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Volumn 802, Issue , 2014, Pages 31-47

Basic components of connective tissues and extracellular matrix: Elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins

Author keywords

Elastin; Fibrillin; Fibulins; Laminin; Tenascins

Indexed keywords

CARTILAGE OLIGOMERIC MATRIX PROTEIN; CELL SURFACE RECEPTOR; COLLAGEN; ELASTIN; FIBRILLIN; FIBRIN; FIBRINOGEN; FIBRONECTIN; FIBULIN; GLYCOPROTEIN; INTEGRIN; LAMININ; MATRIX METALLOPROTEINASE; PROTEOGLYCAN; TENASCIN; THROMBIN; THROMBOSPONDIN; TRANSFORMING GROWTH FACTOR BETA; TROPOELASTIN; COLLAGEN TYPE 1; COLLAGEN TYPE 3; COLLAGEN TYPE 4; EPIDERMAL GROWTH FACTOR; FIBRILLIN 1; FIBULIN 5; FOCAL ADHESION KINASE; GELATINASE B; INTERLEUKIN 1; INTERSTITIAL COLLAGENASE; PLATELET DERIVED GROWTH FACTOR; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; THROMBOSPONDIN 1; TISSUE INHIBITOR OF METALLOPROTEINASE 1; UNINDEXED DRUG; VASCULOTROPIN; VERY LATE ACTIVATION ANTIGEN 2;

EID: 84934438461     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-7-7893-1_3     Document Type: Article
Times cited : (389)

References (145)
  • 1
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • Kjaer M (2004) Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol Rev 84:649-698
    • (2004) Physiol Rev , vol.84 , pp. 649-698
    • Kjaer, M.1
  • 2
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fi bronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I, Erickson HP (1996) 2.0 A crystal structure of a four-domain segment of human fi bronectin encompassing the RGD loop and synergy region. Cell 84:155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 5
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fi brillogenesis, a cell-mediated matrix assembly process
    • Mao Y, Schwarzbauer J (2005) Fibronectin fi brillogenesis, a cell-mediated matrix assembly process. Matrix Biol 24:389-399
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.2
  • 7
    • 84869128551 scopus 로고    scopus 로고
    • Fibronectin and stem cell differentiation - lessons from chondrogenesis
    • Singh P, Schwarzbauer JE (2012) Fibronectin and stem cell differentiation - lessons from chondrogenesis. J Cell Sci 125:3703-3712
    • (2012) J Cell Sci , vol.125 , pp. 3703-3712
    • Singh, P.1    Schwarzbauer, J.E.2
  • 8
    • 33748550344 scopus 로고    scopus 로고
    • Dynamics of assembly and reorganization of extracellular matrix proteins
    • Dallas SL, Chen Q, Sivakumar P (2006) Dynamics of assembly and reorganization of extracellular matrix proteins. Curr Top Dev Biol 75:1-24
    • (2006) Curr Top Dev Biol , vol.75 , pp. 1-24
    • Dallas, S.L.1    Chen, Q.2    Sivakumar, P.3
  • 12
    • 77951975118 scopus 로고    scopus 로고
    • Laminin chain assembly is regulated by specifi c coiled-coil interactions
    • MacDonald PR, Lustig A, Steinmetz MO, Kammerer RA (2010) Laminin chain assembly is regulated by specifi c coiled-coil interactions. J Struct Biol 170:398-405
    • (2010) J Struct Biol , vol.170 , pp. 398-405
    • MacDonald, P.R.1    Lustig, A.2    Steinmetz, M.O.3    Kammerer, R.A.4
  • 13
    • 28644439538 scopus 로고    scopus 로고
    • Strength at the extracellular matrix-muscle interface
    • Grounds MD, Sorokin L, White J (2005) Strength at the extracellular matrix-muscle interface. Scand J Med Sci Sports 15:381-391
    • (2005) Scand J Med Sci Sports , vol.15 , pp. 381-391
    • Grounds, M.D.1    Sorokin, L.2    White, J.3
  • 14
    • 79551543833 scopus 로고    scopus 로고
    • Tendon is covered by a basement membrane epithelium that is required for cell retention and the prevention of adhesion formation
    • Taylor SH, Al-Youha S, Van Agtmael T, Lu Y, Wong J, McGrouther DA, Kadler KE (2011) Tendon is covered by a basement membrane epithelium that is required for cell retention and the prevention of adhesion formation. PLoS One 6:e16337
    • (2011) PLoS One , vol.6
    • Taylor, S.H.1    Al-Youha, S.2    Van Agtmael, T.3    Lu, Y.4    Wong, J.5    McGrouther, D.A.6    Kadler, K.E.7
  • 15
    • 33748934067 scopus 로고    scopus 로고
    • Gene expression changes in SNAP-stimulated and iNOS-Transfected tenocytes-expression of extracellular matrix genes and its implications for tendonhealing
    • Molloy TJ, de Bock CE, Wang Y, Murrell GA (2006) Gene expression changes in SNAP-stimulated and iNOS-Transfected tenocytes-expression of extracellular matrix genes and its implications for tendonhealing. J Orthop Res 24:1869-1882
    • (2006) J Orthop Res , vol.24 , pp. 1869-1882
    • Molloy, T.J.1    De Bock, C.E.2    Wang, Y.3    Murrell, G.A.4
  • 16
    • 0033198894 scopus 로고    scopus 로고
    • Abnormal deposition of laminin and type IV collagen at corneal epithelial basement membrane during wound healing in Diabetic rats
    • Sato N, Nakamura M, Chikama T, Nishida T (1999) Abnormal deposition of laminin and type IV collagen at corneal epithelial basement membrane during wound healing in Diabetic rats. Jpn J Ophthalmol 43:343-347
    • (1999) Jpn J Ophthalmol , vol.43 , pp. 343-347
    • Sato, N.1    Nakamura, M.2    Chikama, T.3    Nishida, T.4
  • 19
    • 0017891368 scopus 로고
    • Designation of sequences involved in the coiled- coil' interdominal connections in fi brinogen: Constructions of an atomic scale model
    • Doolittle RF, Goldbaum DM, Doolittle LR (1978) Designation of sequences involved in the coiled- coil' interdominal connections in fi brinogen: Constructions of an atomic scale model. J Mol Biol 120:311-325
    • (1978) J Mol Biol , vol.120 , pp. 311-325
    • Doolittle, R.F.1    Goldbaum, D.M.2    Doolittle, L.R.3
  • 20
    • 0036682920 scopus 로고    scopus 로고
    • Role of factor XIII in fi brin clot formation and effects of genetic polymorphisms
    • Ariens RA, Lai TS, Weisel JW, Greenberg CS, Grant PJ (2002) Role of factor XIII in fi brin clot formation and effects of genetic polymorphisms. Blood 100:743-754
    • (2002) Blood , vol.100 , pp. 743-754
    • Ariens, R.A.1    Lai, T.S.2    Weisel, J.W.3    Greenberg, C.S.4    Grant, P.J.5
  • 22
    • 0034548802 scopus 로고    scopus 로고
    • Vascular endothelial growth factor binds to fi brinogen and fi brin and stimulates endothelial cell proliferation
    • Sahni A, Francis CW (2000) Vascular endothelial growth factor binds to fi brinogen and fi brin and stimulates endothelial cell proliferation. Blood 96:3772-3778
    • (2000) Blood , vol.96 , pp. 3772-3778
    • Sahni, A.1    Francis, C.W.2
  • 23
    • 0032571259 scopus 로고    scopus 로고
    • Binding of basic fi broblast growth factor to fi brinogen and fi brin
    • Sahni A, Odrljin T, Francis CW (1998) Binding of basic fi broblast growth factor to fi brinogen and fi brin. J Biol Chem 273:7554-7559
    • (1998) J Biol Chem , vol.273 , pp. 7554-7559
    • Sahni, A.1    Odrljin, T.2    Francis, C.W.3
  • 24
    • 0020264236 scopus 로고
    • Fibronectin and fi brin provide a provisional matrix for epidermal cell migration During wound reepithelialization
    • Clark RA, Lanigan JM, DellaPelle P, Manseau E, Dvorak HF, Colvin RB (1982) Fibronectin and fi brin provide a provisional matrix for epidermal cell migration During wound reepithelialization. J Invest Dermatol 79:264-269
    • (1982) J Invest Dermatol , vol.79 , pp. 264-269
    • Clark, R.A.1    Lanigan, J.M.2    DellaPelle, P.3    Manseau, E.4    Dvorak, H.F.5    Colvin, R.B.6
  • 25
    • 0024459632 scopus 로고
    • Fibrinogen-mediated epidermal cell migration: Structural correlates for fi brinogen function
    • Donaldson DJ, Mahan JT, Amrani D, Hawiger J (1989) Fibrinogen-mediated epidermal cell migration: Structural correlates for fi brinogen function. J Cell Sci 94:101-108
    • (1989) J Cell Sci , vol.94 , pp. 101-108
    • Donaldson, D.J.1    Mahan, J.T.2    Amrani, D.3    Hawiger, J.4
  • 26
    • 84860531948 scopus 로고    scopus 로고
    • GPIIb/IIIa inhibitors: From bench to bedside and back to bench again
    • Armstrong PC, Peter K (2012) GPIIb/IIIa inhibitors: From bench to bedside and back to bench again. Thromb Haemost 107:808-814
    • (2012) Thromb Haemost , vol.107 , pp. 808-814
    • Armstrong, P.C.1    Peter, K.2
  • 28
    • 84877079892 scopus 로고    scopus 로고
    • Tropoelastin - A multifaceted naturally smart material
    • Mithieux SM, Wise SG, Weiss AS (2013) Tropoelastin - A multifaceted naturally smart material. Adv Drug Deliv Rev 65:421-428
    • (2013) Adv Drug Deliv Rev , vol.65 , pp. 421-428
    • Mithieux, S.M.1    Wise, S.G.2    Weiss, A.S.3
  • 29
    • 33746943302 scopus 로고    scopus 로고
    • Elastic fi bres in health and disease
    • Kielty CM (2006) Elastic fi bres in health and disease. Expert Rev Mol Med 8:1-23
    • (2006) Expert Rev Mol Med , vol.8 , pp. 1-23
    • Kielty, C.M.1
  • 30
    • 0035232015 scopus 로고    scopus 로고
    • Lysyl oxidases: A novel multifunctional amine oxidase family
    • Csiszar K (2001) Lysyl oxidases: A novel multifunctional amine oxidase family. Prog Nucleic Acid Res Mol Biol 70:1-32
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.70 , pp. 1-32
    • Csiszar, K.1
  • 31
    • 33846013585 scopus 로고    scopus 로고
    • A tissue-specifi c variant of the human lysyl oxidase-like protein 3 (LOXL3) functions as an amine oxidase with substrate specifi city
    • Lee JE, Kim Y (2006) A tissue-specifi c variant of the human lysyl oxidase-like protein 3 (LOXL3) functions as an amine oxidase with substrate specifi city. J Biol Chem 281:37282-37290
    • (2006) J Biol Chem , vol.281 , pp. 37282-37290
    • Lee, J.E.1    Kim, Y.2
  • 32
    • 78651102861 scopus 로고    scopus 로고
    • The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin
    • Kim YM, Kim EC, Kim Y (2011) The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin. Mol Biol Rep 38:145-149
    • (2011) Mol Biol Rep , vol.38 , pp. 145-149
    • Kim, Y.M.1    Kim, E.C.2    Kim, Y.3
  • 33
    • 0028263645 scopus 로고
    • 67-kD elastinbinding protein is a protective companion' of extracellular insoluble elastin and intracellular tropoelastin
    • Hinek A, Rabinovitch M (1994) 67-kD elastinbinding protein is a protective companion' of extracellular insoluble elastin and intracellular tropoelastin. J Cell Biol 126:563-574
    • (1994) J Cell Biol , vol.126 , pp. 563-574
    • Hinek, A.1    Rabinovitch, M.2
  • 39
    • 2542431944 scopus 로고    scopus 로고
    • Deposition of tropoelastin into the extracellular matrix requires a competent elastic fi ber scaffold but not live cells
    • Kozel BA, Ciliberto CH, Mecham RP (2004) Deposition of tropoelastin into the extracellular matrix requires a competent elastic fi ber scaffold but not live cells. Matrix Biol 23:23-34
    • (2004) Matrix Biol , vol.23 , pp. 23-34
    • Kozel, B.A.1    Ciliberto, C.H.2    Mecham, R.P.3
  • 40
    • 84865844525 scopus 로고    scopus 로고
    • Elastin in large artery stiffness and hypertension
    • Wagenseil JE, Mecham RP (2012) Elastin in large artery stiffness and hypertension. J Cardiovasc Transl Res 5:264-273
    • (2012) J Cardiovasc Transl Res , vol.5 , pp. 264-273
    • Wagenseil, J.E.1    Mecham, R.P.2
  • 42
    • 33751009077 scopus 로고    scopus 로고
    • Sequences and domain structures of mammalian, avian, amphibian, and teleost tropoelastins: Clues to the evolutionary history of elastin
    • Chung MI, Miao M, Stahl RJ, Chan E, Parkinson J, Keeley FW (2006) Sequences and domain structures of mammalian, avian, amphibian, and teleost tropoelastins: Clues to the evolutionary history of elastin. Matrix Biol 25:495-504
    • (2006) Matrix Biol , vol.25 , pp. 495-504
    • Chung, M.I.1    Miao, M.2    Stahl, R.J.3    Chan, E.4    Parkinson, J.5    Keeley, F.W.6
  • 46
    • 67650875881 scopus 로고    scopus 로고
    • Vascular extracellular matrix and arterial mechanics
    • Wagenseil JE, Mecham RP (2009) Vascular extracellular matrix and arterial mechanics. Physiol Rev 89:957-989
    • (2009) Physiol Rev , vol.89 , pp. 957-989
    • Wagenseil, J.E.1    Mecham, R.P.2
  • 47
    • 84892544343 scopus 로고    scopus 로고
    • Age-related changes in structure and extracellular matrix protein expression levels in rat tendons
    • Kostrominova TY, Brooks SV (2013) Age-related changes in structure and extracellular matrix protein expression levels in rat tendons. Age 35:2203-2214
    • (2013) Age , vol.35 , pp. 2203-2214
    • Kostrominova, T.Y.1    Brooks, S.V.2
  • 48
    • 33846670534 scopus 로고    scopus 로고
    • Ageing of the conduit arteries
    • Greenwald SJ (2008) Ageing of the conduit arteries. J Pathol 211:157-172
    • (2008) J Pathol , vol.211 , pp. 157-172
    • Greenwald, S.J.1
  • 49
    • 0032916924 scopus 로고    scopus 로고
    • Increased expression of matrix metalloproteinase-2 in the thickened intima of aged rats
    • Li Z, Froehlich J, Galis ZS, Lakatta EG (1999) Increased expression of matrix metalloproteinase-2 in the thickened intima of aged rats. Hypertension 33:116-123
    • (1999) Hypertension , vol.33 , pp. 116-123
    • Li, Z.1    Froehlich, J.2    Galis, Z.S.3    Lakatta, E.G.4
  • 50
    • 0030824354 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their inhibitors in anuerysm and normal aorta
    • Tamarina NA, McMillan WD, Shively VP, Pearce WH (1999) Expression of matrix metalloproteinases and their inhibitors in anuerysm and normal aorta. Surgery 122:264-271
    • (1999) Surgery , vol.122 , pp. 264-271
    • Tamarina, N.A.1    McMillan, W.D.2    Shively, V.P.3    Pearce, W.H.4
  • 51
    • 0032190478 scopus 로고    scopus 로고
    • Local overexpression of TIMP-1 prevents aortic aneurysm degeneration and rupture in a rat model
    • Allaire E, Forough R, Clowes M, Starcher B, Clowes AW (1998) Local overexpression of TIMP-1 prevents aortic aneurysm degeneration and rupture in a rat model. J Clin Invest 102:1413-1420
    • (1998) J Clin Invest , vol.102 , pp. 1413-1420
    • Allaire, E.1    Forough, R.2    Clowes, M.3    Starcher, B.4    Clowes, A.W.5
  • 54
    • 0014767651 scopus 로고
    • Response of the rat aortic media to hypertension Morphological and chemical studies
    • Wolinsky H (1970) Response of the rat aortic media to hypertension. Morphological and chemical studies. Circ Res 26:507-522
    • (1970) Circ Res , vol.26 , pp. 507-522
    • Wolinsky, H.1
  • 55
    • 0023867659 scopus 로고
    • Altered elastin and collagen synthesis associated with progressive pulmonary hypertension induced by monocrotaline A biochemical and ultrastructural study
    • Todorovich-Hunter L, Johnson D, Ranger P, Keeley F, Rabinovitch M (1988) Altered elastin and collagen synthesis associated with progressive pulmonary hypertension induced by monocrotaline. A biochemical and ultrastructural study. Lab Invest 58:184-195
    • (1988) Lab Invest , vol.58 , pp. 184-195
    • Todorovich-Hunter, L.1    Johnson, D.2    Ranger, P.3    Keeley, F.4    Rabinovitch, M.5
  • 64
    • 0028267099 scopus 로고
    • Structure and expression of fi brillin-2, a novel microfi brillar component preferentially located in elastic matrices
    • Zhang H, Apfelroth SD, Hu W, Davis EC, Sanguineti C, Bonadio J, Mecham RP, Ramirez F (1994) Structure and expression of fi brillin-2, a novel microfi brillar component preferentially located in elastic matrices. J Cell Biol 124: 855-863
    • (1994) J Cell Biol , vol.124 , pp. 855-863
    • Zhang, H.1    Apfelroth, S.D.2    Hu, W.3    Davis, E.C.4    Sanguineti, C.5    Bonadio, J.6    Mecham, R.P.7    Ramirez, F.8
  • 68
    • 0028902039 scopus 로고
    • A mutation in FBN1 disrupts profi brillin processing and results in isolated skeletal features of the Marfan syndrome
    • Milewicz DM, Grossfi eld J, Cao SN, Kielty C, Covitz W, Jewett T (1995) A mutation in FBN1 disrupts profi brillin processing and results in isolated skeletal features of the Marfan syndrome. J Clin Invest 95:2373-2378
    • (1995) J Clin Invest , vol.95 , pp. 2373-2378
    • Milewicz, D.M.1    Grossfield, J.2    Cao, S.N.3    Kielty, C.4    Covitz, W.5    Jewett, T.6
  • 70
    • 79958819483 scopus 로고    scopus 로고
    • Homocysteine modifi es structural and functional properties of fi bronectin and interferes with the fi bronectin-fi brillin-1 interaction
    • Hubmacher D, Sabatier L, Annis DS, Mosher DF, Reinhardt DP (2011) Homocysteine modifi es structural and functional properties of fi bronectin and interferes with the fi bronectin-fi brillin-1 interaction. Biochemistry 50:5322-5332
    • (2011) Biochemistry , vol.50 , pp. 5322-5332
    • Hubmacher, D.1    Sabatier, L.2    Annis, D.S.3    Mosher, D.F.4    Reinhardt, D.P.5
  • 71
    • 77953494050 scopus 로고    scopus 로고
    • Unraveling the mechanism of elastic fi ber assembly: The roles of short fi bulins
    • Yanagisawa H, Davis EC (2010) Unraveling the mechanism of elastic fi ber assembly: The roles of short fi bulins. Int J Biochem Cell Biol 42:1084-1093
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 1084-1093
    • Yanagisawa, H.1    Davis, E.C.2
  • 74
    • 72449168333 scopus 로고    scopus 로고
    • Fibulin-5, an integrin-binding matricellular protein: Its function in Development and disease
    • Yanagisawa H, Schluterman MK, Brekken RA (2009) Fibulin-5, an integrin-binding matricellular protein: Its function in Development and disease. J Cell Commun Signal 3:337-347
    • (2009) J Cell Commun Signal , vol.3 , pp. 337-347
    • Yanagisawa, H.1    Schluterman, M.K.2    Brekken, R.A.3
  • 79
    • 34248167590 scopus 로고    scopus 로고
    • Distinct steps of cross-linking, self-Association, and maturation of tropoelastin are necessary for elastic fi ber formation
    • Sato F, Wachi H, Ishida M, Nonaka R, Onoue S, Urban Z, Starcher BC, Seyama Y (2007) Distinct steps of cross-linking, self-Association, and maturation of tropoelastin are necessary for elastic fi ber formation. J Mol Biol 369:841-851
    • (2007) J Mol Biol , vol.369 , pp. 841-851
    • Sato, F.1    Wachi, H.2    Ishida, M.3    Nonaka, R.4    Onoue, S.5    Urban, Z.6    Starcher, B.C.7    Seyama, Y.8
  • 80
    • 3142714511 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase- 3 (TIMP-3) is a binding partner of epithelial growth factor-containing fi bulin-like extracellular matrix protein 1 (EFEMP1): Implications for macular degenerations
    • Klenotic PA, Munier FL, Marmorstein LY, Anand- Apte B (2004) Tissue inhibitor of metalloproteinase- 3 (TIMP-3) is a binding partner of epithelial growth factor-containing fi bulin-like extracellular matrix protein 1 (EFEMP1): Implications for macular degenerations. J Biol Chem 279:30469-30473
    • (2004) J Biol Chem , vol.279 , pp. 30469-30473
    • Klenotic, P.A.1    Munier, F.L.2    Marmorstein, L.Y.3    Anand- Apte, B.4
  • 81
    • 34848842170 scopus 로고    scopus 로고
    • Fibrillin-rich microfi - brils: Structural determinants of morphogenetic and homeostatic events
    • Ramirez F, Dietz HC (2007) Fibrillin-rich microfi - brils: Structural determinants of morphogenetic and homeostatic events. J Cell Physiol 213:326-330
    • (2007) J Cell Physiol , vol.213 , pp. 326-330
    • Ramirez, F.1    Dietz, H.C.2
  • 82
    • 69949132246 scopus 로고    scopus 로고
    • Fibulins: Multiple roles in matrix structures and tissue functions
    • DeVega A, Iwamoto T, Yamada Y (2009) Fibulins: Multiple roles in matrix structures and tissue functions. Cell Mol Life Sci 66:1890-1902
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1890-1902
    • DeVega, A.1    Iwamoto, T.2    Yamada, Y.3
  • 83
    • 0029935171 scopus 로고    scopus 로고
    • Fibulin-1 and fi bulin-2 expression During organogenesis in the developing mouse embryo
    • Zhang HY, Timpl R, Sasaki T, Chu ML, Ekblom P (1996) Fibulin-1 and fi bulin-2 expression During organogenesis in the developing mouse embryo. Dev Dyn 205:348-364
    • (1996) Dev Dyn , vol.205 , pp. 348-364
    • Zhang, H.Y.1    Timpl, R.2    Sasaki, T.3    Chu, M.L.4    Ekblom, P.5
  • 84
    • 0034873979 scopus 로고    scopus 로고
    • Fibulin-2 expression marks transformed mesenchymal cells in Developing cardiac valves, aortic arch vessels and coronary vessels
    • Tsuda T, Wang H, Timpl R, Chu ML (2001) Fibulin-2 expression marks transformed mesenchymal cells in Developing cardiac valves, aortic arch vessels and coronary vessels. Dev Dyn 222:89-100
    • (2001) Dev Dyn , vol.222 , pp. 89-100
    • Tsuda, T.1    Wang, H.2    Timpl, R.3    Chu, M.L.4
  • 86
    • 67349268473 scopus 로고    scopus 로고
    • The regulation of tenascin expression by tissue microenvironments
    • Tucker RP, Chiquet-Ehrismann R (2009) The regulation of tenascin expression by tissue microenvironments. Biochim Biophys Acta 1793:888-892
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 888-892
    • Tucker, R.P.1    Chiquet-Ehrismann, R.2
  • 87
    • 84856750390 scopus 로고    scopus 로고
    • Matricellular proteins: New molecular targets to prevent heart failure
    • Okamoto H, Imanaka-Yoshida K (2012) Matricellular proteins: New molecular targets to prevent heart failure. Cardiovasc Ther 30:e198-e209
    • (2012) Cardiovasc Ther , vol.30
    • Okamoto, H.1    Imanaka-Yoshida, K.2
  • 89
    • 0035576810 scopus 로고    scopus 로고
    • Interference of tenascin-C with syndecan-4 binding to fi bronectin blocks cell adhesion and stimulates tumor cell proliferation
    • Huang W, Chiquet-Ehrismann R, Moyano JV, Garcia-Pardo V, Orend G (2001) Interference of tenascin-C with syndecan-4 binding to fi bronectin blocks cell adhesion and stimulates tumor cell proliferation. Cancer Res 61:8586-8594
    • (2001) Cancer Res , vol.61 , pp. 8586-8594
    • Huang, W.1    Chiquet-Ehrismann, R.2    Moyano, J.V.3    Garcia-Pardo, V.4    Orend, G.5
  • 90
    • 0036800346 scopus 로고    scopus 로고
    • Tenascin-C modulates matrix contraction via focal adhesion kinase- And Rho-mediated signaling pathways
    • Midwood KS, Schwarzbauer JS (2002) Tenascin-C modulates matrix contraction via focal adhesion kinase- And Rho-mediated signaling pathways. Mol Biol Cell 13:3601-3613
    • (2002) Mol Biol Cell , vol.13 , pp. 3601-3613
    • Midwood, K.S.1    Schwarzbauer, J.S.2
  • 91
    • 0038236713 scopus 로고    scopus 로고
    • Regulation and putative functions during pathological stress
    • Chiquet-Ehrismann R, Chiquet M (2003) Regulation and putative functions during pathological stress. J Pathol 200:488-499
    • (2003) J Pathol , vol.200 , pp. 488-499
    • Chiquet-Ehrismann, R.1    Chiquet, M.2
  • 92
    • 0034117025 scopus 로고    scopus 로고
    • The tenascin family of ECM glycoproteins: Structure, function, and regulation During embryonic development and tissue remodeling
    • Jones FS, Jones PL (2000) The tenascin family of ECM glycoproteins: Structure, function, and regulation During embryonic development and tissue remodeling. Dev Dyn 218:235-259
    • (2000) Dev Dyn , vol.218 , pp. 235-259
    • Jones, F.S.1    Jones, P.L.2
  • 93
    • 84867403336 scopus 로고    scopus 로고
    • Effects of mechanical strain on human mesenchymal stem cells and ligament fi broblasts in a textured poly(L-lactide) scaffold for ligament tissue engineering
    • Kreja L, Liedert A, Schlenker H, Brenner RE, Fiedler J, Friemert B, DÜrselen L, Ignatius A (2012) Effects of mechanical strain on human mesenchymal stem cells and ligament fi broblasts in a textured poly(L-lactide) scaffold for ligament tissue engineering. J Mater Sci Mater Med 23:2575-2582
    • (2012) J Mater Sci Mater Med , vol.23 , pp. 2575-2582
    • Kreja, L.1    Liedert, A.2    Schlenker, H.3    Brenner, R.E.4    Fiedler, J.5    Friemert, B.6    Dürselen, L.7    Ignatius, A.8
  • 94
    • 0037348805 scopus 로고    scopus 로고
    • Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle
    • Järvinen TA, Józsa L, Kannus P, Järvinen TL, Hurme T, Kvist M, Pelto-Huikko M, Kalimo H, Järvinen M (2003) Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle. J Cell Sci 116:857-866
    • (2003) J Cell Sci , vol.116 , pp. 857-866
    • Järvinen, T.A.1    Józsa, L.2    Kannus, P.3    Järvinen, T.L.4    Hurme, T.5    Kvist, M.6    Pelto-Huikko, M.7    Kalimo, H.8    Järvinen, M.9
  • 95
  • 97
    • 84872668477 scopus 로고    scopus 로고
    • Tenascin-C levels in synovial fl uid are elevated after injury to the human and canine joint and correlate with markers of infl ammation and matrix degradation
    • Chockalingam PS, Glasson SS, Lohmander LS (2013) Tenascin-C levels in synovial fl uid are elevated after injury to the human and canine joint and correlate with markers of infl ammation and matrix degradation. Osteoarthritis Cartilage 21:339-345
    • (2013) Osteoarthritis Cartilage , vol.21 , pp. 339-345
    • Chockalingam, P.S.1    Glasson, S.S.2    Lohmander, L.S.3
  • 98
    • 84869129525 scopus 로고    scopus 로고
    • Tenascin-C in cardiovascular tissue remodeling: From development to infl ammation and repair
    • Imanaka-Yoshida K (2012) Tenascin-C in cardiovascular tissue remodeling: From development to infl ammation and repair. Circ J 76:2513-2520
    • (2012) Circ J , vol.76 , pp. 2513-2520
    • Imanaka-Yoshida, K.1
  • 101
    • 0033740717 scopus 로고    scopus 로고
    • Rapid and reciprocal regulation of tenascin-C and tenascin- Y expression by loading of skeletal muscle
    • FlÜck M, Tunc-Civelek V, Chiquet M (2000) Rapid and reciprocal regulation of tenascin-C and tenascin- Y expression by loading of skeletal muscle. J Cell Sci 113:3583-3591
    • (2000) J Cell Sci , vol.113 , pp. 3583-3591
    • FlÜck, M.1    Tunc-Civelek, V.2    Chiquet, M.3
  • 102
    • 67349089040 scopus 로고    scopus 로고
    • From mechanostransduction to extracellular matrix gene expression in fi broblasts
    • Chiquet M, Gelman L, Lutz R, Maier S (2009) From mechanostransduction to extracellular matrix gene expression in fi broblasts. Biochim Biophys Acta 1793:911-920
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 911-920
    • Chiquet, M.1    Gelman, L.2    Lutz, R.3    Maier, S.4
  • 103
    • 0029822205 scopus 로고    scopus 로고
    • Tenascin-Y: A protein of novel domain structure is secreted by differentiated fi broblasts of muscle connective tissue
    • Hagios C, Koch M, Spring J, Chiquet M, Chiquet- Ehrismann R (1996) Tenascin-Y: A protein of novel domain structure is secreted by differentiated fi broblasts of muscle connective tissue. J Cell Biol 134:1499-1512
    • (1996) J Cell Biol , vol.134 , pp. 1499-1512
    • Hagios, C.1    Koch, M.2    Spring, J.3    Chiquet, M.4    Chiquet- Ehrismann, R.5
  • 104
    • 0028232965 scopus 로고
    • Appearance of the myofi broblastic phenotype in Dupuytren's disease is associated with a fi bronectin, laminin, collagen type IV and tenascin extracellular matrix
    • Berndt A, Kosmehl H, Katenkamp D, Tauchmann V (1994) Appearance of the myofi broblastic phenotype in Dupuytren's disease is associated with a fi bronectin, laminin, collagen type IV and tenascin extracellular matrix. Pathobiology 62:55-58
    • (1994) Pathobiology , vol.62 , pp. 55-58
    • Berndt, A.1    Kosmehl, H.2    Katenkamp, D.3    Tauchmann, V.4
  • 107
    • 84857790767 scopus 로고    scopus 로고
    • Thrombospondins in physiology and disease: New tricks for old dogs
    • Murphy-Ullrich JE, Iozzo RV (2012) Thrombospondins in physiology and disease: New tricks for old dogs. Matrix Biol 31:152-154
    • (2012) Matrix Biol , vol.31 , pp. 152-154
    • Murphy-Ullrich, J.E.1    Iozzo, R.V.2
  • 110
    • 84857791001 scopus 로고    scopus 로고
    • Adhesion-modulating/ matricellular ECM protein families: A structural, functional and evolutionary appraisal
    • Mosher DF, Adams JC (2012) Adhesion-modulating/ matricellular ECM protein families: A structural, functional and evolutionary appraisal. Matrix Biol 31:155-161
    • (2012) Matrix Biol , vol.31 , pp. 155-161
    • Mosher, D.F.1    Adams, J.C.2
  • 111
    • 79959473807 scopus 로고    scopus 로고
    • Blockade of TSP-1 dependent TGF-beta activity reduces renal injury and proteinuria in a murine model of diabetic nephropathy
    • Lu A, Miao M, Schoeb TR, Agarwal A, Murphy- Ullrich JE (2011) Blockade of TSP-1 dependent TGF-beta activity reduces renal injury and proteinuria in a murine model of diabetic nephropathy. Am J Pathol 178:2573-2586
    • (2011) Am J Pathol , vol.178 , pp. 2573-2586
    • Lu, A.1    Miao, M.2    Schoeb, T.R.3    Agarwal, A.4    Murphy- Ullrich, J.E.5
  • 112
    • 34548827039 scopus 로고    scopus 로고
    • A thrombospondin-1 antagonist of transforming growth factor-beta activation blocks cardiomyopathy in rats with diabetes and elevated angiotensin II
    • Belmadani S, Bernal J, Wei CC, Pallero MA, Dell'italia L, Murphy-Ullrich JE, Brecek KH (2007) A thrombospondin-1 antagonist of transforming growth factor-beta activation blocks cardiomyopathy in rats with diabetes and elevated angiotensin II. Am J Pathol 171:777-789
    • (2007) Am J Pathol , vol.171 , pp. 777-789
    • Belmadani, S.1    Bernal, J.2    Wei, C.C.3    Pallero, M.A.4    Dell'italia, L.5    Murphy-Ullrich, J.E.6    Brecek, K.H.7
  • 114
    • 17844395977 scopus 로고    scopus 로고
    • Constitutive thrombospondin-1 overexpression contributes to autocrine transforming growth factor-beta signaling in cultured scleroderma fi broblasts
    • Mimura Y, Ihn H, Jinnin M, Assano Y, Yamane K, Tamaki K (2005) Constitutive thrombospondin-1 overexpression contributes to autocrine transforming growth factor-beta signaling in cultured scleroderma fi broblasts. Am J Pathol 166:1451-1463
    • (2005) Am J Pathol , vol.166 , pp. 1451-1463
    • Mimura, Y.1    Ihn, H.2    Jinnin, M.3    Assano, Y.4    Yamane, K.5    Tamaki, K.6
  • 115
    • 84857788858 scopus 로고    scopus 로고
    • Thrombospondin1 in tissue repair and fi brosis: TGF- β- dependent and independent mechanisms
    • Sweetwyne MT, Murphy-Ullrich JE (2012) Thrombospondin1 in tissue repair and fi brosis: TGF- β- dependent and independent mechanisms. Matrix Biol 31:178-186
    • (2012) Matrix Biol , vol.31 , pp. 178-186
    • Sweetwyne, M.T.1    Murphy-Ullrich, J.E.2
  • 116
    • 84867704506 scopus 로고    scopus 로고
    • Activated CD47 regulates multiple vascular and stress responses: Implications for acute kidney injury and its management
    • Rogers NM, Yao M, Novelli EM, Thomson AW, Roberts DD, Isenberg JS (2012) Activated CD47 regulates multiple vascular and stress responses: Implications for acute kidney injury and its management. Am J Physiol Renal Physiol 303:F1117-F1125
    • (2012) Am J Physiol Renal Physiol , vol.303
    • Rogers, N.M.1    Yao, M.2    Novelli, E.M.3    Thomson, A.W.4    Roberts, D.D.5    Isenberg, J.S.6
  • 117
    • 0036731861 scopus 로고    scopus 로고
    • The lack of thrombospondin-1 (TSP1) dictates the course of wound healing in Double-TSP1/ TSP/2-null mice
    • Agah A, Kyriakides TR, Lawler J, Bornstein P (2002) The lack of thrombospondin-1 (TSP1) dictates the course of wound healing in Double-TSP1/ TSP/2-null mice. Am J Pathol 161:831-839
    • (2002) Am J Pathol , vol.161 , pp. 831-839
    • Agah, A.1    Kyriakides, T.R.2    Lawler, J.3    Bornstein, P.4
  • 118
    • 56749149615 scopus 로고    scopus 로고
    • Correlation of enhanced thrombospondin-1 expression TGF-beta signalling, and proteinuria in human type-2 diabetic nephropathy
    • Hohenstein B, Daniel C, Hausknecht B, Boehmer K, Riess R, Amann KU, Hugo CP (2008) Correlation of enhanced thrombospondin-1 expression, TGF-beta signalling, and proteinuria in human type-2 diabetic nephropathy. Nephrol Dial Transplant 23:3880-3887
    • (2008) Nephrol Dial Transplant , vol.23 , pp. 3880-3887
    • Hohenstein, B.1    Daniel, C.2    Hausknecht, B.3    Boehmer, K.4    Riess, R.5    Amann, K.U.6    Hugo, C.P.7
  • 119
    • 0033574442 scopus 로고    scopus 로고
    • Pro-Adhesive and chemotactic activities of thrombospondin-1 for breast carcinoma cells are mediated by alpha3beta1 integrin and regulated by insulin-like growth factor-1 and CD98
    • Chandrasekaran S, Guo NH, Rodrigues RG, Kaiser J, Roberts DD (1999) Pro-Adhesive and chemotactic activities of thrombospondin-1 for breast carcinoma cells are mediated by alpha3beta1 integrin and regulated by insulin-like growth factor-1 and CD98. J Biol Chem 274:11408-11416
    • (1999) J Biol Chem , vol.274 , pp. 11408-11416
    • Chandrasekaran, S.1    Guo, N.H.2    Rodrigues, R.G.3    Kaiser, J.4    Roberts, D.D.5
  • 120
    • 0029765458 scopus 로고    scopus 로고
    • Binding and degradation of thrombospondin-1 mediated through heparan sulfate proteoglucans and low-density-lipoprotein receptor-related protein: Localization of the functional activity to the trimeric N-Terminal heparin-binding region of thrombospondin-1
    • Chen H, Sottile J, Strickland DK, Mosher DF (1996) Binding and degradation of thrombospondin-1 mediated through heparan sulfate proteoglucans and low-density-lipoprotein receptor-related protein: Localization of the functional activity to the trimeric N-Terminal heparin-binding region of thrombospondin-1. Biochem J 318:959-963
    • (1996) Biochem J , vol.318 , pp. 959-963
    • Chen, H.1    Sottile, J.2    Strickland, D.K.3    Mosher, D.F.4
  • 121
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-beta by thrombospondin-1: Mechanism and physiology
    • Murphy-Ullrich JE, Poczatek M (2000) Activation of latent TGF-beta by thrombospondin-1: Mechanism and physiology. Cytokine Growth Factor Rev 11:59-69
    • (2000) Cytokine Growth Factor Rev , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 122
    • 16544391915 scopus 로고    scopus 로고
    • The N-Terminus of thrombospondin: The domain stands apart
    • Elzie CA, Murphy-Ullrich JE (2004) The N-Terminus of thrombospondin: The domain stands apart. Int J Biochem Cell Biol 36:1090-1101
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1090-1101
    • Elzie, C.A.1    Murphy-Ullrich, J.E.2
  • 123
    • 0032896852 scopus 로고    scopus 로고
    • Thrombospondin-1 induces tyrosine phosphorylation of adherens junction proteins and regulates an endothelial paracellular pathway
    • Goldblum SE, Young BA, Wang P, Murphy-Ullrich JE (1999) Thrombospondin-1 induces tyrosine phosphorylation of adherens junction proteins and regulates an endothelial paracellular pathway. Mol Biol Cell 10:1537-1551
    • (1999) Mol Biol Cell , vol.10 , pp. 1537-1551
    • Goldblum, S.E.1    Young, B.A.2    Wang, P.3    Murphy-Ullrich, J.E.4
  • 124
    • 84857787530 scopus 로고    scopus 로고
    • The matricellular protein thrombospondin- 1 globally regulates cardiovascular function and responses to stress via CD47
    • Robert DD, Miller TW, Rogers NM, Yao M, Isenberg JS (2012) The matricellular protein thrombospondin- 1 globally regulates cardiovascular function and responses to stress via CD47. Matrix Biol 31:162-169
    • (2012) Matrix Biol , vol.31 , pp. 162-169
    • Robert, D.D.1    Miller, T.W.2    Rogers, N.M.3    Yao, M.4    Isenberg, J.S.5
  • 125
    • 43149117914 scopus 로고    scopus 로고
    • Peter plus syndrome is a new congenital disorder of glycosylation and involves defective O-glycosylation of thrombospondin type 1 repeats
    • Hess D, Keusch JJ, Lesnik Oberstein SA, Hennekam RC, Hofsteenge J (2008) Peter plus syndrome is a new congenital disorder of glycosylation and involves defective O-glycosylation of thrombospondin type 1 repeats. J Biol Chem 283:7354-7360
    • (2008) J Biol Chem , vol.283 , pp. 7354-7360
    • Hess, D.1    Keusch, J.J.2    Lesnik Oberstein, S.A.3    Hennekam, R.C.4    Hofsteenge, J.5
  • 126
    • 60549083110 scopus 로고    scopus 로고
    • Peters'-plus syndrome is a congenital disorder of glycosylation caused by a defect in the beta1,3-glucosyltransferase that modifi es thrombospondin type 1 repeats
    • Heinonen TY, Maki M (2009) Peters'-plus syndrome is a congenital disorder of glycosylation caused by a defect in the beta1,3-glucosyltransferase that modifi es thrombospondin type 1 repeats. Ann Med 41:2-10
    • (2009) Ann Med , vol.41 , pp. 2-10
    • Heinonen, T.Y.1    Maki, M.2
  • 127
    • 77956017877 scopus 로고    scopus 로고
    • Severe Peters Plus syndrome-like phenotype with anterior eye staphyloma and hypoplastic left heart syndrome: Proposal of a new syndrome
    • Kyoto
    • Shimizu R, Saito R, Hoshino K, Ogawa K, Negishi T, Nishimura J, Mitsui N, Osawa M, Ohashi H (2010) Severe Peters Plus syndrome-like phenotype with anterior eye staphyloma and hypoplastic left heart syndrome: Proposal of a new syndrome. Congenit Anom (Kyoto) 50:197-199
    • (2010) Congenit Anom , vol.50 , pp. 197-199
    • Shimizu, R.1    Saito, R.2    Hoshino, K.3    Ogawa, K.4    Negishi, T.5    Nishimura, J.6    Mitsui, N.7    Osawa, M.8    Ohashi, H.9
  • 129
    • 77950467353 scopus 로고    scopus 로고
    • Intensive intracorneal keloid formation in a case of Peters plus syndrome and in Peters anomaly with maximum manifestation
    • Eberwein P, Reinhard T, Agostini H, Poloschek CM, Guthoff R, Auw-Haedrich C (2010) Intensive intracorneal keloid formation in a case of Peters plus syndrome and in Peters anomaly with maximum manifestation. Ophthalmologe 107:178-181
    • (2010) Ophthalmologe , vol.107 , pp. 178-181
    • Eberwein, P.1    Reinhard, T.2    Agostini, H.3    Poloschek, C.M.4    Guthoff, R.5    Auw-Haedrich, C.6
  • 130
    • 0026499722 scopus 로고
    • COMP (cartilage oligomeric matrix protein) is structurally related to thrombospondins
    • Oldberg Å, Antonssen P, Lindholm K, Heinegård D (1992) COMP (cartilage oligomeric matrix protein) is structurally related to thrombospondins. J Biol Chem 267:22346-22350
    • (1992) J Biol Chem , vol.267 , pp. 22346-22350
    • Oldberg Å Antonssen, P.1    Lindholm, K.2    Heinegård, D.3
  • 131
    • 77951296975 scopus 로고    scopus 로고
    • Cartilage oligometric matrix protein promotes cell attachment via two independent mechanisms involving CD47 and aVβ3 integrin
    • Rock MJ, Holden P, Horton WA, Cohn DH (2010) Cartilage oligometric matrix protein promotes cell attachment via two independent mechanisms involving CD47 and aVβ3 integrin. Mol Cell Biochem 338:215-224
    • (2010) Mol Cell Biochem , vol.338 , pp. 215-224
    • Rock, M.J.1    Holden, P.2    Horton, W.A.3    Cohn, D.H.4
  • 132
    • 0035937135 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein interacts with type IX collagen, and disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family
    • Holden P, Meadows RS, Chapman KL, Grant ME, Kadler KE, Briggs MD (2001) Cartilage oligomeric matrix protein interacts with type IX collagen, and disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family. J Biol Chem 276:6046-6055
    • (2001) J Biol Chem , vol.276 , pp. 6046-6055
    • Holden, P.1    Meadows, R.S.2    Chapman, K.L.3    Grant, M.E.4    Kadler, K.E.5    Briggs, M.D.6
  • 133
    • 0032493665 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein shows high affi nity zinc-dependent interaction with triple helical collagen
    • Rosenberg K, Olsson H, Mörgelin M, Heinegård D (1998) Cartilage oligomeric matrix protein shows high affi nity zinc-dependent interaction with triple helical collagen. J Biol Chem 273:20397-20403
    • (1998) J Biol Chem , vol.273 , pp. 20397-20403
    • Rosenberg, K.1    Olsson, H.2    Mörgelin, M.3    Heinegård, D.4
  • 134
    • 0028090357 scopus 로고
    • Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon
    • Di Cesare P, Hauser N, Lehman D, Pasumarti S, Paulsson M (1994) Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon. FEBS Lett 354:237-240
    • (1994) FEBS Lett , vol.354 , pp. 237-240
    • Di Cesare, P.1    Hauser, N.2    Lehman, D.3    Pasumarti, S.4    Paulsson, M.5
  • 135
    • 71449114734 scopus 로고    scopus 로고
    • Proteoglycans and more - from molecules to biology
    • Heinegård D (2009) Proteoglycans and more - from molecules to biology. Int J Exp Path 70:575-586
    • (2009) Int J Exp Path , vol.70 , pp. 575-586
    • Heinegård, D.1
  • 136
    • 0031282595 scopus 로고    scopus 로고
    • The distribution of cartilage oligomeric matrix protein (COMP) in tendon and its variation with tendon site, age and load
    • Smith RKW, Zunino L, Webbon PM, Heinegård D (1997) The distribution of cartilage oligomeric matrix protein (COMP) in tendon and its variation with tendon site, age and load. Matrix Biol 16:255-271
    • (1997) Matrix Biol , vol.16 , pp. 255-271
    • Smith, R.K.W.1    Zunino, L.2    Webbon, P.M.3    Heinegård, D.4
  • 137
    • 84872136816 scopus 로고    scopus 로고
    • Immunolocalization of collagens I and III) and cartilage oligomeric matrix protein in the normal and injured equine superfi cial digital fl exor tendon
    • Södersten F, Hultenby K, Heinegård D, Johnston C, Ekman S (2013) Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein in the normal and injured equine superfi cial digital fl exor tendon. Connect Tissue Res 54:62-69
    • (2013) Connect Tissue Res , vol.54 , pp. 62-69
    • Södersten, F.1    Hultenby, K.2    Heinegård, D.3    Johnston, C.4    Ekman, S.5
  • 139
    • 50249149816 scopus 로고    scopus 로고
    • COMP: A candidate molecule in the pathogenesis of systemic sclerosis with a potential as a disease marker
    • Hesselstrand R, Kassner A, Heinegård D, Saxne T (2008) COMP: A candidate molecule in the pathogenesis of systemic sclerosis with a potential as a disease marker. Ann Rheum Dis 67:1242-1248
    • (2008) Ann Rheum Dis , vol.67 , pp. 1242-1248
    • Hesselstrand, R.1    Kassner, A.2    Heinegård, D.3    Saxne, T.4
  • 140
    • 78650746465 scopus 로고    scopus 로고
    • Increased cartilage oligomeric matrix protein concentrations in equine digital fl exor tendon sheath synovial fl uid predicts interthecal tendon Damage
    • Smith MR, Wright IM, Minshall GJ, Dudhia J, Verheyen K, Heinegård D, Smith RK (2011) Increased cartilage oligomeric matrix protein concentrations in equine digital fl exor tendon sheath synovial fl uid predicts interthecal tendon Damage. Vet Surg 40:54-58
    • (2011) Vet Surg , vol.40 , pp. 54-58
    • Smith, M.R.1    Wright, I.M.2    Minshall, G.J.3    Dudhia, J.4    Verheyen, K.5    Heinegård, D.6    Smith, R.K.7
  • 141
    • 84856150327 scopus 로고    scopus 로고
    • Adamts-7, a novel proteolytic culprit in vascular remodeling
    • Wang L, Wang X, Kong W (2010) ADAMTS-7, a novel proteolytic culprit in vascular remodeling. Sheng Li Xue Bao 62:285-294
    • (2010) Sheng Li Xue Bao , vol.62 , pp. 285-294
    • Wang, L.1    Wang, X.2    Kong, W.3
  • 142
  • 143
    • 0028222276 scopus 로고
    • Regional differences in the distribution of the proteoglycans biglycan and decorin in the extracellular matrix of atherosclerotic and restenotic human coronary arteries
    • Riessen R, Isner JM, Blessing E, Loushin C, Nikol S, Wight TN (1994) Regional differences in the distribution of the proteoglycans biglycan and decorin in the extracellular matrix of atherosclerotic and restenotic human coronary arteries. Am J Pathol 144:962-974
    • (1994) Am J Pathol , vol.144 , pp. 962-974
    • Riessen, R.1    Isner, J.M.2    Blessing, E.3    Loushin, C.4    Nikol, S.5    Wight, T.N.6
  • 145
    • 65849384082 scopus 로고    scopus 로고
    • The role of cartilage oligomeric matrix protein (COMP) in skeletal disease
    • Posey KL, Hecht JT (2008) The role of cartilage oligomeric matrix protein (COMP) in skeletal disease. Curr Drug Targets 9:869-877
    • (2008) Curr Drug Targets , vol.9 , pp. 869-877
    • Posey, K.L.1    Hecht, J.T.2


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