메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages

Secreted protein acidic and rich in cysteine is a matrix scavenger chaperone

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; COLLAGEN FIBRIL; COLLAGEN TYPE 1; FIBRONECTIN; LAMININ; OSTEONECTIN; VITRONECTIN; CALCIUM; CHAPERONE; COLLAGEN; SCLEROPROTEIN;

EID: 80052829995     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023880     Document Type: Article
Times cited : (48)

References (62)
  • 1
    • 72449202606 scopus 로고    scopus 로고
    • The role of SPARC in extracellular matrix assembly
    • Bradshaw AD, (2009) The role of SPARC in extracellular matrix assembly. J Cell Commun Signal 3: 239-246.
    • (2009) J Cell Commun Signal , vol.3 , pp. 239-246
    • Bradshaw, A.D.1
  • 2
    • 75849141781 scopus 로고    scopus 로고
    • Modulation of matrix remodeling by SPARC in neoplastic progression
    • Chlenski A, Cohn SL, (2010) Modulation of matrix remodeling by SPARC in neoplastic progression. Semin Cell Dev Biol 21: 55-65.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 55-65
    • Chlenski, A.1    Cohn, S.L.2
  • 3
    • 3142732175 scopus 로고    scopus 로고
    • Structural variability of BM-40/SPARC/osteonectin glycosylation: implications for collagen affinity
    • Kaufmann B, Muller S, Hanisch FG, Hartmann U, Paulsson M, et al. (2004) Structural variability of BM-40/SPARC/osteonectin glycosylation: implications for collagen affinity. Glycobiology 14: 609-619.
    • (2004) Glycobiology , vol.14 , pp. 609-619
    • Kaufmann, B.1    Muller, S.2    Hanisch, F.G.3    Hartmann, U.4    Paulsson, M.5
  • 4
    • 5644293133 scopus 로고    scopus 로고
    • Neuroblastoma angiogenesis is inhibited with a folded synthetic molecule corresponding to the epidermal growth factor-like module of the follistatin domain of SPARC
    • Chlenski A, Liu S, Baker LJ, Yang Q, Tian Y, et al. (2004) Neuroblastoma angiogenesis is inhibited with a folded synthetic molecule corresponding to the epidermal growth factor-like module of the follistatin domain of SPARC. Cancer Res 64: 7420-7425.
    • (2004) Cancer Res , vol.64 , pp. 7420-7425
    • Chlenski, A.1    Liu, S.2    Baker, L.J.3    Yang, Q.4    Tian, Y.5
  • 5
    • 1842338681 scopus 로고    scopus 로고
    • Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens
    • Sasaki T, Gohring W, Mann K, Maurer P, Hohenester E, et al. (1997) Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J Biol Chem 272: 9237-9243.
    • (1997) J Biol Chem , vol.272 , pp. 9237-9243
    • Sasaki, T.1    Gohring, W.2    Mann, K.3    Maurer, P.4    Hohenester, E.5
  • 6
    • 0024395113 scopus 로고
    • SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix
    • Sage H, Vernon RB, Funk SE, Everitt EA, Angello J, (1989) SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix. J Cell Biol 109: 341-356.
    • (1989) J Cell Biol , vol.109 , pp. 341-356
    • Sage, H.1    Vernon, R.B.2    Funk, S.E.3    Everitt, E.A.4    Angello, J.5
  • 7
    • 0030970685 scopus 로고    scopus 로고
    • Differential modulation of cell adhesion by interaction between adhesive and counter-adhesive proteins: characterization of the binding of vitronectin to osteonectin (BM40, SPARC)
    • Rosenblatt S, Bassuk JA, Alpers CE, Sage EH, Timpl R, et al. (1997) Differential modulation of cell adhesion by interaction between adhesive and counter-adhesive proteins: characterization of the binding of vitronectin to osteonectin (BM40, SPARC). Biochem J 324: 311-319.
    • (1997) Biochem J , vol.324 , pp. 311-319
    • Rosenblatt, S.1    Bassuk, J.A.2    Alpers, C.E.3    Sage, E.H.4    Timpl, R.5
  • 8
    • 31344473092 scopus 로고    scopus 로고
    • Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen
    • Wang H, Workman G, Chen S, Barker TH, Ratner BD, et al. (2006) Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen. Matrix Biol 25: 20-26.
    • (2006) Matrix Biol , vol.25 , pp. 20-26
    • Wang, H.1    Workman, G.2    Chen, S.3    Barker, T.H.4    Ratner, B.D.5
  • 9
    • 0025932742 scopus 로고
    • Osteonectin is an alpha-granule component involved with thrombospondin in platelet aggregation
    • Clezardin P, Malaval L, Morel MC, Guichard J, Lecompte T, et al. (1991) Osteonectin is an alpha-granule component involved with thrombospondin in platelet aggregation. J Bone Miner Res 6: 1059-1070.
    • (1991) J Bone Miner Res , vol.6 , pp. 1059-1070
    • Clezardin, P.1    Malaval, L.2    Morel, M.C.3    Guichard, J.4    Lecompte, T.5
  • 11
    • 0032491588 scopus 로고    scopus 로고
    • SPARC (BM-40, osteonectin) inhibits the mitogenic effect of vascular endothelial growth factor on microvascular endothelial cells
    • Kupprion C, Motamed K, Sage EH, (1998) SPARC (BM-40, osteonectin) inhibits the mitogenic effect of vascular endothelial growth factor on microvascular endothelial cells. J Biol Chem 273: 29635-29640.
    • (1998) J Biol Chem , vol.273 , pp. 29635-29640
    • Kupprion, C.1    Motamed, K.2    Sage, E.H.3
  • 12
    • 0026500981 scopus 로고
    • The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors
    • Raines EW, Lane TF, Iruela-Arispe ML, Ross R, Sage EH, (1992) The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and-BB and inhibits the binding of PDGF to its receptors. Proc Natl Acad Sci U S A 89: 1281-1285.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1281-1285
    • Raines, E.W.1    Lane, T.F.2    Iruela-Arispe, M.L.3    Ross, R.4    Sage, E.H.5
  • 13
    • 34247276194 scopus 로고    scopus 로고
    • Is SPARC an evolutionarily conserved collagen chaperone?
    • Martinek N, Shahab J, Sodek J, Ringuette M, (2007) Is SPARC an evolutionarily conserved collagen chaperone? J Dent Res 86: 296-305.
    • (2007) J Dent Res , vol.86 , pp. 296-305
    • Martinek, N.1    Shahab, J.2    Sodek, J.3    Ringuette, M.4
  • 14
    • 0026547680 scopus 로고
    • Heat-shock response in cultured chick embryo chondrocytes. Osteonectin is a secreted heat-shock protein
    • Neri M, Scalzi-Cancedda F, Cancedda R, (1992) Heat-shock response in cultured chick embryo chondrocytes. Osteonectin is a secreted heat-shock protein. Eur J Biochem 205: 569-574.
    • (1992) Eur J Biochem , vol.205 , pp. 569-574
    • Neri, M.1    Scalzi-Cancedda, F.2    Cancedda, R.3
  • 15
    • 0028306966 scopus 로고
    • Two collagen-binding proteins, osteonectin and HSP47, are coordinately induced in transformed keratinocytes by heat and other stresses
    • Kudo H, Hirayoshi K, Kitagawa Y, Imamura S, Nagata K, (1994) Two collagen-binding proteins, osteonectin and HSP47, are coordinately induced in transformed keratinocytes by heat and other stresses. Exp Cell Res 212: 219-224.
    • (1994) Exp Cell Res , vol.212 , pp. 219-224
    • Kudo, H.1    Hirayoshi, K.2    Kitagawa, Y.3    Imamura, S.4    Nagata, K.5
  • 16
    • 33745634645 scopus 로고    scopus 로고
    • Chaperone-like activity revealed in the matricellular protein SPARC
    • Emerson RO, Sage EH, Ghosh JG, Clark JI, (2006) Chaperone-like activity revealed in the matricellular protein SPARC. J Cell Biochem 98: 701-705.
    • (2006) J Cell Biochem , vol.98 , pp. 701-705
    • Emerson, R.O.1    Sage, E.H.2    Ghosh, J.G.3    Clark, J.I.4
  • 17
    • 50349096759 scopus 로고    scopus 로고
    • Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens
    • Giudici C, Raynal N, Wiedemann H, Cabral WA, Marini JC, et al. (2008) Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens. J Biol Chem 283: 19551-19560.
    • (2008) J Biol Chem , vol.283 , pp. 19551-19560
    • Giudici, C.1    Raynal, N.2    Wiedemann, H.3    Cabral, W.A.4    Marini, J.C.5
  • 18
    • 53849137994 scopus 로고    scopus 로고
    • Vesicular trafficking in osteoclasts
    • Coxon FP, Taylor A, (2008) Vesicular trafficking in osteoclasts. Semin Cell Dev Biol 19: 424-433.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 424-433
    • Coxon, F.P.1    Taylor, A.2
  • 20
    • 33646484782 scopus 로고    scopus 로고
    • Novel function of alternatively activated macrophages: stabilin-1-mediated clearance of SPARC
    • Kzhyshkowska J, Workman G, Cardo-Vila M, Arap W, Pasqualini R, et al. (2006) Novel function of alternatively activated macrophages: stabilin-1-mediated clearance of SPARC. J Immunol 176: 5825-5832.
    • (2006) J Immunol , vol.176 , pp. 5825-5832
    • Kzhyshkowska, J.1    Workman, G.2    Cardo-Vila, M.3    Arap, W.4    Pasqualini, R.5
  • 21
    • 0032984442 scopus 로고    scopus 로고
    • Cell cycle-dependent nuclear location of the matricellular protein SPARC: association with the nuclear matrix
    • Gooden MD, Vernon RB, Bassuk JA, Sage EH, (1999) Cell cycle-dependent nuclear location of the matricellular protein SPARC: association with the nuclear matrix. J Cell Biochem 74: 152-167.
    • (1999) J Cell Biochem , vol.74 , pp. 152-167
    • Gooden, M.D.1    Vernon, R.B.2    Bassuk, J.A.3    Sage, E.H.4
  • 22
    • 55049112979 scopus 로고    scopus 로고
    • IFATS collection: combinatorial peptides identify alpha5beta1 integrin as a receptor for the matricellular protein SPARC on adipose stromal cells
    • Nie J, Chang B, Traktuev DO, Sun J, March K, et al. (2008) IFATS collection: combinatorial peptides identify alpha5beta1 integrin as a receptor for the matricellular protein SPARC on adipose stromal cells. Stem Cells 26: 2735-2745.
    • (2008) Stem Cells , vol.26 , pp. 2735-2745
    • Nie, J.1    Chang, B.2    Traktuev, D.O.3    Sun, J.4    March, K.5
  • 23
    • 34447129655 scopus 로고    scopus 로고
    • SPARC enhances tumor stroma formation and prevents fibroblast activation
    • Chlenski A, Guerrero LJ, Yang Q, Tian Y, Peddinti R, et al. (2007) SPARC enhances tumor stroma formation and prevents fibroblast activation. Oncogene 26: 4513-4522.
    • (2007) Oncogene , vol.26 , pp. 4513-4522
    • Chlenski, A.1    Guerrero, L.J.2    Yang, Q.3    Tian, Y.4    Peddinti, R.5
  • 24
    • 28844466823 scopus 로고    scopus 로고
    • SPARC expression is associated with impaired tumor growth, inhibited angiogenesis and changes in the extracellular matrix
    • Chlenski A, Liu S, Guerrero LJ, Yang Q, Tian Y, et al. (2006) SPARC expression is associated with impaired tumor growth, inhibited angiogenesis and changes in the extracellular matrix. Int J Cancer 118: 310-316.
    • (2006) Int J Cancer , vol.118 , pp. 310-316
    • Chlenski, A.1    Liu, S.2    Guerrero, L.J.3    Yang, Q.4    Tian, Y.5
  • 25
    • 0001472055 scopus 로고
    • The heat precipitation of collagen from neutral salt solutions: some rate-regulating factors
    • Gross J, Kirk D, (1958) The heat precipitation of collagen from neutral salt solutions: some rate-regulating factors. J Biol Chem 233: 355-360.
    • (1958) J Biol Chem , vol.233 , pp. 355-360
    • Gross, J.1    Kirk, D.2
  • 26
    • 33744990640 scopus 로고    scopus 로고
    • A three-dimensional model to study the epigenetic effects induced by the microenvironment of human embryonic stem cells
    • Postovit LM, Seftor EA, Seftor RE, Hendrix MJ, (2006) A three-dimensional model to study the epigenetic effects induced by the microenvironment of human embryonic stem cells. Stem Cells 24: 501-505.
    • (2006) Stem Cells , vol.24 , pp. 501-505
    • Postovit, L.M.1    Seftor, E.A.2    Seftor, R.E.3    Hendrix, M.J.4
  • 27
    • 0037115291 scopus 로고    scopus 로고
    • SPARC is a key Schwannian-derived inhibitor controlling neuroblastoma tumor angiogenesis
    • Chlenski A, Liu S, Crawford SE, Volpert OV, DeVries GH, et al. (2002) SPARC is a key Schwannian-derived inhibitor controlling neuroblastoma tumor angiogenesis. Cancer Res 62: 7357-7363.
    • (2002) Cancer Res , vol.62 , pp. 7357-7363
    • Chlenski, A.1    Liu, S.2    Crawford, S.E.3    Volpert, O.V.4    DeVries, G.H.5
  • 28
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J, Mogk A, Bukau B, (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11: 777-788.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 29
    • 0034682782 scopus 로고    scopus 로고
    • Calcium affinity, cooperativity, and domain interactions of extracellular EF-hands present in BM-40
    • Busch E, Hohenester E, Timpl R, Paulsson M, Maurer P, (2000) Calcium affinity, cooperativity, and domain interactions of extracellular EF-hands present in BM-40. J Biol Chem 275: 25508-25515.
    • (2000) J Biol Chem , vol.275 , pp. 25508-25515
    • Busch, E.1    Hohenester, E.2    Timpl, R.3    Paulsson, M.4    Maurer, P.5
  • 30
    • 0029347102 scopus 로고
    • Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1
    • Bornstein P, (1995) Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1. J Cell Biol 130: 503-506.
    • (1995) J Cell Biol , vol.130 , pp. 503-506
    • Bornstein, P.1
  • 31
    • 72449210973 scopus 로고    scopus 로고
    • The developmental roles of the extracellular matrix: beyond structure to regulation
    • Tsang KY, Cheung MC, Chan D, Cheah KS, (2010) The developmental roles of the extracellular matrix: beyond structure to regulation. Cell Tissue Res 339: 93-110.
    • (2010) Cell Tissue Res , vol.339 , pp. 93-110
    • Tsang, K.Y.1    Cheung, M.C.2    Chan, D.3    Cheah, K.S.4
  • 32
    • 77951234989 scopus 로고    scopus 로고
    • The extracellular matrix in development and morphogenesis: a dynamic view
    • Rozario T, DeSimone DW, (2010) The extracellular matrix in development and morphogenesis: a dynamic view. Dev Biol 341: 126-140.
    • (2010) Dev Biol , vol.341 , pp. 126-140
    • Rozario, T.1    DeSimone, D.W.2
  • 34
    • 77955928161 scopus 로고    scopus 로고
    • Tumors as organs: complex tissues that interface with the entire organism
    • Egeblad M, Nakasone ES, Werb Z, (2010) Tumors as organs: complex tissues that interface with the entire organism. Dev Cell 18: 884-901.
    • (2010) Dev Cell , vol.18 , pp. 884-901
    • Egeblad, M.1    Nakasone, E.S.2    Werb, Z.3
  • 35
    • 0028839859 scopus 로고
    • The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV
    • Maurer P, Hohenadl C, Hohenester E, Gohring W, Timpl R, et al. (1995) The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV. J Mol Biol 253: 347-357.
    • (1995) J Mol Biol , vol.253 , pp. 347-357
    • Maurer, P.1    Hohenadl, C.2    Hohenester, E.3    Gohring, W.4    Timpl, R.5
  • 36
    • 33745617174 scopus 로고    scopus 로고
    • Evolutionary genetics of vertebrate tissue mineralization: the origin and evolution of the secretory calcium-binding phosphoprotein family
    • Kawasaki K, Weiss KM, (2006) Evolutionary genetics of vertebrate tissue mineralization: the origin and evolution of the secretory calcium-binding phosphoprotein family. J Exp Zool B Mol Dev Evol 306: 295-316.
    • (2006) J Exp Zool B Mol Dev Evol , vol.306 , pp. 295-316
    • Kawasaki, K.1    Weiss, K.M.2
  • 37
    • 0032712968 scopus 로고    scopus 로고
    • SPARC, a matricellular glycoprotein with important biological functions
    • Yan Q, Sage EH, (1999) SPARC, a matricellular glycoprotein with important biological functions. J Histochem Cytochem 47: 1495-1506.
    • (1999) J Histochem Cytochem , vol.47 , pp. 1495-1506
    • Yan, Q.1    Sage, E.H.2
  • 39
    • 0028816321 scopus 로고
    • Increased expression of osteonectin and osteopontin, two bone matrix proteins, in human breast cancer
    • Bellahcene A, Castronovo V, (1995) Increased expression of osteonectin and osteopontin, two bone matrix proteins, in human breast cancer. Am J Pathol 146: 95-100.
    • (1995) Am J Pathol , vol.146 , pp. 95-100
    • Bellahcene, A.1    Castronovo, V.2
  • 41
    • 0036472494 scopus 로고    scopus 로고
    • pH-dependent regulation of lysosomal calcium in macrophages
    • Christensen KA, Myers JT, Swanson JA, (2002) pH-dependent regulation of lysosomal calcium in macrophages. J Cell Sci 115: 599-607.
    • (2002) J Cell Sci , vol.115 , pp. 599-607
    • Christensen, K.A.1    Myers, J.T.2    Swanson, J.A.3
  • 42
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • Gerasimenko JV, Tepikin AV, Petersen OH, Gerasimenko OV, (1998) Calcium uptake via endocytosis with rapid release from acidifying endosomes. Curr Biol 8: 1335-1338.
    • (1998) Curr Biol , vol.8 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 43
    • 0023643437 scopus 로고
    • Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues
    • Engel J, Taylor W, Paulsson M, Sage H, Hogan B, (1987) Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues. Biochemistry 26: 6958-6965.
    • (1987) Biochemistry , vol.26 , pp. 6958-6965
    • Engel, J.1    Taylor, W.2    Paulsson, M.3    Sage, H.4    Hogan, B.5
  • 44
    • 0032704239 scopus 로고    scopus 로고
    • Immunochemical and tissue analysis of protease generated neoepitopes of BM-40 (osteonectin, SPARC) which are correlated to a higher affinity binding to collagens
    • Sasaki T, Miosge N, Timpl R, (1999) Immunochemical and tissue analysis of protease generated neoepitopes of BM-40 (osteonectin, SPARC) which are correlated to a higher affinity binding to collagens. Matrix Biol 18: 499-508.
    • (1999) Matrix Biol , vol.18 , pp. 499-508
    • Sasaki, T.1    Miosge, N.2    Timpl, R.3
  • 45
    • 0021323613 scopus 로고
    • Characterization of a novel serum albumin-binding glycoprotein secreted by endothelial cells in culture
    • Sage H, Johnson C, Bornstein P, (1984) Characterization of a novel serum albumin-binding glycoprotein secreted by endothelial cells in culture. J Biol Chem 259: 3993-4007.
    • (1984) J Biol Chem , vol.259 , pp. 3993-4007
    • Sage, H.1    Johnson, C.2    Bornstein, P.3
  • 46
    • 52649119391 scopus 로고    scopus 로고
    • Improved effectiveness of nanoparticle albumin-bound (nab) paclitaxel versus polysorbate-based docetaxel in multiple xenografts as a function of HER2 and SPARC status
    • Desai NP, Trieu V, Hwang LY, Wu R, Soon-Shiong P, et al. (2008) Improved effectiveness of nanoparticle albumin-bound (nab) paclitaxel versus polysorbate-based docetaxel in multiple xenografts as a function of HER2 and SPARC status. Anticancer Drugs 19: 899-909.
    • (2008) Anticancer Drugs , vol.19 , pp. 899-909
    • Desai, N.P.1    Trieu, V.2    Hwang, L.Y.3    Wu, R.4    Soon-Shiong, P.5
  • 47
    • 0027931859 scopus 로고
    • Albondin-mediated capillary permeability to albumin. Differential role of receptors in endothelial transcytosis and endocytosis of native and modified albumins
    • Schnitzer JE, Oh P, (1994) Albondin-mediated capillary permeability to albumin. Differential role of receptors in endothelial transcytosis and endocytosis of native and modified albumins. J Biol Chem 269: 6072-6082.
    • (1994) J Biol Chem , vol.269 , pp. 6072-6082
    • Schnitzer, J.E.1    Oh, P.2
  • 48
    • 0030798998 scopus 로고    scopus 로고
    • Gp60 activation mediates albumin transcytosis in endothelial cells by tyrosine kinase-dependent pathway
    • Tiruppathi C, Song W, Bergenfeldt M, Sass P, Malik AB, (1997) Gp60 activation mediates albumin transcytosis in endothelial cells by tyrosine kinase-dependent pathway. J Biol Chem 272: 25968-25975.
    • (1997) J Biol Chem , vol.272 , pp. 25968-25975
    • Tiruppathi, C.1    Song, W.2    Bergenfeldt, M.3    Sass, P.4    Malik, A.B.5
  • 49
    • 0028203274 scopus 로고
    • SPARC (secreted protein acidic and rich in cysteine) regulates endothelial cell shape and barrier function
    • Goldblum SE, Ding X, Funk SE, Sage EH, (1994) SPARC (secreted protein acidic and rich in cysteine) regulates endothelial cell shape and barrier function. Proc Natl Acad Sci U S A 91: 3448-3452.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3448-3452
    • Goldblum, S.E.1    Ding, X.2    Funk, S.E.3    Sage, E.H.4
  • 50
    • 0032055746 scopus 로고    scopus 로고
    • Mice deficient for the secreted glycoprotein SPARC/osteonectin/BM40 develop normally but show severe age-onset cataract formation and disruption of the lens
    • Gilmour DT, Lyon GJ, Carlton MB, Sanes JR, Cunningham JM, et al. (1998) Mice deficient for the secreted glycoprotein SPARC/osteonectin/BM40 develop normally but show severe age-onset cataract formation and disruption of the lens. EMBO J 17: 1860-1870.
    • (1998) EMBO J , vol.17 , pp. 1860-1870
    • Gilmour, D.T.1    Lyon, G.J.2    Carlton, M.B.3    Sanes, J.R.4    Cunningham, J.M.5
  • 52
    • 0034129090 scopus 로고    scopus 로고
    • Osteopenia and decreased bone formation in osteonectin-deficient mice
    • Delany AM, Amling M, Priemel M, Howe C, Baron R, et al. (2000) Osteopenia and decreased bone formation in osteonectin-deficient mice. J Clin Invest 105: 915-923.
    • (2000) J Clin Invest , vol.105 , pp. 915-923
    • Delany, A.M.1    Amling, M.2    Priemel, M.3    Howe, C.4    Baron, R.5
  • 53
    • 0037791886 scopus 로고    scopus 로고
    • SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength
    • Bradshaw AD, Puolakkainen P, Dasgupta J, Davidson JM, Wight TN, et al. (2003) SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J Invest Dermatol 120: 949-955.
    • (2003) J Invest Dermatol , vol.120 , pp. 949-955
    • Bradshaw, A.D.1    Puolakkainen, P.2    Dasgupta, J.3    Davidson, J.M.4    Wight, T.N.5
  • 54
    • 0038284890 scopus 로고    scopus 로고
    • SPARC-null mice exhibit increased adiposity without significant differences in overall body weight
    • Bradshaw AD, Graves DC, Motamed K, Sage EH, (2003) SPARC-null mice exhibit increased adiposity without significant differences in overall body weight. Proc Natl Acad Sci U S A 100: 6045-6050.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6045-6050
    • Bradshaw, A.D.1    Graves, D.C.2    Motamed, K.3    Sage, E.H.4
  • 55
    • 0036144741 scopus 로고    scopus 로고
    • SPARC-null mice exhibit accelerated cutaneous wound closure
    • Bradshaw AD, Reed MJ, Sage EH, (2002) SPARC-null mice exhibit accelerated cutaneous wound closure. J Histochem Cytochem 50: 1-10.
    • (2002) J Histochem Cytochem , vol.50 , pp. 1-10
    • Bradshaw, A.D.1    Reed, M.J.2    Sage, E.H.3
  • 56
    • 60549088560 scopus 로고    scopus 로고
    • Absence of SPARC results in increased cardiac rupture and dysfunction after acute myocardial infarction
    • Schellings MW, Vanhoutte D, Swinnen M, Cleutjens JP, Debets J, et al. (2009) Absence of SPARC results in increased cardiac rupture and dysfunction after acute myocardial infarction. J Exp Med 206: 113-123.
    • (2009) J Exp Med , vol.206 , pp. 113-123
    • Schellings, M.W.1    Vanhoutte, D.2    Swinnen, M.3    Cleutjens, J.P.4    Debets, J.5
  • 57
    • 0025822677 scopus 로고
    • Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production
    • Mays PK, McAnulty RJ, Campa JS, Laurent GJ, (1991) Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production. Biochem J 276: 307-313.
    • (1991) Biochem J , vol.276 , pp. 307-313
    • Mays, P.K.1    McAnulty, R.J.2    Campa, J.S.3    Laurent, G.J.4
  • 58
    • 77957299067 scopus 로고    scopus 로고
    • SPARC/osteonectin functions to maintain homeostasis of the collagenous extracellular matrix in the periodontal ligament
    • Trombetta JM, Bradshaw AD, (2010) SPARC/osteonectin functions to maintain homeostasis of the collagenous extracellular matrix in the periodontal ligament. J Histochem Cytochem 58: 871-879.
    • (2010) J Histochem Cytochem , vol.58 , pp. 871-879
    • Trombetta, J.M.1    Bradshaw, A.D.2
  • 59
    • 74949090210 scopus 로고    scopus 로고
    • Age-dependent alterations in fibrillar collagen content and myocardial diastolic function: role of SPARC in post-synthetic procollagen processing
    • Bradshaw AD, Baicu CF, Rentz TJ, Van Laer AO, Bonnema DD, et al. (2010) Age-dependent alterations in fibrillar collagen content and myocardial diastolic function: role of SPARC in post-synthetic procollagen processing. Am J Physiol Heart Circ Physiol 298: H614-622.
    • (2010) Am J Physiol Heart Circ Physiol , vol.298 , pp. 614-622
    • Bradshaw, A.D.1    Baicu, C.F.2    Rentz, T.J.3    van Laer, A.O.4    Bonnema, D.D.5
  • 60
    • 84977285683 scopus 로고
    • Current views of collagen degradation. Progress towards understanding the resorption of connective tissues
    • Murphy G, Reynolds JJ, (1985) Current views of collagen degradation. Progress towards understanding the resorption of connective tissues. Bioessays 2: 55-60.
    • (1985) Bioessays , vol.2 , pp. 55-60
    • Murphy, G.1    Reynolds, J.J.2
  • 61
    • 0037417411 scopus 로고    scopus 로고
    • uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion
    • Engelholm LH, List K, Netzel-Arnett S, Cukierman E, Mitola DJ, et al. (2003) uPARAP/Endo180 is essential for cellular uptake of collagen and promotes fibroblast collagen adhesion. J Cell Biol 160: 1009-1015.
    • (2003) J Cell Biol , vol.160 , pp. 1009-1015
    • Engelholm, L.H.1    List, K.2    Netzel-Arnett, S.3    Cukierman, E.4    Mitola, D.J.5
  • 62
    • 0034634627 scopus 로고    scopus 로고
    • A novel model system for characterization of phagosomal maturation, acidification, and intracellular collagen degradation in fibroblasts
    • Arora PD, Manolson MF, Downey GP, Sodek J, McCulloch CA, (2000) A novel model system for characterization of phagosomal maturation, acidification, and intracellular collagen degradation in fibroblasts. J Biol Chem 275: 35432-35441.
    • (2000) J Biol Chem , vol.275 , pp. 35432-35441
    • Arora, P.D.1    Manolson, M.F.2    Downey, G.P.3    Sodek, J.4    McCulloch, C.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.