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Volumn 74, Issue 2, 1999, Pages 152-167

Cell cycle-dependent nuclear location of the matricellular protein SPARC: Association with the nuclear matrix

Author keywords

BM 40; Mitotic cycle; Nuclear matrix components; Nuclear translocation; Nucleus; Osteonectin

Indexed keywords

OSTEONECTIN;

EID: 0032984442     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19990801)74:2<152::AID-JCB2>3.0.CO;2-4     Document Type: Article
Times cited : (75)

References (65)
  • 1
    • 0024374856 scopus 로고
    • Protein disulphide isomerase, a multifunctional endoplasmic reticulum protein
    • Bassuk JA, Berg RA. 1989. Protein disulphide isomerase, a multifunctional endoplasmic reticulum protein. Matrix 9:244-258.
    • (1989) Matrix , vol.9 , pp. 244-258
    • Bassuk, J.A.1    Berg, R.A.2
  • 5
    • 0016861690 scopus 로고
    • Nuclear protein matrix: Association with newly synthesized DNA
    • Berezney R, Coffey DS. 1975. Nuclear protein matrix: association with newly synthesized DNA. Science 189:291-293.
    • (1975) Science , vol.189 , pp. 291-293
    • Berezney, R.1    Coffey, D.S.2
  • 7
    • 0030027917 scopus 로고    scopus 로고
    • Nuclear import of protein kinases and cyclins
    • Boulikas T. 1996. Nuclear import of protein kinases and cyclins. J Biol Chem 60:61-82.
    • (1996) J Biol Chem , vol.60 , pp. 61-82
    • Boulikas, T.1
  • 11
    • 0021046130 scopus 로고
    • Actively transcribed genes are associated with the nuclear matrix
    • Ciejek EM, Tsai MJ, O'Malley BW. 1983. Actively transcribed genes are associated with the nuclear matrix. Nature 306:607.
    • (1983) Nature , vol.306 , pp. 607
    • Ciejek, E.M.1    Tsai, M.J.2    O'Malley, B.W.3
  • 12
  • 13
    • 0025372116 scopus 로고
    • Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation
    • Dworetzky SI, Fey EG, Penman S, Lian JB, Stein JL, Stein GS. 1990. Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation. Proc Natl Acad Sci USA 87:4605-4609.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4605-4609
    • Dworetzky, S.I.1    Fey, E.G.2    Penman, S.3    Lian, J.B.4    Stein, J.L.5    Stein, G.S.6
  • 14
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three-dimensional organization and protein composition
    • Fey EG, Wan KM, Penman S. 1984. Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: three-dimensional organization and protein composition. J Cell Biol 98:1973-1984.
    • (1984) J Cell Biol , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 15
    • 0025921473 scopus 로고
    • 2+-binding glycoprotein SPARC modulates cell cycle progression in bovine aortic endothelial cells
    • 2+-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
  • 16
    • 0027339116 scopus 로고
    • Differential effects of SPARC and cationic SPARC peptides on DNA synthesis by endothelial cells and fibroblasts
    • Funk SE, Sage EH. 1993. Differential effects of SPARC and cationic SPARC peptides on DNA synthesis by endothelial cells and fibroblasts. J Cell Physiol 154:53-63.
    • (1993) J Cell Physiol , vol.154 , pp. 53-63
    • Funk, S.E.1    Sage, E.H.2
  • 17
  • 18
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich D, Mattaj IW. 1996. Nucleocytoplasmic transport. Science 271:1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 19
    • 0025772967 scopus 로고
    • SPARC induces the expression of type I plasminogen activator inhibitor in cultured bovine aortic endothelial cells
    • Hasselaar P, Loskutoff DL, Sawdey M, Sage EH. 1991. SPARC induces the expression of type I plasminogen activator inhibitor in cultured bovine aortic endothelial cells. J Biol Chem 266:13178-13184.
    • (1991) J Biol Chem , vol.266 , pp. 13178-13184
    • Hasselaar, P.1    Loskutoff, D.L.2    Sawdey, M.3    Sage, E.H.4
  • 20
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He D, Nickerson A, Penman S. 1990. Core filaments of the nuclear matrix. J Cell Biol 110:569-580.
    • (1990) J Cell Biol , vol.110 , pp. 569-580
    • He, D.1    Nickerson, A.2    Penman, S.3
  • 21
    • 0030905728 scopus 로고    scopus 로고
    • Nuclear targeting of secretory proteins
    • Henderson JE. 1997. Nuclear targeting of secretory proteins. Mol Cell Endocrinol 129:1-5.
    • (1997) Mol Cell Endocrinol , vol.129 , pp. 1-5
    • Henderson, J.E.1
  • 23
    • 0028947280 scopus 로고
    • Expression of SPARC during development of the chicken chorioallantoic membrane: Evidence for regulated proteolysis in vivo
    • Iruela-Arispe ML, Lane TF, Redmond D, Reilly M, Bolender RP, Kavanagh TJ, Sage EH. 1995. Expression of SPARC during development of the chicken chorioallantoic membrane: evidence for regulated proteolysis in vivo. Mol Biol Cell 6:327-343.
    • (1995) Mol Biol Cell , vol.6 , pp. 327-343
    • Iruela-Arispe, M.L.1    Lane, T.F.2    Redmond, D.3    Reilly, M.4    Bolender, R.P.5    Kavanagh, T.J.6    Sage, E.H.7
  • 24
    • 0029808530 scopus 로고    scopus 로고
    • Type I collagen-deficient Mov-13 mice do not retain SPARC in the extracellular matrix: Implication 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: implication for fibroblast function. Dev Dynam 207:171-183.
    • (1996) Dev Dynam , vol.207 , pp. 171-183
    • Iruela-Arispe, M.L.1    Vernon, R.B.2    Wu, H.3    Jaenisch, R.4    Sage, E.H.5
  • 25
    • 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. 1999. SPARC (BM-40, osteonectin) inhibits the mitogenic effect of vascular endothelial growth factor on microvascular endothelial cells. J Biol Chem 273:29635-28640.
    • (1999) J Biol Chem , vol.273 , pp. 29635-128640
    • Kupprion, C.1    Motamed, K.2    Sage, E.H.3
  • 26
    • 23444459571 scopus 로고
    • The biology of SPARC, a protein that modulates cell-matrix interactions
    • Lane TF, Sage EH. 1994. The biology of SPARC, a protein that modulates cell-matrix interactions. FASEB J 8:163-173.
    • (1994) FASEB J , vol.8 , pp. 163-173
    • Lane, T.F.1    Sage, E.H.2
  • 27
    • 0026742984 scopus 로고
    • Regulation of gene expression by SPARC during angiogenesis in vitro
    • Lane TF, Iruela-Arispe ML, Sage EH. 1992. Regulation of gene expression by SPARC during angiogenesis in vitro. 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
  • 28
    • 0031577557 scopus 로고    scopus 로고
    • Nuclear translocation of human angiogenin in cultured human umbilical endothelial cell is microtubule and lysosome independent
    • Li R, Riodan JF, Hu G. 1997. Nuclear translocation of human angiogenin in cultured human umbilical endothelial cell is microtubule and lysosome independent. Biochem Biophys Res Commun 238:305-312.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 305-312
    • Li, R.1    Riodan, J.F.2    Hu, G.3
  • 30
    • 0027976913 scopus 로고
    • The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein
    • Mancini MA, Shan B, Nickerson JA, Penman S, Lee W. 1994. The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc Natl Acad Sci USA 91:418-422.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 418-422
    • Mancini, M.A.1    Shan, B.2    Nickerson, J.A.3    Penman, S.4    Lee, W.5
  • 32
    • 0029160382 scopus 로고
    • Modulation of ras transformation affecting chromatin supraorganization as assessed by image analysis
    • Mello ML, Contente S, Vidal BC, Planding W, Schenck U. 1995. Modulation of ras transformation affecting chromatin supraorganization as assessed by image analysis. Exp Cell Res 220:374-382.
    • (1995) Exp Cell Res , vol.220 , pp. 374-382
    • Mello, M.L.1    Contente, S.2    Vidal, B.C.3    Planding, W.4    Schenck, U.5
  • 33
    • 0028262977 scopus 로고
    • Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity
    • Moroianu J, Riordan JF. 1994. Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. Proc Natl Acad Sci USA 91:1677-1681.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1677-1681
    • Moroianu, J.1    Riordan, J.F.2
  • 34
    • 0026550137 scopus 로고
    • Distribution of osteonectin mRNA and protein during human embryonic and fetal development
    • Mundlos S, Schwahn B, Reichert T, Zabel B. 1992. Distribution of osteonectin mRNA and protein during human embryonic and fetal development. J Histochem Cytochem 40:283-291.
    • (1992) J Histochem Cytochem , vol.40 , pp. 283-291
    • Mundlos, S.1    Schwahn, B.2    Reichert, T.3    Zabel, B.4
  • 35
    • 0024415409 scopus 로고
    • Thrombospondin modulates focal adhesions in endothelial cells
    • Murphy-Ullrich JE, Höök M. 1989. Thrombospondin modulates focal adhesions in endothelial cells. J Cell Biol 109:1309-1319.
    • (1989) J Cell Biol , vol.109 , pp. 1309-1319
    • Murphy-Ullrich, J.E.1    Höök, M.2
  • 36
    • 0026321941 scopus 로고
    • Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin
    • Murphy-Ullrich JE, Lightner VA, Aukhil I, Yan YZ. 1991. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J Cell Biol 115:1127-1136.
    • (1991) J Cell Biol , vol.115 , pp. 1127-1136
    • Murphy-Ullrich, J.E.1    Lightner, V.A.2    Aukhil, I.3    Yan, Y.Z.4
  • 38
    • 0031860097 scopus 로고    scopus 로고
    • Nuclear dreams: The malignant alteration of nuclear architecture
    • Nickerson JA. 1998. Nuclear dreams: the malignant alteration of nuclear architecture. J Cell Biochem 70:172-180.
    • (1998) J Cell Biochem , vol.70 , pp. 172-180
    • Nickerson, J.A.1
  • 39
    • 0026786668 scopus 로고
    • Localization of nuclear matrix core filament proteins at interphase and mitosis
    • Nickerson JA, Penman S. 1992. Localization of nuclear matrix core filament proteins at interphase and mitosis. Cell Biol Int Rep 16:811-826.
    • (1992) Cell Biol Int Rep , vol.16 , pp. 811-826
    • Nickerson, J.A.1    Penman, S.2
  • 40
    • 0030956629 scopus 로고    scopus 로고
    • The nuclear matrix revealed by eluting chromatin from a cross-linked nucleus
    • Nickerson JA, Krockmalnic G, Wan KM, Penman S. 1997. The nuclear matrix revealed by eluting chromatin from a cross-linked nucleus. Proc Natl Acad Sci USA 94:4446-4450.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4446-4450
    • Nickerson, J.A.1    Krockmalnic, G.2    Wan, K.M.3    Penman, S.4
  • 42
    • 0025265544 scopus 로고
    • Prompt heat-shock and heat-shifted proteins associated with the nuclear matrix-intermediate filament scaffold in Drosophila melanogaster cells
    • Ornelles DA, Penman S. 1990. Prompt heat-shock and heat-shifted proteins associated with the nuclear matrix-intermediate filament scaffold in Drosophila melanogaster cells. J Cell Sci 95:393-404.
    • (1990) J Cell Sci , vol.95 , pp. 393-404
    • Ornelles, D.A.1    Penman, S.2
  • 43
    • 0029078045 scopus 로고
    • Rethinking cell structure
    • Penman S. 1995. Rethinking cell structure. Proc Natl Acad Sci USA 92:5251-5257.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5251-5257
    • Penman, S.1
  • 45
    • 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 LM, 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 USA 89:1281-1285.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1281-1285
    • Raines, E.W.1    Lane, T.F.2    Iruela-Arispe, L.M.3    Ross, R.4    Sage, E.H.5
  • 46
    • 0030004807 scopus 로고    scopus 로고
    • SPARC and the extracellular matrix: Implications for cancer and wound repair
    • Reed MJ, Sage EH. 1996. SPARC and the extracellular matrix: implications for cancer and wound repair. Curr Top Microbiol Immunol 213:81-94.
    • (1996) Curr Top Microbiol Immunol , vol.213 , pp. 81-94
    • Reed, M.J.1    Sage, E.H.2
  • 47
    • 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
  • 49
    • 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
    • Rosenblatt S, Bassuk JA, Alpers CE, Sage EH, Timpl R, Preissner KT. 1997. Differential modulation of cell adhesion by interaction between adhesive and counter-adhesive proteins: characterization of the binding of vitronectin to osteonectin. J Biochem 324:311-319.
    • (1997) J Biochem , vol.324 , pp. 311-319
    • Rosenblatt, S.1    Bassuk, J.A.2    Alpers, C.E.3    Sage, E.H.4    Timpl, R.5    Preissner, K.T.6
  • 50
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin
    • Sage EH, Bornstein P. 1991. Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin. J Biol Chem 266:14831-14834.
    • (1991) J Biol Chem , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 51
    • 0018578691 scopus 로고
    • Collagen synthesis by bovine aortic endothelial cells in culture
    • Sage H, Crouch E, Bornstein P. 1979. Collagen synthesis by bovine aortic endothelial cells in culture. Biochemistry 24:5433-5442.
    • (1979) Biochemistry , vol.24 , pp. 5433-5442
    • Sage, H.1    Crouch, E.2    Bornstein, P.3
  • 55
    • 0031586585 scopus 로고    scopus 로고
    • Nuclear association of cyclin D1 in human fibroblasts: Tight binding to nuclear structures and modulation by protein kinase inhibitors
    • Scovassi AI, Stivala LA, Rossi L, Bianchi L, Prosperi E. 1997. Nuclear association of cyclin D1 in human fibroblasts: tight binding to nuclear structures and modulation by protein kinase inhibitors. Exp Cell Res 237:127-134.
    • (1997) Exp Cell Res , vol.237 , pp. 127-134
    • Scovassi, A.I.1    Stivala, L.A.2    Rossi, L.3    Bianchi, L.4    Prosperi, E.5
  • 56
    • 0029043047 scopus 로고
    • Electron microscopic visualization of insulin translocation into the cytoplasm and nuclei of intact H35 hepatoma cells using covalently linked nanogold-insulin
    • Shah N, Zhang S, Harada S, Smith RM, Jarett L. 1995. Electron microscopic visualization of insulin translocation into the cytoplasm and nuclei of intact H35 hepatoma cells using covalently linked Nanogold-insulin. Endocrinology 136:2825-2835.
    • (1995) Endocrinology , vol.136 , pp. 2825-2835
    • Shah, N.1    Zhang, S.2    Harada, S.3    Smith, R.M.4    Jarett, L.5
  • 57
    • 0031832031 scopus 로고    scopus 로고
    • Interrelationships of nuclear architecture with gene expression: Functional encounters on a long and winding road
    • Stein GS. 1998. Interrelationships of nuclear architecture with gene expression: functional encounters on a long and winding road. J Cell Biochem 70:157-158.
    • (1998) J Cell Biochem , vol.70 , pp. 157-158
    • Stein, G.S.1
  • 58
    • 0029799798 scopus 로고    scopus 로고
    • Functional interrelationships between nuclear structure and transcriptional control: Contributions to regulation of cell cycle-and tissue-specific gene expression
    • Stein GS, Stein JL, Lian JB, van Wijnen AJ, Montecino M. 1996. Functional interrelationships between nuclear structure and transcriptional control: contributions to regulation of cell cycle-and tissue-specific gene expression. J Cell Biochem 62:198-209.
    • (1996) J Cell Biochem , vol.62 , pp. 198-209
    • Stein, G.S.1    Stein, J.L.2    Lian, J.B.3    Van Wijnen, A.J.4    Montecino, M.5
  • 59
    • 0031830805 scopus 로고    scopus 로고
    • Interrelationships of nuclear structure and transcription control: Functional consequences of being in the right place at the right time
    • Stein GS, van Wijnen JA, Stein JL, Lian JB, Pockwinse S, McNeil S. 1998. Interrelationships of nuclear structure and transcription control: functional consequences of being in the right place at the right time. J Cell Biochem 70:200-212.
    • (1998) J Cell Biochem , vol.70 , pp. 200-212
    • Stein, G.S.1    Van Wijnen, J.A.2    Stein, J.L.3    Lian, J.B.4    Pockwinse, S.5    McNeil, S.6
  • 60
    • 0019785123 scopus 로고
    • Osteonectin, a bone-specific protein linking mineral to collagen
    • Termine JD, Kleinman HK, Whitson SW, Conn KM. 1981. Osteonectin, a bone-specific protein linking mineral to collagen. Cell 26:99-105.
    • (1981) Cell , vol.26 , pp. 99-105
    • Termine, J.D.1    Kleinman, H.K.2    Whitson, S.W.3    Conn, K.M.4
  • 61
    • 0027297962 scopus 로고
    • SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloprotein ases 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 metalloprotein ases 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
  • 62
    • 0024433444 scopus 로고
    • The calcium-binding protein SPARC is secreted by leydig and sertoli cells of the adult mouse testis
    • Vernon RB, Sage EH. 1989. The calcium-binding protein SPARC is secreted by Leydig and Sertoli cells of the adult mouse testis. Biol Reprod 40:1329-1340.
    • (1989) Biol Reprod , vol.40 , pp. 1329-1340
    • Vernon, R.B.1    Sage, E.H.2
  • 63
    • 9544239348 scopus 로고    scopus 로고
    • Immunolocalization of osteonectin in avian tibial dyschondroplastic cartilage
    • Wu J, Pines M, Gay CV, Hurwitz S, Leach RM. 1996. Immunolocalization of osteonectin in avian tibial dyschondroplastic cartilage. Dev Dynam 207:69-74.
    • (1996) Dev Dynam , vol.207 , pp. 69-74
    • Wu, J.1    Pines, M.2    Gay, C.V.3    Hurwitz, S.4    Leach, R.M.5
  • 64
    • 0031965271 scopus 로고    scopus 로고
    • SPARC is expressed by ganglion cells and astrocytes in bovine retina
    • Yan Q, Sage EH, Hendrickson AE. 1998. SPARC is expressed by ganglion cells and astrocytes in bovine retina. J Histochem Cytochem 46:3-10.
    • (1998) J Histochem Cytochem , vol.46 , pp. 3-10
    • Yan, Q.1    Sage, E.H.2    Hendrickson, A.E.3
  • 65
    • 0027491595 scopus 로고
    • Specific interaction of SPARC with endothelial cells is mediated through a carboxyl-terminal sequence containing a calcium-binding EF hand
    • Yost JC, Sage EH. 1993. Specific interaction of SPARC with endothelial cells is mediated through a carboxyl-terminal sequence containing a calcium-binding EF hand. J Biol Chem 268:25790-25796.
    • (1993) J Biol Chem , vol.268 , pp. 25790-25796
    • Yost, J.C.1    Sage, E.H.2


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