메뉴 건너뛰기




Volumn , Issue , 2012, Pages 185-196

Small leucine-rich proteoglycans: Multifunctional signaling effectors

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84877715193     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (15)

References (87)
  • 1
    • 79551667507 scopus 로고    scopus 로고
    • Biglycan recruits utrophin to the sarcolemma and counters dystrophic pathology in mdx mice
    • Amenta, A. R., Yilmaz, A., Bogdanovich, S., et al. (2011). Biglycan recruits utrophin to the sarcolemma and counters dystrophic pathology in mdx mice. Proc Natl Acad Sci U S A 108, 762-767.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 762-767
    • Amenta, A.R.1    Yilmaz, A.2    Bogdanovich, S.3
  • 2
    • 0036235834 scopus 로고    scopus 로고
    • Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis
    • Ameye, L., Aria, D., Jepsen, K., Oldberg, A., Xu, T., and Young, M. F. (2002). Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis. FASEB J 16, 673-680.
    • (2002) FASEB J , vol.16 , pp. 673-680
    • Ameye, L.1    Aria, D.2    Jepsen, K.3    Oldberg, A.4    Xu, T.5    Young, M.F.6
  • 3
    • 0036744260 scopus 로고    scopus 로고
    • Mice deficient in small leucine-rich proteoglycans: Novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases
    • Ameye, L., and Young, M. F. (2002). Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases. Glycobiology 12, 107R-116R.
    • (2002) Glycobiology , vol.12 , pp. 107R-116R
    • Ameye, L.1    Young, M.F.2
  • 4
    • 33846834018 scopus 로고    scopus 로고
    • Neoplastic transformation of ciliary body epithelium is associated with loss of opticin expression
    • Assheton, D. C., Guerin, E. P., Sheridan, C. M., Bishop, P. N., and Hiscott, P. S. (2007). Neoplastic transformation of ciliary body epithelium is associated with loss of opticin expression. Br J Ophthalmol 91, 230-232.
    • (2007) Br J Ophthalmol , vol.91 , pp. 230-232
    • Assheton, D.C.1    Guerin, E.P.2    Sheridan, C.M.3    Bishop, P.N.4    Hiscott, P.S.5
  • 5
    • 69949175486 scopus 로고    scopus 로고
    • Biglycan, a danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors
    • Babelova, A., Moreth, K., Tsalastra-Greul, W., et al. (2009). Biglycan, a danger signal that activates the NLRP3 inflammasome via toll-like and P2X receptors. J Biol Chem 284, 24035-24048.
    • (2009) J Biol Chem , vol.284 , pp. 24035-24048
    • Babelova, A.1    Moreth, K.2    Tsalastra-Greul, W.3
  • 6
    • 48549105035 scopus 로고    scopus 로고
    • The role of biglycan in the heart
    • Bereczki, E., and Santha, M. (2008). The role of biglycan in the heart. Connect Tissue Res 49, 129-132.
    • (2008) Connect Tissue Res , vol.49 , pp. 129-132
    • Bereczki, E.1    Santha, M.2
  • 7
    • 34948899331 scopus 로고    scopus 로고
    • Identification of tendon stem/progenitor cells and the role of the extracellular matrix in their niche
    • Bi, Y., Ehirchiou, D., Kilts, T. M., et al. (2007). Identification of tendon stem/progenitor cells and the role of the extracellular matrix in their niche. Nat Med 13, 1219-1227.
    • (2007) Nat Med , vol.13 , pp. 1219-1227
    • Bi, Y.1    Ehirchiou, D.2    Kilts, T.M.3
  • 8
    • 0034003134 scopus 로고    scopus 로고
    • Structural macromolecules and supramolecular organisation of the vitreous gel
    • Bishop, P. N. (2000). Structural macromolecules and supramolecular organisation of the vitreous gel. Prog Retin Eye Res 19, 323-344.
    • (2000) Prog Retin Eye Res , vol.19 , pp. 323-344
    • Bishop, P.N.1
  • 9
    • 0036330632 scopus 로고    scopus 로고
    • The role of the posterior ciliary body in the biosynthesis of vitreous humour
    • Bishop, P. N., Takanosu, M., Le Goff, M., and Mayne, R. (2002). The role of the posterior ciliary body in the biosynthesis of vitreous humour. Eye (Lond) 16, 454-460.
    • (2002) Eye (Lond) , vol.16 , pp. 454-460
    • Bishop, P.N.1    Takanosu, M.2    Le Goff, M.3    Mayne, R.4
  • 10
    • 0026676859 scopus 로고
    • Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease
    • Border, W. A., Noble, N. A., Yamamoto, T., et al. (1992). Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Nature 360, 361-364.
    • (1992) Nature , vol.360 , pp. 361-364
    • Border, W.A.1    Noble, N.A.2    Yamamoto, T.3
  • 11
    • 78650584377 scopus 로고    scopus 로고
    • Identification of differentially expressed proteins in the aqueous humor of primary congenital glaucoma
    • Bouhenni, R. A., Al Shahwan, S., Morales, J., et al. (2011). Identification of differentially expressed proteins in the aqueous humor of primary congenital glaucoma. Exp Eye Res 92, 67-75.
    • (2011) Exp Eye Res , vol.92 , pp. 67-75
    • Bouhenni, R.A.1    Al Shahwan, S.2    Morales, J.3
  • 12
    • 56949083199 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy
    • Brandan, E., Cabello-Verrugio, C., and Vial, C. (2008). Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy. Matrix Biol 27, 700-708.
    • (2008) Matrix Biol , vol.27 , pp. 700-708
    • Brandan, E.1    Cabello-Verrugio, C.2    Vial, C.3
  • 13
    • 77950487962 scopus 로고    scopus 로고
    • Lumican inhibits B16F1 melanoma cell lung metastasis
    • Brezillon, S., Zeltz, C., Schneider, L., et al. (2009). Lumican inhibits B16F1 melanoma cell lung metastasis. J Physiol Pharmacol 60 (Suppl. 4), 15-22.
    • (2009) J Physiol Pharmacol , vol.60 , pp. 15-22
    • Brezillon, S.1    Zeltz, C.2    Schneider, L.3
  • 14
    • 78650674666 scopus 로고    scopus 로고
    • Decorin antagonizes Met receptor activity and down-regulates beta-catenin and Myc levels
    • Buraschi, S., Pal, N., Tyler-Rubinstein, N., Owens, R. T., Neill, T., and Iozzo, R. V. (2010). Decorin antagonizes Met receptor activity and down-regulates beta-catenin and Myc levels. J Biol Chem 285, 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
  • 15
    • 37249010513 scopus 로고    scopus 로고
    • Keratocan and lumican regulate neutrophil infiltration and corneal clarity in lipopolysaccharide-induced keratitis by direct interaction with CXCL1
    • Carlson, E. C., Lin, M., Liu, C. Y., Kao, W. W., Perez, V. L., and Pearlman, E. (2007). Keratocan and lumican regulate neutrophil infiltration and corneal clarity in lipopolysaccharide-induced keratitis by direct interaction with CXCL1. J Biol Chem 282, 35502-35509.
    • (2007) J Biol Chem , vol.282 , pp. 35502-35509
    • Carlson, E.C.1    Lin, M.2    Liu, C.Y.3    Kao, W.W.4    Perez, V.L.5    Pearlman, E.6
  • 17
    • 0033779690 scopus 로고    scopus 로고
    • Corneal opacity in lumican-null mice: Defects in collagen fibril structure and packing in the posterior stroma
    • Chakravarti, S., Petroll, W. M., Hassell, J. R., et al. (2000). Corneal opacity in lumican-null mice: defects in collagen fibril structure and packing in the posterior stroma. Invest Ophthalmol Vis Sci 41, 3365-3373.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 3365-3373
    • Chakravarti, S.1    Petroll, W.M.2    Hassell, J.R.3
  • 18
    • 0036153106 scopus 로고    scopus 로고
    • Age-related osteoporosis in biglycan-deficient mice is related to defects in bone marrow stromal cells
    • Chen, X. D., Shi, S., Xu, T., Robey, P. G., and Young, M. F. (2002). Age-related osteoporosis in biglycan-deficient mice is related to defects in bone marrow stromal cells. J Bone Miner Res 17, 331-340.
    • (2002) J Bone Miner Res , vol.17 , pp. 331-340
    • Chen, X.D.1    Shi, S.2    Xu, T.3    Robey, P.G.4    Young, M.F.5
  • 19
    • 77649275822 scopus 로고    scopus 로고
    • Biglycan protects cardiomyocytes against hypoxia/reoxygenation injury: Role of nitric oxide
    • Csont, T., Gorbe, A., Bereczki, E., et al. (2010). Biglycan protects cardiomyocytes against hypoxia/reoxygenation injury: role of nitric oxide. J Mol Cell Cardiol 48, 649-652.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 649-652
    • Csont, T.1    Gorbe, A.2    Bereczki, E.3
  • 20
    • 0034693263 scopus 로고    scopus 로고
    • Sustained down-regulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo
    • Csordas, G., Santra, M., Reed, C. C., et al. (2000). Sustained down-regulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo. J Biol Chem 275, 32879-32887.
    • (2000) J Biol Chem , vol.275 , pp. 32879-32887
    • Csordas, G.1    Santra, M.2    Reed, C.C.3
  • 21
    • 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
  • 22
    • 0029785662 scopus 로고    scopus 로고
    • Decorin-induced growth suppression is associated with up-regulation 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 up-regulation 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
  • 23
    • 77953215987 scopus 로고    scopus 로고
    • Increased biglycan in aortic valve stenosis leads to the overexpression of phospholipid transfer protein via Toll-like receptor 2
    • Derbali, H., Bosse, Y., Cote, N., et al. (2010). Increased biglycan in aortic valve stenosis leads to the overexpression of phospholipid transfer protein via Toll-like receptor 2. Am J Pathol 176, 2638-2645.
    • (2010) Am J Pathol , vol.176 , pp. 2638-2645
    • Derbali, H.1    Bosse, Y.2    Cote, N.3
  • 24
    • 36349010640 scopus 로고    scopus 로고
    • Identification of beta1 integrin as mediator of melanoma cell adhesion to lumican
    • D'Onofrio, M. F., Brezillon, S., Baranek, T., et al. (2008). Identification of beta1 integrin as mediator of melanoma cell adhesion to lumican. Biochem Biophys Res Commun 365, 266-272.
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 266-272
    • D'Onofrio, M.F.1    Brezillon, S.2    Baranek, T.3
  • 25
    • 76149122505 scopus 로고    scopus 로고
    • Biglycan and fibromodulin have essential roles in regulating chondrogenesis and extracellular matrix turnover in temporomandibular joint osteoarthritis
    • Embree, M. C., Kilts, T. M., Ono, M., et al. (2010). Biglycan and fibromodulin have essential roles in regulating chondrogenesis and extracellular matrix turnover in temporomandibular joint osteoarthritis. Am J Pathol 176, 812-826.
    • (2010) Am J Pathol , vol.176 , pp. 812-826
    • Embree, M.C.1    Kilts, T.M.2    Ono, M.3
  • 26
    • 66149095761 scopus 로고    scopus 로고
    • Decorin is a novel antagonistic ligand of the Met receptor
    • Goldoni, S., Humphries, A., Nyström, A., et al. (2009). Decorin is a novel antagonistic ligand of the Met receptor. J Cell Biol 185, 743-754.
    • (2009) J Cell Biol , vol.185 , pp. 743-754
    • Goldoni, S.1    Humphries, A.2    Nyström, A.3
  • 27
    • 57349175862 scopus 로고    scopus 로고
    • Tumor microenvironment: Modulation by decorin and related molecules harboring leucine-rich tandem motifs
    • Goldoni, S., and Iozzo, R. V. (2008). Tumor microenvironment: modulation by decorin and related molecules harboring leucine-rich tandem motifs. Int J Cancer 123, 2473-2479.
    • (2008) Int J Cancer , vol.123 , pp. 2473-2479
    • Goldoni, S.1    Iozzo, R.V.2
  • 28
    • 77955842202 scopus 로고    scopus 로고
    • The molecular basis of corneal transparency
    • Hassell, J. R., and Birk, D. E. (2010). The molecular basis of corneal transparency. Exp Eye Res 91, 326-335.
    • (2010) Exp Eye Res , vol.91 , pp. 326-335
    • Hassell, J.R.1    Birk, D.E.2
  • 29
    • 77956891991 scopus 로고    scopus 로고
    • Lumican is required for neutrophil extravasation following corneal injury and wound healing
    • Hayashi, Y., Call, M. K., Chikama, T., et al. (2010). Lumican is required for neutrophil extravasation following corneal injury and wound healing. J Cell Sci 123, 2987-2995.
    • (2010) J Cell Sci , vol.123 , pp. 2987-2995
    • Hayashi, Y.1    Call, M.K.2    Chikama, T.3
  • 30
    • 34249734812 scopus 로고    scopus 로고
    • Biglycan deficiency causes spontaneous aortic dissection and rupture in mice
    • Heegaard, A. M., Corsi, A., Danielsen, C. C., et al. (2007). Biglycan deficiency causes spontaneous aortic dissection and rupture in mice. Circulation 115, 2731-2738.
    • (2007) Circulation , vol.115 , pp. 2731-2738
    • Heegaard, A.M.1    Corsi, A.2    Danielsen, C.C.3
  • 31
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta
    • Hildebrand, A., Romaris, M., Rasmussen, L. M., et al. (1994). Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. Biochem J 302 (Pt 2), 527-534.
    • (1994) Biochem J , vol.302 , Issue.PT 2 , pp. 527-534
    • Hildebrand, A.1    Romaris, M.2    Rasmussen, L.M.3
  • 32
    • 70149091269 scopus 로고    scopus 로고
    • Decorin suppresses prostate tumor growth through inhibition of epidermal growth factor and androgen receptor pathways
    • Hu, Y., Sun, H., Owens, R. T., et al. (2009). Decorin suppresses prostate tumor growth through inhibition of epidermal growth factor and androgen receptor pathways. Neoplasia 1 1, 1042-1053.
    • (2009) Neoplasia 1 , vol.1 , pp. 1042-1053
    • Hu, Y.1    Sun, H.2    Owens, R.T.3
  • 33
    • 57449103799 scopus 로고    scopus 로고
    • The potential functional interaction of biglycan and WISP-1 in controlling differentiation and proliferation of osteogenic cells
    • Inkson, C. A., Ono, M., Bi, Y., Kuznetsov, S. A., Fisher, L. W., and Young, M. F. (2009). The potential functional interaction of biglycan and WISP-1 in controlling differentiation and proliferation of osteogenic cells. Cells Tissues Organs 189, 153-157.
    • (2009) Cells Tissues Organs , vol.189 , pp. 153-157
    • Inkson, C.A.1    Ono, M.2    Bi, Y.3    Kuznetsov, S.A.4    Fisher, L.W.5    Young, M.F.6
  • 34
    • 0033582415 scopus 로고    scopus 로고
    • Decorin is a biological ligand for the epidermal growth factor receptor
    • Iozzo, R. V., Moscatello, D. K., McQuillan, D. J., and Eichstetter, I. (1999). Decorin is a biological ligand for the epidermal growth factor receptor. J Biol Chem 274, 4489-4492.
    • (1999) J Biol Chem , vol.274 , pp. 4489-4492
    • Iozzo, R.V.1    Moscatello, D.K.2    McQuillan, D.J.3    Eichstetter, I.4
  • 35
    • 79957605232 scopus 로고    scopus 로고
    • Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
    • Iozzo, R. V., and Sanderson, R. D. (2011). Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J Cell Mol Med 15, 1013-1031.
    • (2011) J Cell Mol Med , vol.15 , pp. 1013-1031
    • Iozzo, R.V.1    Sanderson, R.D.2
  • 36
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • Iozzo, R. V., and Schaefer, L. (2010). Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans. FEBS J 277, 3864-3875.
    • (2010) FEBS J , vol.277 , pp. 3864-3875
    • Iozzo, R.V.1    Schaefer, L.2
  • 37
    • 0030744592 scopus 로고    scopus 로고
    • Characterization of epiphycan, a small proteoglycan with a leucine-rich repeat core protein
    • Johnson, H. J., Rosenberg, L., Choi, H. U., Garza, S., Hook, M., and Neame, P. J. (1997). Characterization of epiphycan, a small proteoglycan with a leucine-rich repeat core protein. J Biol Chem 272, 18709-18717.
    • (1997) J Biol Chem , vol.272 , pp. 18709-18717
    • Johnson, H.J.1    Rosenberg, L.2    Choi, H.U.3    Garza, S.4    Hook, M.5    Neame, P.J.6
  • 40
    • 0034979153 scopus 로고    scopus 로고
    • Proteoglycans decorin and biglycan differentially modulate TGF-beta-mediated fibrotic responses in the lung
    • Kolb, M., Margetts, P. J., Sime, P. J., and Gauldie, J. (2001). Proteoglycans decorin and biglycan differentially modulate TGF-beta-mediated fibrotic responses in the lung. Am J Physiol Lung Cell Mol Physiol 280, L1327-1334.
    • (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
  • 41
    • 79952443665 scopus 로고    scopus 로고
    • Colocalisation of plasma derived apo B lipoproteins with cerebral proteoglycans in a transgenic-amyloid model of Alzheimer's disease
    • Lam, V., Takechi, R., Pallebage-Gamarallage, M. M., Galloway, S., and Mamo, J. C. (2011). Colocalisation of plasma derived apo B lipoproteins with cerebral proteoglycans in a transgenic-amyloid model of Alzheimer's disease. Neurosci Lett 492, 160-164.
    • (2011) Neurosci Lett , vol.492 , pp. 160-164
    • Lam, V.1    Takechi, R.2    Pallebage-Gamarallage, M.M.3    Galloway, S.4    Mamo, J.C.5
  • 42
    • 69949142985 scopus 로고    scopus 로고
    • Extracellular matrix lumican deposited on the surface of neutrophils promotes migration by binding to beta2 integrin
    • Lee, S., Bowrin, K., Hamad, A. R., and Chakravarti, S. (2009). Extracellular matrix lumican deposited on the surface of neutrophils promotes migration by binding to beta2 integrin. J Biol Chem 284, 23662-23669.
    • (2009) J Biol Chem , vol.284 , pp. 23662-23669
    • Lee, S.1    Bowrin, K.2    Hamad, A.R.3    Chakravarti, S.4
  • 43
    • 4944233738 scopus 로고    scopus 로고
    • Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar
    • Li, Y., Aoki, T., Mori, Y., et al. (2004). Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar. Cancer Res 64, 7058-7064.
    • (2004) Cancer Res , vol.64 , pp. 7058-7064
    • Li, Y.1    Aoki, T.2    Mori, Y.3
  • 44
    • 53549119130 scopus 로고    scopus 로고
    • Hyperelongated biglycan: The surreptitious initiator of atherosclerosis
    • Little, P. J., Osman, N., and O'Brien, K. D. (2008). Hyperelongated biglycan: the surreptitious initiator of atherosclerosis. Curr Opin Lipidol 19, 448-454.
    • (2008) Curr Opin Lipidol , vol.19 , pp. 448-454
    • Little, P.J.1    Osman, N.2    O'Brien, K.D.3
  • 45
    • 83555161650 scopus 로고    scopus 로고
    • Extracellular matrix protein lumican regulates inflammation in a mouse model of colitis
    • Lohr, K., Sardana, H., Lee, S., et al. (2011). Extracellular matrix protein lumican regulates inflammation in a mouse model of colitis. Inflamm Bowel Dis 18 (1), 143-151.
    • (2011) Inflamm Bowel Dis , vol.18 , Issue.1 , pp. 143-151
    • Lohr, K.1    Sardana, H.2    Lee, S.3
  • 46
    • 34047236557 scopus 로고    scopus 로고
    • Novel mutations in the small leucine-rich repeat protein/proteoglycan (SLRP) genes in high myopia
    • Majava, M., Bishop, P. N., Hagg, P., et al. (2007). Novel mutations in the small leucine-rich repeat protein/proteoglycan (SLRP) genes in high myopia. Hum Mutat 28, 336-344.
    • (2007) Hum Mutat , vol.28 , pp. 336-344
    • Majava, M.1    Bishop, P.N.2    Hagg, P.3
  • 47
    • 13544251390 scopus 로고    scopus 로고
    • Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes
    • Mayr, C., Bund, D., Schlee, M., et al. (2005). Fibromodulin as a novel tumor-associated antigen (TAA) in chronic lymphocytic leukemia (CLL), which allows expansion of specific CD8+ autologous T lymphocytes. Blood 105, 1566-1573.
    • (2005) Blood , vol.105 , pp. 1566-1573
    • Mayr, C.1    Bund, D.2    Schlee, M.3
  • 48
    • 79955775556 scopus 로고    scopus 로고
    • Deficiency of biglycan causes cardiac fibroblasts to differentiate into a myofibroblast phenotype
    • Melchior-Becker, A., Dai, G., Ding, Z., et al. (2011). Deficiency of biglycan causes cardiac fibroblasts to differentiate into a myofibroblast phenotype. J Biol Chem 286, 17365-17375.
    • (2011) J Biol Chem , vol.286 , pp. 17365-17375
    • Melchior-Becker, A.1    Dai, G.2    Ding, Z.3
  • 49
    • 72449168557 scopus 로고    scopus 로고
    • Decorin deficiency in diabetic mice: Aggravation of nephropathy due to overexpression of profibrotic factors, enhanced apoptosis and mononuclear cell infiltration
    • Merline, R., Lazaroski, S., Babelova, A., et al. (2009). Decorin deficiency in diabetic mice: aggravation of nephropathy due to overexpression of profibrotic factors, enhanced apoptosis and mononuclear cell infiltration. J Physiol Pharmacol 60 (Suppl. 4), 5-13.
    • (2009) J Physiol Pharmacol , vol.60 , pp. 5-13
    • Merline, R.1    Lazaroski, S.2    Babelova, A.3
  • 50
    • 81455155655 scopus 로고    scopus 로고
    • Signaling by the matrix proteoglycan decorin controls inflammation and cancer through PDCD4 and MicroRNA-21
    • Merline, R., Moreth, K., Beckmann, J., et al. (2011). Signaling by the matrix proteoglycan decorin controls inflammation and cancer through PDCD4 and MicroRNA-21. Sci Signal, 4, ra75.
    • (2011) Sci Signal , vol.4 , pp. ra75
    • Merline, R.1    Moreth, K.2    Beckmann, J.3
  • 51
    • 20444406861 scopus 로고    scopus 로고
    • Fibromodulin, an extracellular matrix protein: Characterization of its unique gene and protein expression in B-cell chronic lymphocytic leukemia and mantle cell lymphoma
    • Mikaelsson, E., Danesh-Manesh, A. H., Luppert, A., et al. (2005). Fibromodulin, an extracellular matrix protein: characterization of its unique gene and protein expression in B-cell chronic lymphocytic leukemia and mantle cell lymphoma. Blood 105, 4828-4835.
    • (2005) Blood , vol.105 , pp. 4828-4835
    • Mikaelsson, E.1    Danesh-Manesh, A.H.2    Luppert, A.3
  • 52
    • 45449087754 scopus 로고    scopus 로고
    • Identification of opticin, a member of the small leucine-rich repeat proteoglycan family, in human articular tissues: A novel target for MMP-13 in osteoarthritis
    • Monfort, J., Tardif, G., Roughley, P., et al. (2008). Identification of opticin, a member of the small leucine-rich repeat proteoglycan family, in human articular tissues: a novel target for MMP-13 in osteoarthritis. Osteoarthritis Cartilage 16, 749-755.
    • (2008) Osteoarthritis Cartilage , vol.16 , pp. 749-755
    • Monfort, J.1    Tardif, G.2    Roughley, P.3
  • 53
    • 78649856319 scopus 로고    scopus 로고
    • The proteoglycan biglycan regulates expression of the B cell chemoattractant CXCL13 and aggravates murine lupus nephritis
    • Moreth, K., Brodbeck, R., Babelova, A., et al. (2010). The proteoglycan biglycan regulates expression of the B cell chemoattractant CXCL13 and aggravates murine lupus nephritis. J Clin Invest 120, 4251-4272.
    • (2010) J Clin Invest , vol.120 , pp. 4251-4272
    • Moreth, K.1    Brodbeck, R.2    Babelova, A.3
  • 54
    • 84861871896 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation
    • Moreth, K., Iozzo, R. V., and Schaefer, L. (2012). Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation. Cell Cycle 11, 2084-2091.
    • (2012) Cell Cycle , vol.11 , pp. 2084-2091
    • Moreth, K.1    Iozzo, R.V.2    Schaefer, L.3
  • 55
    • 0032518407 scopus 로고    scopus 로고
    • Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor
    • Moscatello, D. K., Santra, M., Mann, D. M., McQuillan, D. J., Wong, A. J., and Iozzo, R. V. (1998). Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor. J Clin Invest 101, 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
  • 56
    • 72149096510 scopus 로고    scopus 로고
    • Phenotypic characterization of epiphycandeficient and epiphycan/biglycan double-deficient mice
    • Nuka, S., Zhou, W., Henry, S. P., et al. (2010). Phenotypic characterization of epiphycandeficient and epiphycan/biglycan double-deficient mice. Osteoarthritis Cartilage 18, 88-96.
    • (2010) Osteoarthritis Cartilage , vol.18 , pp. 88-96
    • Nuka, S.1    Zhou, W.2    Henry, S.P.3
  • 57
    • 35348839617 scopus 로고    scopus 로고
    • Collagen-binding proteoglycan fibromodulin can determine stroma matrix structure and fluid balance in experimental carcinoma
    • Oldberg, A., Kalamajski, S., Salnikov, A. V., et al. (2007). Collagen-binding proteoglycan fibromodulin can determine stroma matrix structure and fluid balance in experimental carcinoma. Proc Natl Acad Sci U S A 104, 13966-13971.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13966-13971
    • Oldberg, A.1    Kalamajski, S.2    Salnikov, A.V.3
  • 59
    • 1942453405 scopus 로고    scopus 로고
    • Immunolocalisation of opticin in the human eye
    • Ramesh, S., Bonshek, R. E., and Bishop, P. N. (2004). Immunolocalisation of opticin in the human eye. Br J Ophthalmol 88, 697-702.
    • (2004) Br J Ophthalmol , vol.88 , pp. 697-702
    • Ramesh, S.1    Bonshek, R.E.2    Bishop, P.N.3
  • 60
    • 0034695439 scopus 로고    scopus 로고
    • Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix
    • Reardon, A. J., Le Goff, M., Briggs, M. D., et al. (2000). Identification in vitreous and molecular cloning of opticin, a novel member of the family of leucine-rich repeat proteins of the extracellular matrix. J Biol Chem 275, 2123-2129.
    • (2000) J Biol Chem , vol.275 , pp. 2123-2129
    • Reardon, A.J.1    Le Goff, M.2    Briggs, M.D.3
  • 61
    • 0141763811 scopus 로고    scopus 로고
    • The role of decorin in collagen fibrillogenesis and skin homeostasis
    • Reed, C. C., and Iozzo, R. V. (2002). The role of decorin in collagen fibrillogenesis and skin homeostasis. Glycoconj J 19, 249-255.
    • (2002) Glycoconj J , vol.19 , pp. 249-255
    • Reed, C.C.1    Iozzo, R.V.2
  • 62
    • 13944249920 scopus 로고    scopus 로고
    • Decorin prevents metastatic spreading of breast cancer
    • Reed, C. C., Waterhouse, A., Kirby, S., et al. (2005). Decorin prevents metastatic spreading of breast cancer. Oncogene 24, 1104-1110.
    • (2005) Oncogene , vol.24 , pp. 1104-1110
    • Reed, C.C.1    Waterhouse, A.2    Kirby, S.3
  • 63
    • 33845407527 scopus 로고    scopus 로고
    • The structure and function of cartilage proteoglycans
    • Roughley, P. J. (2006). The structure and function of cartilage proteoglycans. Eur Cell Mater 12, 92-101.
    • (2006) Eur Cell Mater , vol.12 , pp. 92-101
    • Roughley, P.J.1
  • 64
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope
    • Santra, M., Reed, C. C., and Iozzo, R. V. (2002). Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope. J Biol Chem 277, 35671-35681.
    • (2002) J Biol Chem , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 65
    • 79960119978 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans in kidney disease
    • Schaefer, L. (2011). Small leucine-rich proteoglycans in kidney disease. J Am Soc Nephrol 22, 1200-1207.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 1200-1207
    • Schaefer, L.1
  • 66
    • 23644456849 scopus 로고    scopus 로고
    • The matrix component biglycan is proinflammatory and signals through Toll-like receptors 4 and 2 in macrophages
    • Schaefer, L., Babelova, A., Kiss, E., et al. (2005). The matrix component biglycan is proinflammatory and signals through Toll-like receptors 4 and 2 in macrophages. J Clin Invest 115, 2223-2233.
    • (2005) J Clin Invest , vol.115 , pp. 2223-2233
    • Schaefer, L.1    Babelova, A.2    Kiss, E.3
  • 67
    • 52049122865 scopus 로고    scopus 로고
    • Biological functions of the small leucine-rich proteoglycans: From genetics to signal transduction
    • Schaefer, L., and Iozzo, R. V. (2008). Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction. J Biol Chem 283, 21305-21309.
    • (2008) J Biol Chem , vol.283 , pp. 21305-21309
    • Schaefer, L.1    Iozzo, R.V.2
  • 68
    • 84858450953 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation
    • Schaefer, L., and Iozzo, R. V. (2012). Small leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation. Curr Opin Genet Dev 22, 56-57.
    • (2012) Curr Opin Genet Dev , vol.22 , pp. 56-57
    • Schaefer, L.1    Iozzo, R.V.2
  • 69
    • 0036118493 scopus 로고    scopus 로고
    • Absence of decorin adversely influences tubulointerstitial fibrosis of the obstructed kidney by enhanced apoptosis and increased inflammatory reaction
    • Schaefer, L., Macakova, K., Raslik, I., et al. (2002). Absence of decorin adversely influences tubulointerstitial fibrosis of the obstructed kidney by enhanced apoptosis and increased inflammatory reaction. Am J Pathol 160, 1181-1191.
    • (2002) Am J Pathol , vol.160 , pp. 1181-1191
    • Schaefer, L.1    Macakova, K.2    Raslik, I.3
  • 70
    • 33847051740 scopus 로고    scopus 로고
    • Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and mammalian target of rapamycin
    • Schaefer, L., Tsalastra, W., Babelova, A., et al. (2007). Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and mammalian target of rapamycin. Am J Pathol 170, 301-315.
    • (2007) Am J Pathol , vol.170 , pp. 301-315
    • Schaefer, L.1    Tsalastra, W.2    Babelova, A.3
  • 71
    • 18144431289 scopus 로고    scopus 로고
    • Decorin, a novel player in the insulin-like growth factor system
    • Schonherr, E., Sunderkotter, C., Iozzo, R. V., and Schaefer, L. (2005). Decorin, a novel player in the insulin-like growth factor system. J Biol Chem 280, 15767-15772.
    • (2005) J Biol Chem , vol.280 , pp. 15767-15772
    • Schonherr, E.1    Sunderkotter, C.2    Iozzo, R.V.3    Schaefer, L.4
  • 72
    • 33748755116 scopus 로고    scopus 로고
    • Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation
    • Seidler, D. G., Goldoni, S., Agnew, C., et al. (2006). Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation. J Biol Chem 281, 26408-26418.
    • (2006) J Biol Chem , vol.281 , pp. 26408-26418
    • Seidler, D.G.1    Goldoni, S.2    Agnew, C.3
  • 73
    • 59249103181 scopus 로고    scopus 로고
    • Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation
    • Sjoberg, A. P., Manderson, G. A., Morgelin, M., Day, A. J., Heinegard, D., and Blom, A. M. (2009). Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation. Mol Immunol 46, 830-839.
    • (2009) Mol Immunol , vol.46 , pp. 830-839
    • Sjoberg, A.P.1    Manderson, G.A.2    Morgelin, M.3    Day, A.J.4    Heinegard, D.5    Blom, A.M.6
  • 74
    • 0033899374 scopus 로고    scopus 로고
    • Differential expression of fibromodulin, a transforming growth factor-beta modulator, in fetal skin development and scarless repair
    • Soo, C., Hu, F. Y., Zhang, X., et al. (2000). Differential expression of fibromodulin, a transforming growth factor-beta modulator, in fetal skin development and scarless repair. Am J Pathol 157, 423-433.
    • (2000) Am J Pathol , vol.157 , pp. 423-433
    • Soo, C.1    Hu, F.Y.2    Zhang, X.3
  • 75
    • 0040436000 scopus 로고    scopus 로고
    • Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon
    • Svensson, L., Aszodi, A., Reinholt, F. P., Fassler, R., Heinegard, D., and Oldberg, A. (1999). Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J Biol Chem 274, 9636-9647.
    • (1999) J Biol Chem , vol.274 , pp. 9636-9647
    • Svensson, L.1    Aszodi, A.2    Reinholt, F.P.3    Fassler, R.4    Heinegard, D.5    Oldberg, A.6
  • 76
    • 0037364506 scopus 로고    scopus 로고
    • In vivo selective and distant killing of cancer cells using adenovirus-mediated decorin gene transfer
    • Tralhao, J. G., Schaefer, L., Micegova, M., et al. (2003). In vivo selective and distant killing of cancer cells using adenovirus-mediated decorin gene transfer. FASEB J 17, 464-466.
    • (2003) FASEB J , vol.17 , pp. 464-466
    • Tralhao, J.G.1    Schaefer, L.2    Micegova, M.3
  • 77
    • 79959865250 scopus 로고    scopus 로고
    • Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity
    • Vial, C., Gutierrez, J., Santander, C., Cabrera, D., and Brandan, E. (2011). Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity. J Biol Chem 286, 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
  • 78
    • 1642421036 scopus 로고    scopus 로고
    • Lumican suppresses cell proliferation and aids Fas-Fas ligand mediated apoptosis: Implications in the cornea
    • Vij, N., Roberts, L., Joyce, S., and Chakravarti, S. (2004). Lumican suppresses cell proliferation and aids Fas-Fas ligand mediated apoptosis: implications in the cornea. Exp Eye Res 78, 957-971.
    • (2004) Exp Eye Res , vol.78 , pp. 957-971
    • Vij, N.1    Roberts, L.2    Joyce, S.3    Chakravarti, S.4
  • 79
    • 11144256156 scopus 로고    scopus 로고
    • Lumican regulates corneal inflammatory responses by modulating Fas-Fas ligand signaling
    • Vij, N., Roberts, L., Joyce, S., and Chakravarti, S. (2005). Lumican regulates corneal inflammatory responses by modulating Fas-Fas ligand signaling. Invest Ophthalmol Vis Sci 46, 88-95.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 88-95
    • Vij, N.1    Roberts, L.2    Joyce, S.3    Chakravarti, S.4
  • 80
    • 2442570675 scopus 로고    scopus 로고
    • The small leucine-rich proteoglycan lumican inhibits melanoma progression
    • Vuillermoz, B., Khoruzhenko, A., D'Onofrio, M. F., et al. (2004). The small leucine-rich proteoglycan lumican inhibits melanoma progression. Exp Cell Res 296, 294-306.
    • (2004) Exp Cell Res , vol.296 , pp. 294-306
    • Vuillermoz, B.1    Khoruzhenko, A.2    D'Onofrio, M.F.3
  • 81
    • 40549086587 scopus 로고    scopus 로고
    • Biglycan is required for adaptive remodeling after myocardial infarction
    • Westermann, D., Mersmann, J., Melchior, A., et al. (2008). Biglycan is required for adaptive remodeling after myocardial infarction. Circulation 117, 1269-1276.
    • (2008) Circulation , vol.117 , pp. 1269-1276
    • Westermann, D.1    Mersmann, J.2    Melchior, A.3
  • 82
    • 34548861475 scopus 로고    scopus 로고
    • A novel role of the lumican core protein in bacterial lipopolysaccharide-induced innate immune response
    • Wu, F., Vij, N., Roberts, L., Lopez-Briones, S., Joyce, S., and Chakravarti, S. (2007). A novel role of the lumican core protein in bacterial lipopolysaccharide-induced innate immune response. J Biol Chem 282, 26409-26417.
    • (2007) J Biol Chem , vol.282 , pp. 26409-26417
    • Wu, F.1    Vij, N.2    Roberts, L.3    Lopez-Briones, S.4    Joyce, S.5    Chakravarti, S.6
  • 83
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-beta by the proteoglycan decorin
    • Yamaguchi, Y., Mann, D. M., and Ruoslahti, E. (1990). Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature 346, 281-284.
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 84
    • 0030731947 scopus 로고    scopus 로고
    • Characterization and expression of the mouse lumican gene
    • Ying, S., Shiraishi, A., Kao, C. W., et al. (1997). Characterization and expression of the mouse lumican gene. J Biol Chem 272, 30306-30313.
    • (1997) J Biol Chem , vol.272 , pp. 30306-30313
    • Ying, S.1    Shiraishi, A.2    Kao, C.W.3
  • 85
    • 77956884942 scopus 로고    scopus 로고
    • Lumican inhibits cell migration through alpha2beta1 integrin
    • Zeltz, C., Brezillon, S., Kapyla, J., et al. (2010). Lumican inhibits cell migration through alpha2beta1 integrin. Exp Cell Res 316, 2922-2931.
    • (2010) Exp Cell Res , vol.316 , pp. 2922-2931
    • Zeltz, C.1    Brezillon, S.2    Kapyla, J.3
  • 86
    • 79951508683 scopus 로고    scopus 로고
    • Delayed wound closure infibromodulin-deficient mice is associated with increased TGF-beta3 signaling
    • Zheng, Z., Nguyen, C., Zhang, X., et al. (2011). Delayed wound closure infibromodulin-deficient mice is associated with increased TGF-beta3 signaling. J Invest Dermatol 131, 769-778.
    • (2011) J Invest Dermatol , vol.131 , pp. 769-778
    • Zheng, Z.1    Nguyen, C.2    Zhang, X.3
  • 87
    • 25444503249 scopus 로고    scopus 로고
    • Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis
    • Zhu, J. X., Goldoni, S., Bix, G., et al. (2005). Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis. J Biol Chem 280, 32468-32479.
    • (2005) J Biol Chem , vol.280 , pp. 32468-32479
    • Zhu, J.X.1    Goldoni, S.2    Bix, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.