메뉴 건너뛰기




Volumn 126, Issue 6, 2006, Pages 705-712

Secreted modular calcium-binding protein-1 localization during mouse embryogenesis

Author keywords

Basement membrane; In situ hybridization; Light microscopic immunohistochemistry; Mouse embryogenesis; SMOC 1

Indexed keywords

CALCIUM BINDING PROTEIN; MESSENGER RNA; PROTEIN SMOC 1;

EID: 33845405551     PISSN: 09486143     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00418-006-0200-7     Document Type: Article
Times cited : (24)

References (40)
  • 1
    • 0027269935 scopus 로고
    • Testican, a multidomain testicular proteoglycan resembling modulators of cell social behaviour
    • Alliel PM, Perin JP, Jolles P, Bonnet FJ (1993) Testican, a multidomain testicular proteoglycan resembling modulators of cell social behaviour. Eur J Biochem 214:347-350
    • (1993) Eur J Biochem , vol.214 , pp. 347-350
    • Alliel, P.M.1    Perin, J.P.2    Jolles, P.3    Bonnet, F.J.4
  • 2
    • 2342530856 scopus 로고    scopus 로고
    • Impaired wound healing in mice deficient in a matricellular protein SPARC (osteonectin, BM-40)
    • Basu A, Kligman LH, Samulewicz SJ, Howe CC (2000) Impaired wound healing in mice deficient in a matricellular protein SPARC (osteonectin, BM-40). BMC Cell Biol 2:15
    • (2000) BMC Cell Biol , vol.2 , pp. 15
    • Basu, A.1    Kligman, L.H.2    Samulewicz, S.J.3    Howe, C.C.4
  • 3
    • 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
  • 4
    • 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
  • 5
    • 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
  • 6
    • 0036144741 scopus 로고    scopus 로고
    • SPARC-null mice exhibit accelerated cutaneous wound closure
    • Bradshaw AD, Reed MJ, Sage EH (2002a) 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
  • 7
    • 0035727654 scopus 로고    scopus 로고
    • SPARC-null mice display enhanced fibrovascular invasion of subcutaneous sponge implants
    • Bradshaw AD, Reed MJ, Sage EH (2002b) SPARC-null mice display enhanced fibrovascular invasion of subcutaneous sponge implants. Wound Repair Regen 9:522-530
    • (2002) Wound Repair Regen , vol.9 , pp. 522-530
    • Bradshaw, A.D.1    Reed, M.J.2    Sage, E.H.3
  • 8
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: At the crossroads of cell-matrix communication
    • Brekken RA, Sage EH (2000) SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol 19:816-827
    • (2000) Matrix Biol , vol.19 , pp. 816-827
    • Brekken, R.A.1    Sage, E.H.2
  • 13
    • 0022881604 scopus 로고
    • Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor
    • Dziadek M, Paulsson M, Aumailley M, Timpl R (1986) Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor. Eur J Biochem 161:455-464
    • (1986) Eur J Biochem , vol.161 , pp. 455-464
    • Dziadek, M.1    Paulsson, M.2    Aumailley, M.3    Timpl, R.4
  • 14
    • 20444493196 scopus 로고    scopus 로고
    • Laminin γ3 chain binds to nidogen and is located in murine basement membranes
    • Gersdorff N, Kohfeldt E, Sasaki T, Timpl R, Miosge N (2005) Laminin γ3 chain binds to nidogen and is located in murine basement membranes. J Biol Chem 280:22146-22153
    • (2005) J Biol Chem , vol.280 , pp. 22146-22153
    • Gersdorff, N.1    Kohfeldt, E.2    Sasaki, T.3    Timpl, R.4    Miosge, N.5
  • 15
    • 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 MBL, Sanes JR, Cunningham JM, Anderson JR, Hogan BLM, Evans MJ, Colledge WH (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.L.3    Sanes, J.R.4    Cunningham, J.M.5    Anderson, J.R.6    Hogan, B.L.M.7    Evans, M.J.8    Colledge, W.H.9
  • 16
    • 0029864198 scopus 로고    scopus 로고
    • Modulation of endothelial cell adhesion by hevin, an acidic protein associated with high endothelial venules
    • Girard JP, Springer TA (1996) Modulation of endothelial cell adhesion by hevin, an acidic protein associated with high endothelial venules. J Biol Chem 271:4511-4517
    • (1996) J Biol Chem , vol.271 , pp. 4511-4517
    • Girard, J.P.1    Springer, T.A.2
  • 18
    • 0035127422 scopus 로고    scopus 로고
    • Proteoglycans in the nervous system - The quest for functional roles in vivo
    • Hartmann U, Maurer P (2001) Proteoglycans in the nervous system - the quest for functional roles in vivo. Matrix Biol 20:23-35
    • (2001) Matrix Biol , vol.20 , pp. 23-35
    • Hartmann, U.1    Maurer, P.2
  • 20
    • 0025271330 scopus 로고
    • Molecular cloning of SC1: A putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM-40/SPARC
    • Johnston IG, Paladino T, Gurd JW, Brown IR (1990) Molecular cloning of SC1: a putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM-40/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
  • 21
    • 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
  • 22
    • 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
  • 23
    • 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
  • 25
    • 0028839859 scopus 로고
    • The c-terminal portion of BM-40 (SPARC/Osteonectin) is autonomously folding and crystallisable domain that binds calcium and collagen IV
    • Maurer P, Hohenadl C, Hohenester E, Göhring W, Timpl R, Engel J (1995) The c-terminal portion of BM-40 (SPARC/Osteonectin) is 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    Göhring, W.4    Timpl, R.5    Engel, J.6
  • 26
    • 0028227591 scopus 로고
    • Expression of the gene encoding the extracellular matrix glycoprotein SPARC in the developing and adult mouse brain
    • Mendis DB, Brown IR (1994) Expression of the gene encoding the extracellular matrix glycoprotein SPARC in the developing and adult mouse brain. Brain Res Mol Brain Res 24:11-19
    • (1994) Brain Res Mol Brain Res , vol.24 , pp. 11-19
    • Mendis, D.B.1    Brown, I.R.2
  • 28
    • 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
  • 29
    • 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 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, M.L.3    Ross, R.4    Sage, E.H.5
  • 30
    • 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, Göhring 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. EMBO J 17:1625-1634
    • (1998) EMBO J , vol.17 , pp. 1625-1634
    • Sasaki, T.1    Hohenester, E.2    Göhring, W.3    Timpl, R.4
  • 33
    • 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
  • 34
    • 0032887716 scopus 로고    scopus 로고
    • Collagen accumulation is decreased in SPARC-null mice with bleomycin-induced pulmonary fibrosis
    • Strandjord TP, Madtes DK, Weiss DJ, Sage EH (1999) Collagen accumulation is decreased in SPARC-null mice with bleomycin-induced pulmonary fibrosis. Am J Physiol 277:628-635
    • (1999) Am J Physiol , vol.277 , pp. 628-635
    • Strandjord, T.P.1    Madtes, D.K.2    Weiss, D.J.3    Sage, E.H.4
  • 36
    • 7744227850 scopus 로고    scopus 로고
    • Perlecan in late stages of osteoarthritis of the human knee joint
    • Tesche F, Miosge N (2004) Perlecan in late stages of osteoarthritis of the human knee joint. Osteoarthritis Cartil 12:852-862
    • (2004) Osteoarthritis Cartil , vol.12 , pp. 852-862
    • Tesche, F.1    Miosge, N.2
  • 40
    • 0043069845 scopus 로고    scopus 로고
    • Characterization of SMOC-2, a modular extracellular calcium-binding protein
    • Vanna hme C, Gösling 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    Gösling, S.2    Paulsson, M.3    Maurer, P.4    Hartmann, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.