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Volumn 86, Issue 4, 2007, Pages 296-305

Is SPARC an evolutionarity conserved collagen chaperone?

Author keywords

Collagen; Fibrillogenesis; HSP47; Molecular chaperone; SPARC

Indexed keywords

CHAPERONE; FIBRILLAR COLLAGEN; HEAT SHOCK PROTEIN 47; OSTEONECTIN; PROCOLLAGEN;

EID: 34247276194     PISSN: 00220345     EISSN: None     Source Type: Journal    
DOI: 10.1177/154405910708600402     Document Type: Review
Times cited : (114)

References (83)
  • 1
    • 27744606970 scopus 로고    scopus 로고
    • SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity
    • Barker TH, Baneyx G, Cardo-Vila M, Workman GA, Weaver M, Menon PM, et al. (2005a). SPARC regulates extracellular matrix organization through its modulation of integrin-linked kinase activity. J Biol Chem 280:36483-36493.
    • (2005) J Biol Chem , vol.280 , pp. 36483-36493
    • Barker, T.H.1    Baneyx, G.2    Cardo-Vila, M.3    Workman, G.A.4    Weaver, M.5    Menon, P.M.6
  • 2
    • 14644440585 scopus 로고    scopus 로고
    • Matricellular homologs in the foreign body response: Hevin suppresses inflammation, but hevin and SPARC together diminish angiogenesis
    • Barker TH, Framson P, Puolakkainen PA, Reed M, Funk SE, Sage EH (2005b). Matricellular homologs in the foreign body response: hevin suppresses inflammation, but hevin and SPARC together diminish angiogenesis. Am J Pathol 166:923-933.
    • (2005) Am J Pathol , vol.166 , pp. 923-933
    • Barker, T.H.1    Framson, P.2    Puolakkainen, P.A.3    Reed, M.4    Funk, S.E.5    Sage, E.H.6
  • 3
    • 0036775425 scopus 로고    scopus 로고
    • Matricellular proteins: Extracellular modulators of cell function
    • Bornstein P, Sage EH (2002). Matricellular proteins: extracellular modulators of cell function. Curr Opin Cell Biol 14:608-616.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 608-616
    • Bornstein, P.1    Sage, E.H.2
  • 4
    • 0035022957 scopus 로고    scopus 로고
    • SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury
    • Bradshaw AD, Sage EH (2001). SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury. J Clin Invest 107:1049-1054.
    • (2001) J Clin Invest , vol.107 , pp. 1049-1054
    • Bradshaw, A.D.1    Sage, E.H.2
  • 5
    • 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, Helene Sage E (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    Helene Sage, E.6
  • 6
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: At the crossroads of cell-matrix communication
    • Brekken RA, Sage EH (2001). SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol 19:816-827.
    • (2001) Matrix Biol , vol.19 , pp. 816-827
    • Brekken, R.A.1    Sage, E.H.2
  • 7
    • 0032880280 scopus 로고    scopus 로고
    • Activation of SPARC expression in reactive stroma associated with human epithelial ovarian cancer
    • Brown TJ, Shaw PA, Karp X, Huynh MH, Begley H, Ringuette MJ (1999). Activation of SPARC expression in reactive stroma associated with human epithelial ovarian cancer. Gynecol Oncol 75:25-33.
    • (1999) Gynecol Oncol , vol.75 , pp. 25-33
    • Brown, T.J.1    Shaw, P.A.2    Karp, X.3    Huynh, M.H.4    Begley, H.5    Ringuette, M.J.6
  • 8
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A (2006). Molecular chaperones and protein quality control. Cell 125:443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 9
    • 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
  • 10
    • 0028132222 scopus 로고
    • Transient expression of SPARC in the dorsal axis of early Xenopus embryos: Correlation with calcium-dependent adhesion and electrical coupling
    • Damjanovski S, Malaval L, Ringuette MJ (1994). Transient expression of SPARC in the dorsal axis of early Xenopus embryos: correlation with calcium-dependent adhesion and electrical coupling. Int J Dev Biol 38:439-446.
    • (1994) Int J Dev Biol , vol.38 , pp. 439-446
    • Damjanovski, S.1    Malaval, L.2    Ringuette, M.J.3
  • 11
    • 0031907362 scopus 로고    scopus 로고
    • Regulation of SPARC expression during early Xenopus development: Evolutionary divergence and conservation of DNA regulatory elements between amphibians and mammals
    • Damjanovski S, Huynh MH, Motamed K, Sage EH, Ringuette M (1998). Regulation of SPARC expression during early Xenopus development: evolutionary divergence and conservation of DNA regulatory elements between amphibians and mammals. Dev Genes Evol 207:453-461.
    • (1998) Dev Genes Evol , vol.207 , pp. 453-461
    • Damjanovski, S.1    Huynh, M.H.2    Motamed, K.3    Sage, E.H.4    Ringuette, M.5
  • 12
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • Ellis RJ, Minton AP (2006). Protein aggregation in crowded environments. Biol Chem 387:485-497.
    • (2006) Biol Chem , vol.387 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 13
    • 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
  • 14
    • 0023176745 scopus 로고
    • Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone
    • Fisher LW, Hawkins GR, Tuross N, Termine JD (1987). Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone. J Biol Chem 262:9702-9708.
    • (1987) J Biol Chem , vol.262 , pp. 9702-9708
    • Fisher, L.W.1    Hawkins, G.R.2    Tuross, N.3    Termine, J.D.4
  • 16
    • 0032547991 scopus 로고    scopus 로고
    • Importance of the basement membrane protein SPARC for viability and fertility in Caenorhabditis elegans
    • Fitzgerald MC, Schwarzbauer JE (1998). Importance of the basement membrane protein SPARC for viability and fertility in Caenorhabditis elegans. Curr Biol 8:1285-1288.
    • (1998) Curr Biol , vol.8 , pp. 1285-1288
    • Fitzgerald, M.C.1    Schwarzbauer, J.E.2
  • 17
    • 0025921473 scopus 로고
    • The Ca2(+)-binding glycoprotein SPARC modulates cell cycle progression in bovine aortic endothelial cells
    • Funk SE, Sage EH (1991). The Ca2(+)-binding glycoprotein SPARC modulates cell cycle progression in bovine aortic endothelial cells. Proc Natl Acad Sci USA 88:2648-2652.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2648-2652
    • Funk, S.E.1    Sage, E.H.2
  • 18
    • 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, Anderson JR, 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    Anderson, J.R.6
  • 20
    • 31344465486 scopus 로고    scopus 로고
    • Hamilton AM, Heikkila JJ (2006). Examination of the stress-induced expression of the collagen binding heat shock protein, hsp47, in Xenopus laevis cultured cells and embryos. Comp Biochem Physiol A Mol Integr Physiol 143:133-141.
    • Hamilton AM, Heikkila JJ (2006). Examination of the stress-induced expression of the collagen binding heat shock protein, hsp47, in Xenopus laevis cultured cells and embryos. Comp Biochem Physiol A Mol Integr Physiol 143:133-141.
  • 21
    • 0033135750 scopus 로고    scopus 로고
    • Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines
    • Hebert C, Norris K, Della Coletta R, Reynolds M, Ordóñez J, Sauk JJ (1999). Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines. J Cell Biochem 73:248-258.
    • (1999) J Cell Biochem , vol.73 , pp. 248-258
    • Hebert, C.1    Norris, K.2    Della Coletta, R.3    Reynolds, M.4    Ordóñez, J.5    Sauk, J.J.6
  • 22
    • 0033927046 scopus 로고    scopus 로고
    • Decreased elastin deposition and high proliferation of fibroblasts from Costello syndrome are related to functional deficiency in the 67-kD elastin-binding protein
    • Hinek A, Smith AC, Cutiongco EM, Callahan JW, Gripp KW, Weksberg R (2000). Decreased elastin deposition and high proliferation of fibroblasts from Costello syndrome are related to functional deficiency in the 67-kD elastin-binding protein. Am J Hum Genet 66:859-872.
    • (2000) Am J Hum Genet , vol.66 , pp. 859-872
    • Hinek, A.1    Smith, A.C.2    Cutiongco, E.M.3    Callahan, J.W.4    Gripp, K.W.5    Weksberg, R.6
  • 24
    • 0030995856 scopus 로고    scopus 로고
    • Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40
    • Hohenester E, Maurer P, Timpl R (1997). Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J 16:3778-3786.
    • (1997) EMBO J , vol.16 , pp. 3778-3786
    • Hohenester, E.1    Maurer, P.2    Timpl, R.3
  • 25
    • 0023374396 scopus 로고
    • In vivo expression of mRNA for the Ca++-binding protein SPARC (osteonectin) revealed by in situ hybridization
    • Holland PW, Harper SJ, McVey JH, Hogan BL (1987). In vivo expression of mRNA for the Ca++-binding protein SPARC (osteonectin) revealed by in situ hybridization. J Cell Biol 105:473-482.
    • (1987) J Cell Biol , vol.105 , pp. 473-482
    • Holland, P.W.1    Harper, S.J.2    McVey, J.H.3    Hogan, B.L.4
  • 26
    • 0027494603 scopus 로고
    • Type IV collagen: Structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis
    • Hudson BG, Reeders ST, Tryggvason K (1993). Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis. J Biol Chem 268:26033-26036.
    • (1993) J Biol Chem , vol.268 , pp. 26033-26036
    • Hudson, B.G.1    Reeders, S.T.2    Tryggvason, K.3
  • 27
    • 0033814869 scopus 로고    scopus 로고
    • Association of SPARC (osteonectin, BM-40) with extracellular and intracellular components of the ciliated surface ectoderm of Xenopus embryos
    • Huynh MH, Hong H, Delovitch S, Desser S, Ringuette M (2000). Association of SPARC (osteonectin, BM-40) with extracellular and intracellular components of the ciliated surface ectoderm of Xenopus embryos. Cell Motil Cytoskeleton 47:154-162.
    • (2000) Cell Motil Cytoskeleton , vol.47 , pp. 154-162
    • Huynh, M.H.1    Hong, H.2    Delovitch, S.3    Desser, S.4    Ringuette, M.5
  • 28
  • 29
    • 0036431513 scopus 로고    scopus 로고
    • Type I collagen contains at least 14 cryptic fibronectin binding sites of similar affinity
    • Ingham KC, Brew SA, Migliorini M (2002). Type I collagen contains at least 14 cryptic fibronectin binding sites of similar affinity. Arch Biochem Biophys 407:217-221.
    • (2002) Arch Biochem Biophys , vol.407 , pp. 217-221
    • Ingham, K.C.1    Brew, S.A.2    Migliorini, M.3
  • 30
    • 0029808530 scopus 로고    scopus 로고
    • Type I collagen-deficient Mov-13 mice do not retain SPARC in the extracellular matrix: Implications for fibroblast function
    • Iruela-Arispe ML, Vernon RB, Wu H, Jaenisch R, Sage EH (1996). Type I collagen-deficient Mov-13 mice do not retain SPARC in the extracellular matrix: implications for fibroblast function. Dev Dyn 207:171-183.
    • (1996) Dev Dyn , vol.207 , pp. 171-183
    • Iruela-Arispe, M.L.1    Vernon, R.B.2    Wu, H.3    Jaenisch, R.4    Sage, E.H.5
  • 31
    • 0025271330 scopus 로고
    • Molecular cloning of SCI: A putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM40/SPARC
    • Johnston IG, Paladino T, Gurd JW, Brown IR (1990). Molecular cloning of SCI: a putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM40/SPARC. Neuron 4:165-176.
    • (1990) Neuron , vol.4 , pp. 165-176
    • Johnston, I.G.1    Paladino, T.2    Gurd, J.W.3    Brown, I.R.4
  • 32
    • 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, Maurer P, 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    Maurer, P.6
  • 33
    • 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
  • 34
    • 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
  • 35
    • 23444459571 scopus 로고    scopus 로고
    • Lane TF, Sage EH (1994). The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB.78:163-173.
    • Lane TF, Sage EH (1994). The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB.78:163-173.
  • 36
    • 0026742984 scopus 로고
    • Regulation of gene expression by SPARC during angiogenesis in vitro. Changes in fibronectin, thrombospondin-1, and plasminogen activator inhibitor-1
    • Lane TF, Iruela-Arispe ML, Sage EH (1992). Regulation of gene expression by SPARC during angiogenesis in vitro. Changes in fibronectin, thrombospondin-1, and plasminogen activator inhibitor-1. J Biol Chem 267:16736-16745.
    • (1992) J Biol Chem , vol.267 , pp. 16736-16745
    • Lane, T.F.1    Iruela-Arispe, M.L.2    Sage, E.H.3
  • 37
    • 0037166935 scopus 로고    scopus 로고
    • Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation
    • Li S, Harrison D, Carbonetto S, Fassler R, Smyth N, Edgar D, et al. (2002). Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J Cell Biol 157:1279-1290.
    • (2002) J Cell Biol , vol.157 , pp. 1279-1290
    • Li, S.1    Harrison, D.2    Carbonetto, S.3    Fassler, R.4    Smyth, N.5    Edgar, D.6
  • 38
    • 0036938372 scopus 로고    scopus 로고
    • Evolutionary conservation and association of SPARC with the basal lamina in Drosophila
    • Martinek N, Zou R, Berg M, Sodek J, Ringuette M (2002). Evolutionary conservation and association of SPARC with the basal lamina in Drosophila. Dev Genes Evol 212:124-133.
    • (2002) Dev Genes Evol , vol.212 , pp. 124-133
    • Martinek, N.1    Zou, R.2    Berg, M.3    Sodek, J.4    Ringuette, M.5
  • 40
    • 12344322951 scopus 로고    scopus 로고
    • Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP
    • Marutani T, Yamamoto A, Nagai N, Kubota H, Nagata K (2004). Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP. J Cell Sci 117:5913-5922.
    • (2004) J Cell Sci , vol.117 , pp. 5913-5922
    • Marutani, T.1    Yamamoto, A.2    Nagai, N.3    Kubota, H.4    Nagata, K.5
  • 41
    • 0022758820 scopus 로고
    • Developmental and transformation-sensitive expression of the Sparc gene on mouse chromosome 11
    • Mason IJ, Murphy D, Munke M, Francke U, Elliott RW, Hogan BL (1986). Developmental and transformation-sensitive expression of the Sparc gene on mouse chromosome 11. EMBO J 5:1831-1837.
    • (1986) EMBO J , vol.5 , pp. 1831-1837
    • Mason, I.J.1    Murphy, D.2    Munke, M.3    Francke, U.4    Elliott, R.W.5    Hogan, B.L.6
  • 42
    • 4644234938 scopus 로고    scopus 로고
    • Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells
    • Matsuoka Y, Kubota H, Adachi E, Nagai N, Marutani T, Hosokawa N, et al. (2004). Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells. Mol Biol Cell 15:4467-4475.
    • (2004) Mol Biol Cell , vol.15 , pp. 4467-4475
    • Matsuoka, Y.1    Kubota, H.2    Adachi, E.3    Nagai, N.4    Marutani, T.5    Hosokawa, N.6
  • 43
    • 0030888219 scopus 로고    scopus 로고
    • Structural and functional aspects of calcium binding in extracellular matrix proteins
    • Maurer P, Hohenester E (1997). Structural and functional aspects of calcium binding in extracellular matrix proteins. Matrix Biol 15:569-580.
    • (1997) Matrix Biol , vol.15 , pp. 569-580
    • Maurer, P.1    Hohenester, E.2
  • 44
    • 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, Engel J (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    Engel, J.6
  • 45
    • 0030738396 scopus 로고    scopus 로고
    • Structural and functional characterization of the extracellular calcium-binding protein BM-40/secreted protein, acidic, rich in cysteine/osteonectin from the nematode Caenorhabditis elegans
    • Maurer P, Sasaki T, Mann K, Gohring W, Schwarzbauer JE, Timpl R (1997). Structural and functional characterization of the extracellular calcium-binding protein BM-40/secreted protein, acidic, rich in cysteine/osteonectin from the nematode Caenorhabditis elegans. Eur J Biochem 248:209-216.
    • (1997) Eur J Biochem , vol.248 , pp. 209-216
    • Maurer, P.1    Sasaki, T.2    Mann, K.3    Gohring, W.4    Schwarzbauer, J.E.5    Timpl, R.6
  • 46
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • Nagata K (1996). Hsp47: a collagen-specific molecular chaperone. Trends Biochem Sci 21 :22-26.
    • (1996) Trends Biochem Sci , vol.21 , pp. 22-26
    • Nagata, K.1
  • 47
    • 0742304951 scopus 로고    scopus 로고
    • HSP47 as a collagen-specific molecular chaperone: Function and expression in normal mouse development
    • Nagata K (2003). HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development. Semin Cell Dev Biol 14:275-282.
    • (2003) Semin Cell Dev Biol , vol.14 , pp. 275-282
    • Nagata, K.1
  • 48
    • 8744264023 scopus 로고    scopus 로고
    • The functional consequences of cross-talk between the vitamin D receptor and ERK signaling pathways are cell-specific
    • Narayanan R, Sepulveda VAT, Falzon M, Weigel NL (2004). The functional consequences of cross-talk between the vitamin D receptor and ERK signaling pathways are cell-specific. J Biol Chem 279:47298-47310.
    • (2004) J Biol Chem , vol.279 , pp. 47298-47310
    • Narayanan, R.1    Sepulveda, V.A.T.2    Falzon, M.3    Weigel, N.L.4
  • 50
    • 0033807857 scopus 로고    scopus 로고
    • Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface
    • Norose K, Lo WK, Clark JI, Sage EH, Howe CC (2000). Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface. Exp Eye Res 71:295-307.
    • (2000) Exp Eye Res , vol.71 , pp. 295-307
    • Norose, K.1    Lo, W.K.2    Clark, J.I.3    Sage, E.H.4    Howe, C.C.5
  • 51
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • Poschl E, Schlotzer-Schrehardt U, Brachvogel B, Saito K, Ninomiya Y, Mayer U (2004). Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 131:1619-1628.
    • (2004) Development , vol.131 , pp. 1619-1628
    • Poschl, E.1    Schlotzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 52
    • 0028286760 scopus 로고
    • Changes in calcium and collagen IV binding caused by mutations in the EF hand and other domains of extracellular matrix protein BM-40 (SPARC, osteonectin)
    • Pottgiesser J, Maurer P, Mayer U, Nischt R, Mann K, Timpl R, et al. (1994). Changes in calcium and collagen IV binding caused by mutations in the EF hand and other domains of extracellular matrix protein BM-40 (SPARC, osteonectin). J Mol Biol 238:563-574.
    • (1994) J Mol Biol , vol.238 , pp. 563-574
    • Pottgiesser, J.1    Maurer, P.2    Mayer, U.3    Nischt, R.4    Mann, K.5    Timpl, R.6
  • 53
    • 0027216767 scopus 로고
    • Differential expression of SPARC and thrombospondin 1 in wound repair: Immunolocalization and in situ hybridization
    • Reed MJ, Puolakkainen P, Lane TF, Dickerson D, Bornstein P, Sage EH (1993). Differential expression of SPARC and thrombospondin 1 in wound repair: immunolocalization and in situ hybridization. J Histochem Cytochem 41:1467-1477.
    • (1993) J Histochem Cytochem , vol.41 , pp. 1467-1477
    • Reed, M.J.1    Puolakkainen, P.2    Lane, T.F.3    Dickerson, D.4    Bornstein, P.5    Sage, E.H.6
  • 54
    • 0019138166 scopus 로고
    • 7-S collagen: Characterization of an unusual basement membrane structure
    • Risteli J, Bachinger HP, Engel J, Furthmayr H, Timpl R (1980). 7-S collagen: characterization of an unusual basement membrane structure. Eur J Biochem 108:239-250.
    • (1980) Eur J Biochem , vol.108 , pp. 239-250
    • Risteli, J.1    Bachinger, H.P.2    Engel, J.3    Furthmayr, H.4    Timpl, R.5
  • 55
    • 1542373992 scopus 로고    scopus 로고
    • Fibronectin matrix assembly regulates alpha5betal-mediated cell cohesion
    • Robinson EE, Foty RA, Corbett SA (2004). Fibronectin matrix assembly regulates alpha5betal-mediated cell cohesion. Mol Biol Cell 15:973-981.
    • (2004) Mol Biol Cell , vol.15 , pp. 973-981
    • Robinson, E.E.1    Foty, R.A.2    Corbett, S.A.3
  • 56
    • 16944363757 scopus 로고    scopus 로고
    • Terms of attachment: SPARC and tumorigenesis
    • Sage EH (1997). Terms of attachment: SPARC and tumorigenesis. Nat Med 3:144-146.
    • (1997) Nat Med , vol.3 , pp. 144-146
    • Sage, E.H.1
  • 57
    • 0025032857 scopus 로고
    • Immunohistochemical localization of SPARC (osteonectin) and denatured collagen and their relationship to remodelling in rat dental tissues
    • Salonen J, Domenicucci C, Goldberg HA, Sodek J (1990). Immunohistochemical localization of SPARC (osteonectin) and denatured collagen and their relationship to remodelling in rat dental tissues. Arch Oral Biol 35:337-346.
    • (1990) Arch Oral Biol , vol.35 , pp. 337-346
    • Salonen, J.1    Domenicucci, C.2    Goldberg, H.A.3    Sodek, J.4
  • 58
    • 0345016887 scopus 로고    scopus 로고
    • Leukocyte, rather than tumor-produced SPARC, determines stroma and collagen type IV deposition in mammary carcinoma
    • Sangaletti S, Stoppacciaro A, Guiducci C, Torrisi MR, Colombo MP (2003). Leukocyte, rather than tumor-produced SPARC, determines stroma and collagen type IV deposition in mammary carcinoma. J Exp Med 198:1475-1485.
    • (2003) J Exp Med , vol.198 , pp. 1475-1485
    • Sangaletti, S.1    Stoppacciaro, A.2    Guiducci, C.3    Torrisi, M.R.4    Colombo, M.P.5
  • 59
    • 0032536897 scopus 로고    scopus 로고
    • Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin
    • Sasaki T, Hohenester E, Gohring W, Timpl R (1998). Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin. EMBOJ 17:1625-1634.
    • (1998) EMBOJ , vol.17 , pp. 1625-1634
    • Sasaki, T.1    Hohenester, E.2    Gohring, W.3    Timpl, R.4
  • 60
    • 0026333424 scopus 로고
    • Diverse forms of stress result in changes in cellular levels of osteonectin/SPARC without altering mRNA levels in osteoligament cells
    • Sauk JJ, Noms K, Kerr JM, Somerman MJ, Young MF (1991). Diverse forms of stress result in changes in cellular levels of osteonectin/SPARC without altering mRNA levels in osteoligament cells. Calcif Tissue Int 49:58-62.
    • (1991) Calcif Tissue Int , vol.49 , pp. 58-62
    • Sauk, J.J.1    Noms, K.2    Kerr, J.M.3    Somerman, M.J.4    Young, M.F.5
  • 61
    • 0027431095 scopus 로고
    • Cloning from a mouse osteoblastic cell line of a set of transforming-growth-factor-beta 1-regulated genes, one of which seems to encode a follistatin-related polypeptide
    • Shibanuma M, Mashimo J, Mita A, Kuroki T, Nose K (1993). Cloning from a mouse osteoblastic cell line of a set of transforming-growth-factor-beta 1-regulated genes, one of which seems to encode a follistatin-related polypeptide. Eur J Biochem 217:13-19.
    • (1993) Eur J Biochem , vol.217 , pp. 13-19
    • Shibanuma, M.1    Mashimo, J.2    Mita, A.3    Kuroki, T.4    Nose, K.5
  • 62
    • 33646501394 scopus 로고    scopus 로고
    • The amelogenin story: Origin and evolution
    • Sire JY, Delgado S, Girondot M (2006). The amelogenin story: origin and evolution. Eur J Oral Sci 114(Suppl 1):64-77.
    • (2006) Eur J Oral Sci , vol.114 , Issue.SUPPL. 1 , pp. 64-77
    • Sire, J.Y.1    Delgado, S.2    Girondot, M.3
  • 64
    • 0035996510 scopus 로고    scopus 로고
    • Novel functions of the matricellular proteins osteopontin and osteonectin/SPARC
    • Sodek J, Zhu B, Huynh MH, Brown TJ, Ringuette M (2002). Novel functions of the matricellular proteins osteopontin and osteonectin/SPARC. Connect Tissue Res 43:308-319.
    • (2002) Connect Tissue Res , vol.43 , pp. 308-319
    • Sodek, J.1    Zhu, B.2    Huynh, M.H.3    Brown, T.J.4    Ringuette, M.5
  • 65
    • 0035992868 scopus 로고    scopus 로고
    • Colocalization of intracellular osteopontin with CD44 is associated with migration, cell fusion, and resorption in osteoclasts
    • Suzuki K, Zhu B, Rittling SR, Denhardt DT, Goldberg HA, McCulloch CA, et al. (2002). Colocalization of intracellular osteopontin with CD44 is associated with migration, cell fusion, and resorption in osteoclasts. J Bone Miner Res 17:1486-1497.
    • (2002) J Bone Miner Res , vol.17 , pp. 1486-1497
    • Suzuki, K.1    Zhu, B.2    Rittling, S.R.3    Denhardt, D.T.4    Goldberg, H.A.5    McCulloch, C.A.6
  • 66
    • 0034657132 scopus 로고    scopus 로고
    • Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen
    • Tasab M, Batten MR, Bulleid NJ (2000). Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen. EMBO J 19:2204-2211.
    • (2000) EMBO J , vol.19 , pp. 2204-2211
    • Tasab, M.1    Batten, M.R.2    Bulleid, N.J.3
  • 68
    • 0019781637 scopus 로고
    • A network model for the organization of type IV collagen molecules in basement membranes
    • Timpl R, Wiedemann H, van Delden V, Furthmayr H, Kuhn K (1981). A network model for the organization of type IV collagen molecules in basement membranes. Eur J Biochem 120:203-211.
    • (1981) Eur J Biochem , vol.120 , pp. 203-211
    • Timpl, R.1    Wiedemann, H.2    van Delden, V.3    Furthmayr, H.4    Kuhn, K.5
  • 69
    • 0027297962 scopus 로고
    • SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway
    • Tremble PM, Lane TF, Sage EH, Werb Z (1993). SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway. J Cell Biol 121:1433-1444.
    • (1993) J Cell Biol , vol.121 , pp. 1433-1444
    • Tremble, P.M.1    Lane, T.F.2    Sage, E.H.3    Werb, Z.4
  • 70
    • 0021876040 scopus 로고
    • Specific immunohistochemical localization of osteonectin and collagen types I and III in fetal and adult porcine dental tissues
    • Tung PS, Domenicucci C, Wasi S, Sodek J (1985). Specific immunohistochemical localization of osteonectin and collagen types I and III in fetal and adult porcine dental tissues. J Histochem Cytochem 33:531-540.
    • (1985) J Histochem Cytochem , vol.33 , pp. 531-540
    • Tung, P.S.1    Domenicucci, C.2    Wasi, S.3    Sodek, J.4
  • 71
    • 0037064131 scopus 로고    scopus 로고
    • Characterization of SMOC-1, a novel modular calcium-binding protein in basement membranes
    • Vannahme C, Smyth N, Miosge N, Gosling S, Frie C, Paulsson M, et al. (2002). Characterization of SMOC-1, a novel modular calcium-binding protein in basement membranes. J Biol Chem 277:37977-37986.
    • (2002) J Biol Chem , vol.277 , pp. 37977-37986
    • Vannahme, C.1    Smyth, N.2    Miosge, N.3    Gosling, S.4    Frie, C.5    Paulsson, M.6
  • 72
    • 0043069845 scopus 로고    scopus 로고
    • Characterization of SMOC-2, a modular extracellular calcium-binding protein
    • Vannahme C, Gosling S, Paulsson M, Maurer P, Hartmann U (2003). Characterization of SMOC-2, a modular extracellular calcium-binding protein. Biochem J 373:805-814.
    • (2003) Biochem J , vol.373 , pp. 805-814
    • Vannahme, C.1    Gosling, S.2    Paulsson, M.3    Maurer, P.4    Hartmann, U.5
  • 73
    • 0003005891 scopus 로고
    • Fundamentals of interstitial collagen self-assembly
    • Yurchenco PD, Birk DE, Mecham RP, editors. New York: Academic Press, pp
    • Veis A, George A (1994). Fundamentals of interstitial collagen self-assembly. In: Extracellular matrix assembly and structure. Yurchenco PD, Birk DE, Mecham RP, editors. New York: Academic Press, pp. 15-46.
    • (1994) Extracellular matrix assembly and structure , pp. 15-46
    • Veis, A.1    George, A.2
  • 74
    • 27544439448 scopus 로고    scopus 로고
    • Identifying the SPARC binding sites on collagen I and procollagen I by atomic force microscopy
    • Wang H, Fertala A, Ratner BD, Sage EH, Jiang S (2005). Identifying the SPARC binding sites on collagen I and procollagen I by atomic force microscopy. Anal Chem 77:6765-6771.
    • (2005) Anal Chem , vol.77 , pp. 6765-6771
    • Wang, H.1    Fertala, A.2    Ratner, B.D.3    Sage, E.H.4    Jiang, S.5
  • 75
    • 0023836639 scopus 로고
    • Differential effects of transforming growth factor-beta on the synthesis of extracellular matrix proteins by normal fetal rat calvarial bone cell populations
    • Wrana JL, Maeno M, Hawrylyshyn B, Yao KL, Domenicucci C, Sodek J (1988). Differential effects of transforming growth factor-beta on the synthesis of extracellular matrix proteins by normal fetal rat calvarial bone cell populations. J Cell Biol 106:915-924.
    • (1988) J Cell Biol , vol.106 , pp. 915-924
    • Wrana, J.L.1    Maeno, M.2    Hawrylyshyn, B.3    Yao, K.L.4    Domenicucci, C.5    Sodek, J.6
  • 76
    • 0034671734 scopus 로고    scopus 로고
    • Multiple binding sites in collagen type I for the integrins alpha 1beta1 and alpha2beta1
    • Xu Y, Gurusiddappa S, Rich RL, Owens RT, Keene DR, Mayne R, et al. (2000). Multiple binding sites in collagen type I for the integrins alpha 1beta1 and alpha2beta1. J Biol Chem 275:38981-38989.
    • (2000) J Biol Chem , vol.275 , pp. 38981-38989
    • Xu, Y.1    Gurusiddappa, S.2    Rich, R.L.3    Owens, R.T.4    Keene, D.R.5    Mayne, R.6
  • 77
    • 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
  • 78
    • 14744279741 scopus 로고    scopus 로고
    • Matricellular protein SPARC is translocated to the nuclei of immortalized murine lens epithelial cells
    • Yan Q, Weaver M, Perdue N, Sage EH (2005). Matricellular protein SPARC is translocated to the nuclei of immortalized murine lens epithelial cells. J Cell Physiol 203:286-294.
    • (2005) J Cell Physiol , vol.203 , pp. 286-294
    • Yan, Q.1    Weaver, M.2    Perdue, N.3    Sage, E.H.4
  • 79
    • 20044383563 scopus 로고    scopus 로고
    • Dmp1-deficient mice display severe defects in cartilage formation responsible for a chondrodysplasia-like phenotype
    • Ye L, Mishina Y, Chen D, Huang H, Dallas SL, Dallas MR, et al. (2005). Dmp1-deficient mice display severe defects in cartilage formation responsible for a chondrodysplasia-like phenotype. J Biol Chem 280:6197-6203.
    • (2005) J Biol Chem , vol.280 , pp. 6197-6203
    • Ye, L.1    Mishina, Y.2    Chen, D.3    Huang, H.4    Dallas, S.L.5    Dallas, M.R.6
  • 80
    • 0021342890 scopus 로고
    • Self-assembly of basement membrane collagen
    • Yurchenco PD, Furthmayr H (1984). Self-assembly of basement membrane collagen. Biochemistry 23:1839-1850.
    • (1984) Biochemistry , vol.23 , pp. 1839-1850
    • Yurchenco, P.D.1    Furthmayr, H.2
  • 81
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco PD, Amenta PS, Patton BL (2004). Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol 22:521-538.
    • (2004) Matrix Biol , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 82
    • 0034093124 scopus 로고    scopus 로고
    • Intracellular osteopontin is an integral component of the CD44-ERM complex involved in cell migration
    • Zohar R, Suzuki N, Suzuki K, Arora P, Glogauer M, McCulloch CAG, et al. (2000). Intracellular osteopontin is an integral component of the CD44-ERM complex involved in cell migration. J Cell Physiol 184:118-130.
    • (2000) J Cell Physiol , vol.184 , pp. 118-130
    • Zohar, R.1    Suzuki, N.2    Suzuki, K.3    Arora, P.4    Glogauer, M.5    McCulloch, C.A.G.6
  • 83
    • 0022460019 scopus 로고
    • Osteonectin is a minor component of mineralized connective tissues in rat
    • Zung P, Domenicucci C, Wasi S, Kuwata F, Sodek J (1986). Osteonectin is a minor component of mineralized connective tissues in rat. Biochem Cell Biol 64:356-362.
    • (1986) Biochem Cell Biol , vol.64 , pp. 356-362
    • Zung, P.1    Domenicucci, C.2    Wasi, S.3    Kuwata, F.4    Sodek, J.5


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