectal cancer growth and migration is associated with E-cadherin in vitro and in mice
    • [176] Bi, X., Pohl, N.M., Yang, G.R., Gou, Y., Guzman, G., Kajdacsy-Balla, A., et al. Decorin-mediated inhibition of colorectal cancer growth and migration is associated with E-cadherin in vitro and in mice. Carcinogenesis 33 (2012), 326–330.
    • (2012) Carcinogenesis , vol.33 , pp. 326-330
    • Bi, X.1    Pohl, N.M.2    Yang, G.R.3    Gou, Y.4    Guzman, G.5    Kajdacsy-Balla, A.6
  • 177
    • 84866551287 scopus 로고    scopus 로고
    • Decorin protein core affects the global gene expression profile of the tumor microenvironment in a triple-negative orthotopic breast carcinoma xenograft model
    • [177] Buraschi, S., Neill, T., Owens, R.T., Iniguez, L.A., Purkins, G., Vadigepalli, R., et al. Decorin protein core affects the global gene expression profile of the tumor microenvironment in a triple-negative orthotopic breast carcinoma xenograft model. PLoS One, 7, 2012, e45559.
    • (2012) PLoS One , vol.7 , pp. e45559
    • Buraschi, S.1    Neill, T.2    Owens, R.T.3    Iniguez, L.A.4    Purkins, G.5    Vadigepalli, R.6
  • 178
    • 84876771337 scopus 로고    scopus 로고
    • Thrombospondin-1 receptor mediates autophagy of RAS-expressing cancer cells and triggers tumour growth inhibition
    • [178] Kalas, W., Swiderek, E., Switalska, M., Wietrzyk, J., Rak, J., Strzadala, L., Thrombospondin-1 receptor mediates autophagy of RAS-expressing cancer cells and triggers tumour growth inhibition. Anticancer Res. 33 (2013), 1429–1438.
    • (2013) Anticancer Res. , vol.33 , pp. 1429-1438
    • Kalas, W.1    Swiderek, E.2    Switalska, M.3    Wietrzyk, J.4    Rak, J.5    Strzadala, L.6
  • 179
    • 84946090815 scopus 로고    scopus 로고
    • MatrixDB, the extracellular matrix interaction database: updated content, a new navigator and expanded functionalities
    • [179] Launay, G., Salza, R., Multedo, D., Thierry-Mieg, N., Ricard-Blum, S., MatrixDB, the extracellular matrix interaction database: updated content, a new navigator and expanded functionalities. Nucleic Acids Res. 43 (2015), D321–D327.
    • (2015) Nucleic Acids Res. , vol.43 , pp. D321-D327
    • Launay, G.1    Salza, R.2    Multedo, D.3    Thierry-Mieg, N.4    Ricard-Blum, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.