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Volumn 280, Issue 10, 2013, Pages 2165-2179

Biological interplay between proteoglycans and their innate immune receptors in inflammation

Author keywords

biglycan; decorin; hyaluronan; lumican; versican

Indexed keywords

BIGLYCAN; DECORIN; GLYCOSAMINOGLYCAN; HYALURONIC ACID; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 10; INTERLEUKIN 1BETA; LEUCINE; LUMICAN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEOGLYCAN; PURINERGIC P2X4 RECEPTOR; PURINERGIC P2X7 RECEPTOR; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TRANSFORMING GROWTH FACTOR BETA1; VERSICAN;

EID: 84877703267     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12145     Document Type: Review
Times cited : (210)

References (156)
  • 1
    • 78649526394 scopus 로고    scopus 로고
    • Sterile inflammation: Sensing and reacting to damage
    • Chen GY, &, Nunez G, (2010) Sterile inflammation: sensing and reacting to damage. Nat Rev Immunol 10, 826-837.
    • (2010) Nat Rev Immunol , vol.10 , pp. 826-837
    • Chen, G.Y.1    Nunez, G.2
  • 2
    • 77955383770 scopus 로고    scopus 로고
    • DAMPening inflammation by modulating TLR signalling
    • doi: 10.1155/2010/672395.
    • Piccinini AM, &, Midwood KS, (2010) DAMPening inflammation by modulating TLR signalling. Mediators Inflamm, doi: 10.1155/2010/672395.
    • (2010) Mediators Inflamm
    • Piccinini, A.M.1    Midwood, K.S.2
  • 3
    • 84865299726 scopus 로고    scopus 로고
    • PAMPs and DAMPs: Signals that spur autophagy and immunity
    • Tang D, Kang R, Coyne CB, Zeh HJ, &, Lotze MT, (2012) PAMPs and DAMPs: signals that spur autophagy and immunity. Immunol Rev 249, 158-175.
    • (2012) Immunol Rev , vol.249 , pp. 158-175
    • Tang, D.1    Kang, R.2    Coyne, C.B.3    Zeh, H.J.4    Lotze, M.T.5
  • 4
    • 84859401430 scopus 로고    scopus 로고
    • Cancer and inflammation: An old intuition with rapidly evolving new concepts
    • Trinchieri G, (2012) Cancer and inflammation: an old intuition with rapidly evolving new concepts. Annu Rev Immunol 30, 677-706.
    • (2012) Annu Rev Immunol , vol.30 , pp. 677-706
    • Trinchieri, G.1
  • 5
    • 84858450953 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans, at the crossroad of cancer growth and inflammation
    • Schaefer L, &, Iozzo RV, (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
  • 6
    • 84855163540 scopus 로고    scopus 로고
    • Intrinsic danger: Activation of Toll-like receptors in rheumatoid arthritis
    • Goh FG, &, Midwood KS, (2012) Intrinsic danger: activation of Toll-like receptors in rheumatoid arthritis. Rheumatology (Oxford) 51, 7-23.
    • (2012) Rheumatology (Oxford) , vol.51 , pp. 7-23
    • Goh, F.G.1    Midwood, K.S.2
  • 7
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, &, Akira S, (2010) Pattern recognition receptors and inflammation. Cell 140, 805-820.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 8
    • 80052740181 scopus 로고    scopus 로고
    • Innate immune recognition receptors and damage-associated molecular patterns in plaque inflammation
    • Lundberg AM, &, Yan ZQ, (2011) Innate immune recognition receptors and damage-associated molecular patterns in plaque inflammation. Curr Opin Lipidol 22, 343-349.
    • (2011) Curr Opin Lipidol , vol.22 , pp. 343-349
    • Lundberg, A.M.1    Yan, Z.Q.2
  • 9
    • 84861474688 scopus 로고    scopus 로고
    • Signaling in innate immunity and inflammation
    • doi: 10.1101/cshperspect.a006049.
    • Newton K, &, Dixit VM, (2012) Signaling in innate immunity and inflammation. Cold Spring Harb Perspect Biol, doi: 10.1101/cshperspect.a006049.
    • (2012) Cold Spring Harb Perspect Biol
    • Newton, K.1    Dixit, V.M.2
  • 10
    • 77954005130 scopus 로고    scopus 로고
    • Endogenous ligands of TLR2 and TLR4: Agonists or assistants?
    • Erridge C, (2010) Endogenous ligands of TLR2 and TLR4: agonists or assistants? J Leukoc Biol 87, 989-999.
    • (2010) J Leukoc Biol , vol.87 , pp. 989-999
    • Erridge, C.1
  • 11
    • 48749128643 scopus 로고    scopus 로고
    • Structures of the toll-like receptor family and its ligand complexes
    • Jin MS, &, Lee JO, (2008) Structures of the toll-like receptor family and its ligand complexes. Immunity 29, 182-191.
    • (2008) Immunity , vol.29 , pp. 182-191
    • Jin, M.S.1    Lee, J.O.2
  • 13
    • 73349095696 scopus 로고    scopus 로고
    • CD14 but not MD2 transmit signals from DAMP
    • Chun KH, &, Seong SY, (2010) CD14 but not MD2 transmit signals from DAMP. Int Immunopharmacol 10, 98-106.
    • (2010) Int Immunopharmacol , vol.10 , pp. 98-106
    • Chun, K.H.1    Seong, S.Y.2
  • 14
    • 77649180575 scopus 로고    scopus 로고
    • TLRs and chronic inflammation
    • Ospelt C, &, Gay S, (2010) TLRs and chronic inflammation. Int J Biochem Cell Biol 42, 495-505.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 495-505
    • Ospelt, C.1    Gay, S.2
  • 21
    • 0029952227 scopus 로고    scopus 로고
    • Hyaluronan fragments activate an NF-κB/I-κBα autoregulatory loop in murine macrophages
    • DOI 10.1084/jem.183.5.2373
    • Noble PW, McKee CM, Cowman M, &, Shin HS, (1996) Hyaluronan fragments activate an NF-kappa B/I-kappa B alpha autoregulatory loop in murine macrophages. J Exp Med 183, 2373-2378. (Pubitemid 26158930)
    • (1996) Journal of Experimental Medicine , vol.183 , Issue.5 , pp. 2373-2378
    • Noble, P.W.1    McKee, C.M.2    Cowman, M.3    Shin, H.S.4
  • 22
    • 67650502739 scopus 로고    scopus 로고
    • Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease
    • Midwood K, Sacre S, Piccinini AM, Inglis J, Trebaul A, Chan E, Drexler S, Sofat N, Kashiwagi M, Orend G, et al,. (2009) Tenascin-C is an endogenous activator of Toll-like receptor 4 that is essential for maintaining inflammation in arthritic joint disease. Nat Med 15, 774-780.
    • (2009) Nat Med , vol.15 , pp. 774-780
    • Midwood, K.1    Sacre, S.2    Piccinini, A.M.3    Inglis, J.4    Trebaul, A.5    Chan, E.6    Drexler, S.7    Sofat, N.8    Kashiwagi, M.9    Orend, G.10
  • 23
    • 0037094084 scopus 로고    scopus 로고
    • Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by toll-like receptor 4
    • Johnson GB, Brunn GJ, Kodaira Y, &, Platt JL, (2002) Receptor-mediated monitoring of tissue well-being via detection of soluble heparan sulfate by Toll-like receptor 4. J Immunol 168, 5233-5239. (Pubitemid 34495991)
    • (2002) Journal of Immunology , vol.168 , Issue.10 , pp. 5233-5239
    • Johnson, G.B.1    Brunn, G.J.2    Kodaira, Y.3    Platt, J.L.4
  • 24
    • 77949683133 scopus 로고    scopus 로고
    • Extracellular matrix molecules: Endogenous danger signals as new drug targets in kidney diseases
    • Schaefer L, (2010) Extracellular matrix molecules: endogenous danger signals as new drug targets in kidney diseases. Curr Opin Pharmacol 10, 185-190.
    • (2010) Curr Opin Pharmacol , vol.10 , pp. 185-190
    • Schaefer, L.1
  • 25
    • 84861871896 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans orchestrate receptor crosstalk during inflammation
    • Moreth K, Iozzo RV, &, 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
  • 26
    • 77957221743 scopus 로고    scopus 로고
    • The impact of the extracellular matrix on inflammation
    • Sorokin L, (2010) The impact of the extracellular matrix on inflammation. Nat Rev Immunol 10, 712-723.
    • (2010) Nat Rev Immunol , vol.10 , pp. 712-723
    • Sorokin, L.1
  • 27
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • DOI 10.1146/annurev.biochem.67.1.609
    • Iozzo RV, (1998) Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 67, 609-652. (Pubitemid 28411140)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 28
    • 72449147268 scopus 로고    scopus 로고
    • Proteoglycans: From structural compounds to signaling molecules
    • Schaefer L, &, Schaefer RM, (2010) Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res 339, 237-246.
    • (2010) Cell Tissue Res , vol.339 , pp. 237-246
    • Schaefer, L.1    Schaefer, R.M.2
  • 29
    • 84877715706 scopus 로고    scopus 로고
    • Introduction to proteoglycans: Structure, pathobiology and signaling
    • In (Karamanos N.K. ed.), Walter de Gruyter, Berlin/Boston.
    • Schaefer L, (2012) Introduction to proteoglycans: structure, pathobiology and signaling. In Extracellular Matrix: Pathobiology and Signaling (, Karamanos NK, ed.), pp. 135-140. Walter de Gruyter, Berlin/Boston.
    • (2012) Extracellular Matrix: Pathobiology and Signaling , pp. 135-140
    • Schaefer, L.1
  • 31
    • 0033812683 scopus 로고    scopus 로고
    • Hyaluronan: A multifunctional, megaDalton, stealth molecule
    • Lee JY, &, Spicer AP, (2000) Hyaluronan: a multifunctional, megaDalton, stealth molecule. Curr Opin Cell Biol 12, 581-586.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 581-586
    • Lee, J.Y.1    Spicer, A.P.2
  • 32
    • 48749106343 scopus 로고    scopus 로고
    • Simple primary structure, complex turnover regulation and multiple roles of hyaluronan
    • Itano N, (2008) Simple primary structure, complex turnover regulation and multiple roles of hyaluronan. J Biochem 144, 131-137.
    • (2008) J Biochem , vol.144 , pp. 131-137
    • Itano, N.1
  • 33
    • 0025110119 scopus 로고
    • Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues
    • Bianco P, Fisher LW, Young MF, Termine JD, &, Robey PG, (1990) Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues. J Histochem Cytochem 38, 1549-1563. (Pubitemid 20346965)
    • (1990) Journal of Histochemistry and Cytochemistry , vol.38 , Issue.11 , pp. 1549-1563
    • Bianco, P.1    Fisher, L.W.2    Young, M.F.3    Termine, J.D.4    Robey, P.G.5
  • 34
    • 0024596126 scopus 로고
    • Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-Sepharose chromatography
    • Choi HU, Johnson TL, Pal S, Tang LH, Rosenberg L, &, Neame PJ, (1989) Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography. J Biol Chem 264, 2876-2884. (Pubitemid 19057783)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.5 , pp. 2876-2884
    • Choi, H.U.1    Johnson, T.L.2    Pal, S.3    Tang, L.-H.4    Rosenberg, L.5    Neame, P.J.6
  • 35
    • 0025357497 scopus 로고
    • Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively
    • DOI 10.1016/0888-7543(90)90560-H
    • McBride OW, Fisher LW, &, Young MF, (1990) Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively. Genomics 6, 219-225. (Pubitemid 20164189)
    • (1990) Genomics , vol.6 , Issue.2 , pp. 219-225
    • McBride, O.W.1
  • 36
    • 0024550294 scopus 로고
    • Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species
    • Fisher LW, Termine JD, &, Young MF, (1989) Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species. J Biol Chem 264, 4571-4576. (Pubitemid 19081361)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.8 , pp. 4571-4576
    • Fisher, L.W.1    Termine, J.D.2    Young, M.F.3
  • 37
    • 0020540538 scopus 로고
    • Proteoglycans of developing bone
    • Fisher LW, Termine JD, Dejter SW Jr, Whitson SW, Yanagishita M, Kimura JH, Hascall VC, Kleinman HK, Hassell JR, &, Nilsson B, (1983) Proteoglycans of developing bone. J Biol Chem 258, 6588-6594. (Pubitemid 13106831)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.10 , pp. 6588-6594
    • Fisher, L.W.1    Termine, J.D.2    Dejter Jr., S.W.3
  • 38
    • 0027275296 scopus 로고
    • Identification and characterization of glycanated and non-glycanated of biglycan and decorin in the human intervertebral disc
    • Johnstone B, Markopoulos M, Neame P, &, Caterson B, (1993) Identification and characterization of glycanated and non-glycanated forms of biglycan and decorin in the human intervertebral disc. Biochem J 292, 661-666. (Pubitemid 23210192)
    • (1993) Biochemical Journal , vol.292 , Issue.3 , pp. 661-666
    • Johnstone, B.1    Markopoulos, M.2    Neame, P.3    Caterson, B.4
  • 42
    • 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
    • DOI 10.1074/jbc.M109540200
    • Reinboth B, Hanssen E, Cleary EG, &, Gibson MA, (2002) 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, 3950-3957. (Pubitemid 34968648)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 3950-3957
    • Reinboth, B.1    Hanssen, E.2    Cleary, E.G.3    Gibson, M.A.4
  • 43
    • 33748366399 scopus 로고    scopus 로고
    • Fibrillogenesis of collagen types I, II, and III with small leucine-rich proteoglycans decorin and biglycan
    • DOI 10.1021/bm0603746
    • Douglas T, Heinemann S, Bierbaum S, Scharnweber D, &, Worch H, (2006) Fibrillogenesis of collagen types I, II, and III with small leucine-rich proteoglycans decorin and biglycan. Biomacromolecules 7, 2388-2393. (Pubitemid 44336350)
    • (2006) Biomacromolecules , vol.7 , Issue.8 , pp. 2388-2393
    • Douglas, T.1    Heinemann, S.2    Bierbaum, S.3    Scharnweber, D.4    Worch, H.5
  • 44
    • 57149110014 scopus 로고    scopus 로고
    • Retrovirally mediated overexpression of glycosaminoglycan-deficient biglycan in arterial smooth muscle cells induces tropoelastin synthesis and elastic fiber formation in vitro and in neointimae after vascular injury
    • Hwang JY, Johnson PY, Braun KR, Hinek A, Fischer JW, O'Brien KD, Starcher B, Clowes AW, Merrilees MJ, &, Wight TN, (2008) Retrovirally mediated overexpression of glycosaminoglycan-deficient biglycan in arterial smooth muscle cells induces tropoelastin synthesis and elastic fiber formation in vitro and in neointimae after vascular injury. Am J Pathol 173, 1919-1928.
    • (2008) Am J Pathol , vol.173 , pp. 1919-1928
    • Hwang, J.Y.1    Johnson, P.Y.2    Braun, K.R.3    Hinek, A.4    Fischer, J.W.5    O'Brien, K.D.6    Starcher, B.7    Clowes, A.W.8    Merrilees, M.J.9    Wight, T.N.10
  • 45
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor β
    • Hildebrand A, Romaris M, Rasmussen LM, Heinegard D, Twardzik DR, Border WA, &, Ruoslahti E, (1994) Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. Biochem J 302, 527-534. (Pubitemid 24280108)
    • (1994) Biochemical Journal , vol.302 , Issue.2 , pp. 527-534
    • Hildebrand, A.1    Romaris, M.2    Rasmussen, M.3    Heinegard, D.4    Twardzik, D.R.5    Border, W.A.6    Ruoslahti, E.7
  • 46
    • 0037163862 scopus 로고    scopus 로고
    • Tumour necrosis factor-α interacts with biglycan and decorin
    • DOI 10.1016/S0014-5793(02)03439-7, PII S0014579302034397
    • Tufvesson E, &, Westergren-Thorsson G, (2002) Tumour necrosis factor-alpha interacts with biglycan and decorin. FEBS Lett 530, 124-128. (Pubitemid 35248197)
    • (2002) FEBS Letters , vol.530 , Issue.1-3 , pp. 124-128
    • Tufvesson, E.1    Westergren-Thorsson, G.2
  • 47
    • 2942706108 scopus 로고    scopus 로고
    • The small leucine-rich proteoglycan biglycan modulates BMP-4-induced osteoblast differentiation
    • DOI 10.1096/fj.03-0899com
    • Chen XD, Fisher LW, Robey PG, &, Young MF, (2004) The small leucine-rich proteoglycan biglycan modulates BMP-4-induced osteoblast differentiation. FASEB J 18, 948-958. (Pubitemid 38787591)
    • (2004) FASEB Journal , vol.18 , Issue.9 , pp. 948-958
    • Chen, X.-D.1    Fisher, L.W.2    Robey, P.G.3    Young, M.F.4
  • 48
    • 84934438944 scopus 로고    scopus 로고
    • Biglycan is a positive modulator of BMP-2 induced osteoblast differentiation
    • Mochida Y, Parisuthiman D, &, Yamauchi M, (2006) Biglycan is a positive modulator of BMP-2 induced osteoblast differentiation. Adv Exp Med Biol 585, 101-113.
    • (2006) Adv Exp Med Biol , vol.585 , pp. 101-113
    • Mochida, Y.1    Parisuthiman, D.2    Yamauchi, M.3
  • 49
    • 0035861577 scopus 로고    scopus 로고
    • WISP-1 binds to decorin and biglycan
    • Desnoyers L, Arnott D, &, Pennica D, (2001) WISP-1 binds to decorin and biglycan. J Biol Chem 276, 47599-47607.
    • (2001) J Biol Chem , vol.276 , pp. 47599-47607
    • Desnoyers, L.1    Arnott, D.2    Pennica, D.3
  • 50
    • 52049122865 scopus 로고    scopus 로고
    • Biological functions of the small leucine-rich proteoglycans: From genetics to signal transduction
    • Schaefer L, &, Iozzo RV, (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
  • 51
    • 72449146700 scopus 로고    scopus 로고
    • The matricellular functions of small leucine-rich proteoglycans (SLRPs)
    • Merline R, Schaefer RM, &, Schaefer L, (2009) The matricellular functions of small leucine-rich proteoglycans (SLRPs). J Cell Commun Signal 3, 323-335.
    • (2009) J Cell Commun Signal , vol.3 , pp. 323-335
    • Merline, R.1    Schaefer, R.M.2    Schaefer, L.3
  • 52
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • Iozzo RV, &, 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
  • 53
    • 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
  • 54
    • 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, &, 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
  • 55
    • 53549119130 scopus 로고    scopus 로고
    • Hyperelongated biglycan: The surreptitious initiator of atherosclerosis
    • Little PJ, Osman N, &, O'Brien KD, (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
  • 56
    • 84865579177 scopus 로고    scopus 로고
    • Biglycan: A promising new therapeutic for neuromuscular and musculoskeletal diseases
    • Young MF, &, Fallon JR, (2012) Biglycan: a promising new therapeutic for neuromuscular and musculoskeletal diseases. Curr Opin Genet Dev 22, 398-400.
    • (2012) Curr Opin Genet Dev , vol.22 , pp. 398-400
    • Young, M.F.1    Fallon, J.R.2
  • 57
    • 84877715193 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans: Multifunctional signaling effectors
    • In (Karamanos N.K. ed.), Walter de Gruyter, Berlin/Boston.
    • Merline R, Nastase MV, Iozzo RV, &, Schaefer L, (2012) Small leucine-rich proteoglycans: multifunctional signaling effectors. In Extracellular Matrix: Pathobiology and Signaling (, Karamanos NK, ed.), pp. 185-196. Walter de Gruyter, Berlin/Boston.
    • (2012) Extracellular Matrix: Pathobiology and Signaling , pp. 185-196
    • Merline, R.1    Nastase, M.V.2    Iozzo, R.V.3    Schaefer, L.4
  • 58
    • 84873028647 scopus 로고    scopus 로고
    • Biglycan: A multivalent proteoglycan providing structure and signals
    • Nastase MV, Young MF, &, Schaefer L, (2012) Biglycan: a multivalent proteoglycan providing structure and signals. J Histochem Cytochem 60, 963-975.
    • (2012) J Histochem Cytochem , vol.60 , pp. 963-975
    • Nastase, M.V.1    Young, M.F.2    Schaefer, L.3
  • 62
    • 84869504451 scopus 로고    scopus 로고
    • Inflammasomes and their roles in health and disease
    • Lamkanfi M, &, Dixit VM, (2012) Inflammasomes and their roles in health and disease. Annu Rev Cell Dev Biol 28, 137-161.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 137-161
    • Lamkanfi, M.1    Dixit, V.M.2
  • 63
  • 64
    • 84862162972 scopus 로고    scopus 로고
    • Adipose tissue biglycan as a potential antiinflammatory target of sodium salicylate in mice fed a high fat diet
    • Adapala VJ, Ward M, &, Ajuwon K, (2012) Adipose tissue biglycan as a potential antiinflammatory target of sodium salicylate in mice fed a high fat diet. J Inflamm (Lond) 9, 15.
    • (2012) J Inflamm (Lond) , vol.9 , pp. 15
    • Adapala, V.J.1    Ward, M.2    Ajuwon, K.3
  • 66
    • 59249103181 scopus 로고    scopus 로고
    • Short leucine-rich glycoproteins of the extracellular matrix display diverse patterns of complement interaction and activation
    • Sjoberg AP, Manderson GA, Morgelin M, Day AJ, Heinegard D, &, Blom AM, (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
  • 67
    • 61449155448 scopus 로고    scopus 로고
    • Dermatan sulfate proteoglycan biglycan as a potential selectin L/CD44 ligand involved in selective recruitment of peripheral blood CD16(-) natural killer cells into human endometrium
    • Kitaya K, &, Yasuo T, (2009) Dermatan sulfate proteoglycan biglycan as a potential selectin L/CD44 ligand involved in selective recruitment of peripheral blood CD16(-) natural killer cells into human endometrium. J Leukoc Biol 85, 391-400.
    • (2009) J Leukoc Biol , vol.85 , pp. 391-400
    • Kitaya, K.1    Yasuo, T.2
  • 68
    • 0141763811 scopus 로고    scopus 로고
    • The role of decorin in collagen fibrillogenesis and skin homeostasis
    • DOI 10.1023/A:1025383913444
    • Reed CC, &, Iozzo RV, (2002) The role of decorin in collagen fibrillogenesis and skin homeostasis. Glycoconj J 19, 249-255. (Pubitemid 37174552)
    • (2002) Glycoconjugate Journal , vol.19 , Issue.4-5 , pp. 249-255
    • Reed, C.C.1    Iozzo, R.V.2
  • 69
    • 84867745182 scopus 로고    scopus 로고
    • The galactosaminoglycan-containing decorin and its impact on diseases
    • Seidler DG, (2012) The galactosaminoglycan-containing decorin and its impact on diseases. Curr Opin Struct Biol 22, 578-582.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 578-582
    • Seidler, D.G.1
  • 70
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • DOI 10.1083/jcb.136.3.729
    • Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, &, Iozzo RV, (1997) Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol 136, 729-743. (Pubitemid 27083772)
    • (1997) Journal of Cell Biology , vol.136 , Issue.3 , 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
  • 72
    • 42049100773 scopus 로고    scopus 로고
    • Influence of cyclic strain and decorin deficiency on 3D cellularized collagen matrices
    • Ferdous Z, Lazaro LD, Iozzo RV, Hook M, &, Grande-Allen KJ, (2008) Influence of cyclic strain and decorin deficiency on 3D cellularized collagen matrices. Biomaterials 29, 2740-2748.
    • (2008) Biomaterials , vol.29 , pp. 2740-2748
    • Ferdous, Z.1    Lazaro, L.D.2    Iozzo, R.V.3    Hook, M.4    Grande-Allen, K.J.5
  • 73
    • 0033582415 scopus 로고    scopus 로고
    • Decorin is a biological ligand for the epidermal growth factor receptor
    • Iozzo RV, Moscatello DK, McQuillan DJ, &, 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
  • 75
    • 84864138010 scopus 로고    scopus 로고
    • Decorin: A guardian from the matrix
    • Neill T, Schaefer L, &, Iozzo RV, (2012) Decorin: a guardian from the matrix. Am J Pathol 181, 380-387.
    • (2012) Am J Pathol , vol.181 , pp. 380-387
    • Neill, T.1    Schaefer, L.2    Iozzo, R.V.3
  • 76
  • 81
    • 79961009000 scopus 로고    scopus 로고
    • Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast
    • Khan GA, Girish GV, Lala N, Di Guglielmo GM, &, Lala PK, (2011) Decorin is a novel VEGFR-2-binding antagonist for the human extravillous trophoblast. Mol Endocrinol 25, 1431-1443.
    • (2011) Mol Endocrinol , vol.25 , pp. 1431-1443
    • Khan, G.A.1    Girish, G.V.2    Lala, N.3    Di Guglielmo, G.M.4    Lala, P.K.5
  • 82
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin
    • DOI 10.1074/jbc.M602919200
    • Brandan E, Retamal C, Cabello-Verrugio C, &, Marzolo MP, (2006) The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin. J Biol Chem 281, 31562-31571. (Pubitemid 46041422)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.42 , pp. 31562-31571
    • Brandan, E.1    Retamal, C.2    Cabello-Verrugio, C.3    Marzolo, M.-P.4
  • 83
    • 79957605232 scopus 로고    scopus 로고
    • Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
    • Iozzo RV, &, Sanderson RD, (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
  • 85
    • 57349175862 scopus 로고    scopus 로고
    • Tumor microenvironment: Modulation by decorin and related molecules harboring leucine-rich tandem motifs
    • Goldoni S, &, Iozzo RV, (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
  • 86
    • 77956641177 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel roles for proteoglycans in malignancy and their pharmacological targeting
    • Theocharis AD, Skandalis SS, Tzanakakis GN, &, Karamanos NK, (2010) Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting. FEBS J 277, 3904-3923.
    • (2010) FEBS J , vol.277 , pp. 3904-3923
    • Theocharis, A.D.1    Skandalis, S.S.2    Tzanakakis, G.N.3    Karamanos, N.K.4
  • 87
    • 0026676859 scopus 로고
    • Natural inhibitor of transforming growth factor-β protects against scarring in experimental kidney disease
    • DOI 10.1038/360361a0
    • Border WA, Noble NA, Yamamoto T, Harper JR, Yamaguchi Y, Pierschbacher MD, &, Ruoslahti E, (1992) Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Nature 360, 361-364. (Pubitemid 23000677)
    • (1992) Nature , vol.360 , Issue.6402 , pp. 361-364
    • Border, W.A.1    Noble, N.A.2    Yamamoto, T.3    Harper, J.R.4    Yamaguchi, Y.5    Pierschbacher, M.D.6    Ruoslahti, E.7
  • 89
    • 0034979153 scopus 로고    scopus 로고
    • Proteoglycans decorin and biglycan differentially modulate TGF-beta-mediated fibrotic responses in the lung
    • Kolb M, Margetts PJ, Sime PJ, &, 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-L1334.
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.280
    • Kolb, M.1    Margetts, P.J.2    Sime, P.J.3    Gauldie, J.4
  • 91
    • 84864796944 scopus 로고    scopus 로고
    • Decorin-TGFbeta axis in hepatic fibrosis and cirrhosis
    • Baghy K, Iozzo RV, &, Kovalszky I, (2012) Decorin-TGFbeta axis in hepatic fibrosis and cirrhosis. J Histochem Cytochem 60, 262-268.
    • (2012) J Histochem Cytochem , vol.60 , pp. 262-268
    • Baghy, K.1    Iozzo, R.V.2    Kovalszky, I.3
  • 92
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-beta by the proteoglycan decorin
    • Yamaguchi Y, Mann DM, &, 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
  • 94
    • 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, &, 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
  • 96
    • 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 CC, &, Iozzo RV, (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
  • 98
    • 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
    • DOI 10.1074/jbc.M602853200
    • Seidler DG, Goldoni S, Agnew C, Cardi C, Thakur ML, Owens RT, McQuillan DJ, &, Iozzo RV, (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. (Pubitemid 44401849)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26408-26418
    • Seidler, D.G.1    Goldoni, S.2    Agnew, C.3    Cardi, C.4    Thakur, M.L.5    Owens, R.T.6    McQuillan, D.J.7    Iozzo, R.V.8
  • 99
    • 84857308088 scopus 로고    scopus 로고
    • Decorin antagonizes the angiogenic network: Concurrent inhibition of Met, hypoxia inducible factor 1alpha, vascular endothelial growth factor A, and induction of thrombospondin-1 and TIMP3
    • Neill T, Painter H, Buraschi S, Owens RT, Lisanti MP, Schaefer L, &, Iozzo RV, (2012) Decorin antagonizes the angiogenic network: concurrent inhibition of Met, hypoxia inducible factor 1alpha, vascular endothelial growth factor A, and induction of thrombospondin-1 and TIMP3. J Biol Chem 287, 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    Iozzo, R.V.7
  • 100
    • 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 RT, Neill T, &, Iozzo RV, (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
  • 101
    • 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
    • Buraschi S, Neill T, Owens RT, Iniguez LA, Purkins G, Vadigepalli R, Evans B, Schaefer L, Peiper SC, Wang ZX, et al,. (2012) 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, e45559.
    • (2012) PLoS ONE , vol.7
    • Buraschi, S.1    Neill, T.2    Owens, R.T.3    Iniguez, L.A.4    Purkins, G.5    Vadigepalli, R.6    Evans, B.7    Schaefer, L.8    Peiper, S.C.9    Wang, Z.X.10
  • 102
    • 84870362178 scopus 로고    scopus 로고
    • More than matrix: The multifaceted role of decorin in cancer
    • Sofeu Feugaing DD, Gotte M, &, Viola M, (2013) More than matrix: the multifaceted role of decorin in cancer. Eur J Cell Biol 92, 1-11.
    • (2013) Eur J Cell Biol , vol.92 , pp. 1-11
    • Sofeu Feugaing, D.D.1    Gotte, M.2    Viola, M.3
  • 104
    • 84873052431 scopus 로고    scopus 로고
    • Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population
    • Onuma H, Tabara Y, Kawamura R, Ohashi J, Nishida W, Takata Y, Ochi M, Nishimiya T, Kawamoto R, Kohara K, et al,. (2012) Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population. Diabetes 62, 649-652.
    • (2012) Diabetes , vol.62 , pp. 649-652
    • Onuma, H.1    Tabara, Y.2    Kawamura, R.3    Ohashi, J.4    Nishida, W.5    Takata, Y.6    Ochi, M.7    Nishimiya, T.8    Kawamoto, R.9    Kohara, K.10
  • 107
    • 84860227203 scopus 로고    scopus 로고
    • Domain combination of the vertebrate-like TLR gene family: Implications for their origin and evolution
    • Wu B, Huan T, Gong J, Zhou P, &, Bai Z, (2011) Domain combination of the vertebrate-like TLR gene family: implications for their origin and evolution. J Genet 90, 401-408.
    • (2011) J Genet , vol.90 , pp. 401-408
    • Wu, B.1    Huan, T.2    Gong, J.3    Zhou, P.4    Bai, Z.5
  • 108
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease
    • DOI 10.1146/annurev.biochem.74.082803.133347
    • Inohara N, Chamaillard M, McDonald C, &, Nunez G, (2005) NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu Rev Biochem 74, 355-383. (Pubitemid 40995511)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 355-383
    • Inohara, N.1    Chamaillard, M.2    McDonald, C.3    Nunez, G.4
  • 109
    • 11144256156 scopus 로고    scopus 로고
    • Lumican regulates corneal inflammatory responses by modulating Fas-Fas ligand signaling
    • DOI 10.1167/iovs.04-0833
    • Vij N, Roberts L, Joyce S, &, Chakravarti S, (2005) Lumican regulates corneal inflammatory responses by modulating Fas-Fas ligand signaling. Invest Ophthalmol Vis Sci 46, 88-95. (Pubitemid 40041183)
    • (2005) Investigative Ophthalmology and Visual Science , vol.46 , Issue.1 , pp. 88-95
    • Vij, N.1    Roberts, L.2    Joyce, S.3    Chakravarti, S.4
  • 110
    • 37249010513 scopus 로고    scopus 로고
    • Keratocan and lumican regulate neutrophil infiltration and corneal clarity in lipopolysaccharide-induced keratitis by direct interaction with CXCL1
    • DOI 10.1074/jbc.M705823200
    • Carlson EC, Lin M, Liu CY, Kao WW, Perez VL, &, 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. (Pubitemid 350277127)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35502-35509
    • Carlson, E.C.1    Lin, M.2    Liu, C.-Y.3    Kao, W.W.-Y.4    Perez, V.L.5    Pearlman, E.6
  • 113
    • 34548861475 scopus 로고    scopus 로고
    • A novel role of the lumican core protein in bacterial lipopolysaccharide- induced innate immune response
    • DOI 10.1074/jbc.M702402200
    • Wu F, Vij N, Roberts L, Lopez-Briones S, Joyce S, &, Chakravarti S, (2007) A novel role of the lumican core protein in bacterial lipopolysaccharide-induced innate immune response. J Biol Chem 282, 26409-26417. (Pubitemid 47443780)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26409-26417
    • Wu, F.1    Vij, N.2    Roberts, L.3    Lopez-Briones, S.4    Joyce, S.5    Chakravarti, S.6
  • 117
    • 84862489198 scopus 로고    scopus 로고
    • Inflammation amplification by versican: The first mediator
    • Zhang Z, Miao L, &, Wang L, (2012) Inflammation amplification by versican: the first mediator. Int J Mol Sci 13, 6873-6882.
    • (2012) Int J Mol Sci , vol.13 , pp. 6873-6882
    • Zhang, Z.1    Miao, L.2    Wang, L.3
  • 118
    • 84857033876 scopus 로고    scopus 로고
    • Hyaluronan and versican in the control of human T-lymphocyte adhesion and migration
    • Evanko SP, Potter-Perigo S, Bollyky PL, Nepom GT, &, Wight TN, (2012) Hyaluronan and versican in the control of human T-lymphocyte adhesion and migration. Matrix Biol 31, 90-100.
    • (2012) Matrix Biol , vol.31 , pp. 90-100
    • Evanko, S.P.1    Potter-Perigo, S.2    Bollyky, P.L.3    Nepom, G.T.4    Wight, T.N.5
  • 120
    • 84859719825 scopus 로고    scopus 로고
    • RhoGDI2 suppresses lung metastasis in mice by reducing tumor versican expression and macrophage infiltration
    • Said N, Sanchez-Carbayo M, Smith SC, &, Theodorescu D, (2012) RhoGDI2 suppresses lung metastasis in mice by reducing tumor versican expression and macrophage infiltration. J Clin Invest 122, 1503-1518.
    • (2012) J Clin Invest , vol.122 , pp. 1503-1518
    • Said, N.1    Sanchez-Carbayo, M.2    Smith, S.C.3    Theodorescu, D.4
  • 121
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo RV, &, Murdoch AD, (1996) Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J 10, 598-614. (Pubitemid 26141171)
    • (1996) FASEB Journal , vol.10 , Issue.5 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 122
    • 27244432621 scopus 로고    scopus 로고
    • The interaction of versican with its binding partners
    • DOI 10.1038/sj.cr.7290318
    • Wu YJ, La Pierre DP, Wu J, Yee AJ, &, Yang BB, (2005) The interaction of versican with its binding partners. Cell Res 15, 483-494. (Pubitemid 41653919)
    • (2005) Cell Research , vol.15 , Issue.7 , pp. 483-494
    • Wu, Y.J.1    La Pierre, D.P.2    Wu, J.3    Yee, A.J.4    Yang, B.B.5
  • 123
    • 42649136260 scopus 로고    scopus 로고
    • Arterial remodeling in vascular disease: A key role for hyaluronan and versican
    • DOI 10.2741/3052
    • Wight TN, (2008) Arterial remodeling in vascular disease: a key role for hyaluronan and versican. Front Biosci 13, 4933-4937. (Pubitemid 351599647)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.13 , pp. 4933-4937
    • Wight, T.N.1
  • 124
    • 84878242170 scopus 로고    scopus 로고
    • MiRNAs regulate expression and function of extracellular matrix molecules
    • doi: 10.1016/jmatbio.2012.11.003.
    • Rutnam ZJ, Wight TN, &, Yang BB, (2012) miRNAs regulate expression and function of extracellular matrix molecules. Matrix Biol, doi: 10.1016/jmatbio.2012.11.003.
    • (2012) Matrix Biol
    • Rutnam, Z.J.1    Wight, T.N.2    Yang, B.B.3
  • 125
    • 79952261122 scopus 로고    scopus 로고
    • Role of versican, hyaluronan and CD44 in ovarian cancer metastasis
    • Ween MP, Oehler MK, &, Ricciardelli C, (2011) Role of versican, hyaluronan and CD44 in ovarian cancer metastasis. Int J Mol Sci 12, 1009-1029.
    • (2011) Int J Mol Sci , vol.12 , pp. 1009-1029
    • Ween, M.P.1    Oehler, M.K.2    Ricciardelli, C.3
  • 126
    • 84877720509 scopus 로고    scopus 로고
    • The pathobiology of versican
    • In (Karamanos N.K. ed.), Walter de Gruyter, Berlin/Boston.
    • Wight TN, (2012) The pathobiology of versican. In Extracellular Matrix: Pathobiology and Signaling (, Karamanos NK, ed.), pp. 154-170. Walter de Gruyter, Berlin/Boston.
    • (2012) Extracellular Matrix: Pathobiology and Signaling , pp. 154-170
    • Wight, T.N.1
  • 127
    • 0036775241 scopus 로고    scopus 로고
    • Versican: A versatile extracellular matrix proteoglycan in cell biology
    • DOI 10.1016/S0955-0674(02)00375-7
    • Wight TN, (2002) Versican: a versatile extracellular matrix proteoglycan in cell biology. Curr Opin Cell Biol 14, 617-623. (Pubitemid 35247746)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.5 , pp. 617-623
    • Wight, T.N.1
  • 130
    • 0036721716 scopus 로고    scopus 로고
    • Shaping gene expression in activated and resting primary macrophages by IL-10
    • Lang R, Patel D, Morris JJ, Rutschman RL, &, Murray PJ, (2002) Shaping gene expression in activated and resting primary macrophages by IL-10. J Immunol 169, 2253-2263. (Pubitemid 34920965)
    • (2002) Journal of Immunology , vol.169 , Issue.5 , pp. 2253-2263
    • Lang, R.1    Patel, D.2    Morris, J.J.3    Rutschman, R.L.4    Murray, P.J.5
  • 131
    • 79952104239 scopus 로고    scopus 로고
    • Macrophages exposed to hypoxia secrete proteoglycans for which LDL has higher affinity
    • Asplund A, Friden V, Stillemark-Billton P, Camejo G, &, Bondjers G, (2011) Macrophages exposed to hypoxia secrete proteoglycans for which LDL has higher affinity. Atherosclerosis 215, 77-81.
    • (2011) Atherosclerosis , vol.215 , pp. 77-81
    • Asplund, A.1    Friden, V.2    Stillemark-Billton, P.3    Camejo, G.4    Bondjers, G.5
  • 132
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • Hynes RO, (2009) The extracellular matrix: not just pretty fibrils. Science 326, 1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 134
    • 0032698135 scopus 로고    scopus 로고
    • Mononuclear leukocytes preferentially bind via CD44 to hyaluronan on human intestinal mucosal smooth muscle cells after virus infection or treatment with poly(IC)
    • De La Motte CA, Hascall VC, Calabro A, Yen-Lieberman B, &, Strong SA, (1999) Mononuclear leukocytes preferentially bind via CD44 to hyaluronan on human intestinal mucosal smooth muscle cells after virus infection or treatment with poly(IC). J Biol Chem 274, 30747-30755.
    • (1999) J Biol Chem , vol.274 , pp. 30747-30755
    • De La Motte, C.A.1    Hascall, V.C.2    Calabro, A.3    Yen-Lieberman, B.4    Strong, S.A.5
  • 135
    • 0034634577 scopus 로고    scopus 로고
    • Binding of a large chondroitin sulfate/dermatan sulfate proteoglycan, versican, to L-selectin, P-selectin, and CD44
    • Kawashima H, Hirose M, Hirose J, Nagakubo D, Plaas AH, &, Miyasaka M, (2000) Binding of a large chondroitin sulfate/dermatan sulfate proteoglycan, versican, to L-selectin, P-selectin, and CD44. J Biol Chem 275, 35448-35456.
    • (2000) J Biol Chem , vol.275 , pp. 35448-35456
    • Kawashima, H.1    Hirose, M.2    Hirose, J.3    Nagakubo, D.4    Plaas, A.H.5    Miyasaka, M.6
  • 138
    • 78751670809 scopus 로고    scopus 로고
    • Hyaluronan as an immune regulator in human diseases
    • Jiang D, Liang J, &, Noble PW, (2011) Hyaluronan as an immune regulator in human diseases. Physiol Rev 91, 221-264.
    • (2011) Physiol Rev , vol.91 , pp. 221-264
    • Jiang, D.1    Liang, J.2    Noble, P.W.3
  • 139
    • 80055068206 scopus 로고    scopus 로고
    • Role of receptor for hyaluronic acid-mediated motility (RHAMM) in low molecular weight hyaluronan (LMWHA)-mediated fibrosarcoma cell adhesion
    • Kouvidi K, Berdiaki A, Nikitovic D, Katonis P, Afratis N, Hascall VC, Karamanos NK, &, Tzanakakis GN, (2011) Role of receptor for hyaluronic acid-mediated motility (RHAMM) in low molecular weight hyaluronan (LMWHA)-mediated fibrosarcoma cell adhesion. J Biol Chem 286, 38509-38520.
    • (2011) J Biol Chem , vol.286 , pp. 38509-38520
    • Kouvidi, K.1    Berdiaki, A.2    Nikitovic, D.3    Katonis, P.4    Afratis, N.5    Hascall, V.C.6    Karamanos, N.K.7    Tzanakakis, G.N.8
  • 140
    • 78651099927 scopus 로고    scopus 로고
    • Hyaluronan
    • In (2nd edition) (Varki A. Cummings R.D. Esko J.D. Freeze H.H. Stanley P. Bertozzi C.R. Hart G.W. & Etzler M.E. eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY).
    • Hascall V, &, Esko JD, (2009) Hyaluronan. In Essentials of Glycobiology (2nd edition) (, Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, &, Etzler ME, eds), pp. 219-228. Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY).
    • (2009) Essentials of Glycobiology , pp. 219-228
    • Hascall, V.1    Esko, J.D.2
  • 141
    • 79955054709 scopus 로고    scopus 로고
    • Regulatory roles of hyaluronan in health and disease
    • Hascall V, &, Karamanos N, (2011) Regulatory roles of hyaluronan in health and disease. FEBS J 278, 1411.
    • (2011) FEBS J , vol.278 , pp. 1411
    • Hascall, V.1    Karamanos, N.2
  • 142
    • 79955063269 scopus 로고    scopus 로고
    • Hyaluronan matrices in pathobiological processes
    • Wang A, De la Motte C, Lauer M, &, Hascall V, (2011) Hyaluronan matrices in pathobiological processes. FEBS J 278, 1412-1418.
    • (2011) FEBS J , vol.278 , pp. 1412-1418
    • Wang, A.1    De La Motte, C.2    Lauer, M.3    Hascall, V.4
  • 143
    • 84874855190 scopus 로고    scopus 로고
    • Multiple roles of hyaluronan as a target and modifier of the inflammatory response
    • In (Karamanos N.K. ed.), Walter de Gruyter, Berlin/Boston.
    • Oikari SJT, Tammi RH, &, Tammi MI, (2012) Multiple roles of hyaluronan as a target and modifier of the inflammatory response. In Extracellular Matrix: Pathobiology and Signaling (, Karamanos NK, ed.), pp. 39-65. Walter de Gruyter, Berlin/Boston.
    • (2012) Extracellular Matrix: Pathobiology and Signaling , pp. 39-65
    • Oikari, S.J.T.1    Tammi, R.H.2    Tammi, M.I.3
  • 144
    • 82455175828 scopus 로고    scopus 로고
    • Hyaluronan in intestinal homeostasis and inflammation: Implications for fibrosis
    • De la Motte CA, (2011) Hyaluronan in intestinal homeostasis and inflammation: implications for fibrosis. Am J Physiol Gastrointest Liver Physiol 301, G945-G949.
    • (2011) Am J Physiol Gastrointest Liver Physiol , vol.301
    • De La Motte, C.A.1
  • 145
    • 84865703946 scopus 로고    scopus 로고
    • Specific-sized hyaluronan fragments promote expression of human beta-defensin 2 in intestinal epithelium
    • Hill DR, Kessler SP, Rho HK, Cowman MK, &, De la Motte CA, (2012) Specific-sized hyaluronan fragments promote expression of human beta-defensin 2 in intestinal epithelium. J Biol Chem 287, 30610-30624.
    • (2012) J Biol Chem , vol.287 , pp. 30610-30624
    • Hill, D.R.1    Kessler, S.P.2    Rho, H.K.3    Cowman, M.K.4    De La Motte, C.A.5
  • 146
    • 53349122005 scopus 로고    scopus 로고
    • High-molecular-weight hyaluronan - A possible new treatment for sepsis-induced lung injury: A preclinical study in mechanically ventilated rats
    • Liu YY, Lee CH, Dedaj R, Zhao H, Mrabat H, Sheidlin A, Syrkina O, Huang PM, Garg HG, Hales CA, et al,. (2008) High-molecular-weight hyaluronan-a possible new treatment for sepsis-induced lung injury: a preclinical study in mechanically ventilated rats. Crit Care 12, R102.
    • (2008) Crit Care , vol.12
    • Liu, Y.Y.1    Lee, C.H.2    Dedaj, R.3    Zhao, H.4    Mrabat, H.5    Sheidlin, A.6    Syrkina, O.7    Huang, P.M.8    Garg, H.G.9    Hales, C.A.10
  • 149
    • 0033280661 scopus 로고    scopus 로고
    • The proinflammatory role of hyaluronan-CD44 interactions in renal injury
    • Wuthrich RP, (1999) The proinflammatory role of hyaluronan-CD44 interactions in renal injury. Nephrol Dial Transplant 14, 2554-2556. (Pubitemid 32208356)
    • (1999) Nephrology Dialysis Transplantation , vol.14 , Issue.11 , pp. 2554-2556
    • Wuthrich, R.P.1
  • 151
    • 34547127890 scopus 로고    scopus 로고
    • Recognition of hyaluronan released in sterile injury involves a unique receptor complex dependent on toll-like receptor 4, CD44, and MD-2
    • DOI 10.1074/jbc.M606352200
    • Taylor KR, Yamasaki K, Radek KA, Di Nardo A, Goodarzi H, Golenbock D, Beutler B, &, Gallo RL, (2007) Recognition of hyaluronan released in sterile injury involves a unique receptor complex dependent on Toll-like receptor 4, CD44, and MD-2. J Biol Chem 282, 18265-18275. (Pubitemid 47100227)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18265-18275
    • Taylor, K.R.1    Yamasaki, K.2    Radek, K.A.3    Di Nardo, A.4    Goodarzi, H.5    Golenbock, D.6    Beutler, B.7    Gallo, R.L.8
  • 152
    • 67649831360 scopus 로고    scopus 로고
    • NLRP3/cryopyrin is necessary for interleukin-1beta (IL-1beta) release in response to hyaluronan, an endogenous trigger of inflammation in response to injury
    • Yamasaki K, Muto J, Taylor KR, Cogen AL, Audish D, Bertin J, Grant EP, Coyle AJ, Misaghi A, Hoffman HM, et al,. (2009) NLRP3/cryopyrin is necessary for interleukin-1beta (IL-1beta) release in response to hyaluronan, an endogenous trigger of inflammation in response to injury. J Biol Chem 284, 12762-12771.
    • (2009) J Biol Chem , vol.284 , pp. 12762-12771
    • Yamasaki, K.1    Muto, J.2    Taylor, K.R.3    Cogen, A.L.4    Audish, D.5    Bertin, J.6    Grant, E.P.7    Coyle, A.J.8    Misaghi, A.9    Hoffman, H.M.10
  • 154
    • 34548727522 scopus 로고    scopus 로고
    • Cutting edge: High molecular weight hyaluronan promotes the suppressive effects of CD4+CD25+ regulatory T cells
    • Bollyky PL, Lord JD, Masewicz SA, Evanko SP, Buckner JH, Wight TN, &, Nepom GT, (2007) Cutting edge: high molecular weight hyaluronan promotes the suppressive effects of CD4+CD25+ regulatory T cells. J Immunol 179, 744-747.
    • (2007) J Immunol , vol.179 , pp. 744-747
    • Bollyky, P.L.1    Lord, J.D.2    Masewicz, S.A.3    Evanko, S.P.4    Buckner, J.H.5    Wight, T.N.6    Nepom, G.T.7
  • 156
    • 27744571610 scopus 로고    scopus 로고
    • Hyaluronan cross-linking: A protective mechanism in inflammation?
    • DOI 10.1016/j.it.2005.09.009, PII S1471490605002450
    • Day AJ, &, De la Motte CA, (2005) Hyaluronan cross-linking: a protective mechanism in inflammation? Trends Immunol 26, 637-643. (Pubitemid 41628196)
    • (2005) Trends in Immunology , vol.26 , Issue.12 , pp. 637-643
    • Day, A.J.1    De La Motte, C.A.2


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