메뉴 건너뛰기




Volumn 89, Issue 3, 2009, Pages 416-425

Absence of SPARC leads to impaired lens circulation

Author keywords

capsule; cataract; circulation; electrophysiology; lens; matrix; microarray; SPARC

Indexed keywords

CADHERIN; FIBROMODULIN; GLIAL FIBRILLARY ACIDIC PROTEIN; GLUTAMATE DECARBOXYLASE; GLUTAMATE RECEPTOR; GLYCINE RECEPTOR; ION CHANNEL; KERATIN; KININOGEN; NEUREXIN; NEUROFILAMENT PROTEIN; OSTEONECTIN; PROTEIN S; THROMBOSPONDIN 2;

EID: 67651232580     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2009.04.008     Document Type: Article
Times cited : (13)

References (52)
  • 1
    • 0038519687 scopus 로고    scopus 로고
    • Morphology and organization of posterior fiber ends during migration
    • Al-Ghoul K.J., Kuszak J.R., Lu J.Y., and Owens M.J. Morphology and organization of posterior fiber ends during migration. Mol. Vis. 9 (2003) 119-128
    • (2003) Mol. Vis. , vol.9 , pp. 119-128
    • Al-Ghoul, K.J.1    Kuszak, J.R.2    Lu, J.Y.3    Owens, M.J.4
  • 2
    • 0036073033 scopus 로고    scopus 로고
    • Effect of basal lamina of ovarian follicle on T- and L-type Ca(2+) currents in differentiated granulosa cells
    • Asem E.K., Qin W., and Rane S.G. Effect of basal lamina of ovarian follicle on T- and L-type Ca(2+) currents in differentiated granulosa cells. Am. J. Physiol. Endocrinol. Metab. 282 (2002) E184-E196
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.282
    • Asem, E.K.1    Qin, W.2    Rane, S.G.3
  • 3
    • 0026768033 scopus 로고
    • Spatial variations in membrane properties in the intact rat lens
    • Baldo G.J., and Mathias R.T. Spatial variations in membrane properties in the intact rat lens. Biophys. J. 63 (1992) 518-529
    • (1992) Biophys. J. , vol.63 , pp. 518-529
    • Baldo, G.J.1    Mathias, R.T.2
  • 6
    • 0036775425 scopus 로고    scopus 로고
    • Matricellular proteins: extracellular modulators of cell function
    • Bornstein P., and Sage E.H. Matricellular proteins: extracellular modulators of cell function. Curr. Opin. Cell Biol. 14 (2002) 608-616
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 608-616
    • Bornstein, P.1    Sage, E.H.2
  • 7
    • 33644952358 scopus 로고    scopus 로고
    • Integrin-linked kinase and its partners: a modular platform regulating cell-matrix adhesion dynamics and cytoskeletal organization
    • Boulter E., and Van Obberghen-Schilling E. Integrin-linked kinase and its partners: a modular platform regulating cell-matrix adhesion dynamics and cytoskeletal organization. Eur. J. Cell Biol. 85 (2006) 255-263
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 255-263
    • Boulter, E.1    Van Obberghen-Schilling, E.2
  • 8
    • 0037791886 scopus 로고    scopus 로고
    • SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength
    • Bradshaw A.D., Puolakkainen P., Dasgupta J., Davidson J.M., Wight T.N., and Helene Sage E. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J. Invest. Dermatol. 120 (2003) 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
  • 9
    • 0035022957 scopus 로고    scopus 로고
    • SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury
    • Bradshaw A.D., and Sage E.H. SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury. J. Clin. Invest. 107 (2001) 1049-1054
    • (2001) J. Clin. Invest. , vol.107 , pp. 1049-1054
    • Bradshaw, A.D.1    Sage, E.H.2
  • 11
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: at the crossroads of cell-matrix communication
    • Brekken R.A., and Sage E.H. SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol. 19 (2001) 816-827
    • (2001) Matrix Biol. , vol.19 , pp. 816-827
    • Brekken, R.A.1    Sage, E.H.2
  • 13
    • 0037736569 scopus 로고    scopus 로고
    • Osteonectin-null mutation compromises osteoblast formation, maturation, and survival
    • Delany A.M., Kalajzic I., Bradshaw A.D., Sage E.H., and Canalis E. Osteonectin-null mutation compromises osteoblast formation, maturation, and survival. Endocrinology 144 (2003) 2588-2596
    • (2003) Endocrinology , vol.144 , pp. 2588-2596
    • Delany, A.M.1    Kalajzic, I.2    Bradshaw, A.D.3    Sage, E.H.4    Canalis, E.5
  • 14
    • 0035354578 scopus 로고    scopus 로고
    • Molecular solutions to mammalian lens transparency
    • Donaldson P., Kistler J., and Mathias R.T. Molecular solutions to mammalian lens transparency. News Physiol. Sci. 16 (2001) 118-123
    • (2001) News Physiol. Sci. , vol.16 , pp. 118-123
    • Donaldson, P.1    Kistler, J.2    Mathias, R.T.3
  • 15
    • 67651245828 scopus 로고    scopus 로고
    • Draghici S. (Ed), Chapman & Hall/CRC, Boca Raton, FL
    • In: Draghici S. (Ed). Data Analysis Tools for DNA Microarrays (2003), Chapman & Hall/CRC, Boca Raton, FL 345-349
    • (2003) Data Analysis Tools for DNA Microarrays , pp. 345-349
  • 16
    • 0036032864 scopus 로고    scopus 로고
    • Calcium signalling in ocular tissues: functional activity of G-protein and tyrosine-kinase coupled receptors
    • Duncan G., and Collison D.J. Calcium signalling in ocular tissues: functional activity of G-protein and tyrosine-kinase coupled receptors. Exp. Eye Res. 75 (2002) 377-389
    • (2002) Exp. Eye Res. , vol.75 , pp. 377-389
    • Duncan, G.1    Collison, D.J.2
  • 18
    • 0021731563 scopus 로고
    • Calcium and the physiology of cataract
    • Duncan G., and Jacob T.J. Calcium and the physiology of cataract. Ciba Found. Symp. 106 (1984) 132-152
    • (1984) Ciba Found. Symp. , vol.106 , pp. 132-152
    • Duncan, G.1    Jacob, T.J.2
  • 19
    • 0032803953 scopus 로고    scopus 로고
    • Calcium cell signalling and cataract: role of the endoplasmic reticulum
    • Duncan G., and Wormstone I.M. Calcium cell signalling and cataract: role of the endoplasmic reticulum. Eye 13 Pt 3b (1999) 480-483
    • (1999) Eye , vol.13 , Issue.PART 3b , pp. 480-483
    • Duncan, G.1    Wormstone, I.M.2
  • 20
    • 0036081355 scopus 로고    scopus 로고
    • Gene Expression Omnibus: NCBI gene expression and hybridization array data repository
    • Edgar R., Domrachev M., and Lash A.E. Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res. 30 (2002) 207-210
    • (2002) Nucleic Acids Res. , vol.30 , pp. 207-210
    • Edgar, R.1    Domrachev, M.2    Lash, A.E.3
  • 21
    • 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 D.T., Lyon G.J., Carlton M.B., Sanes J.R., Cunningham J.M., Anderson J.R., Hogan B.L., Evans M.J., and Colledge W.H. 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 (1998) 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    Hogan, B.L.7    Evans, M.J.8    Colledge, W.H.9
  • 23
    • 35748979134 scopus 로고    scopus 로고
    • An in vitro model of posterior capsular opacity: sPARC and TGF-beta2 minimize epithelial-to-mesenchymal transition in lens epithelium
    • Gotoh N., Perdue N.R., Matsushima H., Sage E.H., Yan Q., and Clark J.I. An in vitro model of posterior capsular opacity: sPARC and TGF-beta2 minimize epithelial-to-mesenchymal transition in lens epithelium. Invest. Ophthalmol. Vis. Sci. 48 (2007) 4679-4687
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , pp. 4679-4687
    • Gotoh, N.1    Perdue, N.R.2    Matsushima, H.3    Sage, E.H.4    Yan, Q.5    Clark, J.I.6
  • 25
    • 0041419592 scopus 로고    scopus 로고
    • Resolving morphology and antibody labeling over large distances in tissue sections
    • Jacobs M.D., Donaldson P.J., Cannell M.B., and Soeller C. Resolving morphology and antibody labeling over large distances in tissue sections. Microsc. Res. Tech. 62 (2003) 83-91
    • (2003) Microsc. Res. Tech. , vol.62 , pp. 83-91
    • Jacobs, M.D.1    Donaldson, P.J.2    Cannell, M.B.3    Soeller, C.4
  • 26
    • 34147114722 scopus 로고    scopus 로고
    • The neuronal channel NALCN contributes resting sodium permeability and is required for normal respiratory rhythm
    • Lu B., Su Y., Das S., Liu J., Xia J., and Ren D. The neuronal channel NALCN contributes resting sodium permeability and is required for normal respiratory rhythm. Cell 129 (2007) 371-383
    • (2007) Cell , vol.129 , pp. 371-383
    • Lu, B.1    Su, Y.2    Das, S.3    Liu, J.4    Xia, J.5    Ren, D.6
  • 27
    • 52449129231 scopus 로고    scopus 로고
    • Accentuated osteoclastic response to parathyroid hormone undermines bone mass acquisition in osteonectin-null mice
    • Machado do Reis L., Kessler C.B., Adams D.J., Lorenzo J., Jorgetti V., and Delany A.M. Accentuated osteoclastic response to parathyroid hormone undermines bone mass acquisition in osteonectin-null mice. Bone 43 (2008) 264-273
    • (2008) Bone , vol.43 , pp. 264-273
    • Machado do Reis, L.1    Kessler, C.B.2    Adams, D.J.3    Lorenzo, J.4    Jorgetti, V.5    Delany, A.M.6
  • 28
    • 2642544131 scopus 로고    scopus 로고
    • Impaired cytoskeletal organization and membrane integrity in lens fibers of a Rho GTPase functional knockout transgenic mouse
    • Maddala R., Deng P.F., Costello J.M., Wawrousek E.F., Zigler J.S., and Rao V.P. Impaired cytoskeletal organization and membrane integrity in lens fibers of a Rho GTPase functional knockout transgenic mouse. Lab. Invest. 84 (2004) 679-692
    • (2004) Lab. Invest. , vol.84 , pp. 679-692
    • Maddala, R.1    Deng, P.F.2    Costello, J.M.3    Wawrousek, E.F.4    Zigler, J.S.5    Rao, V.P.6
  • 29
    • 39249084792 scopus 로고    scopus 로고
    • Rho GDP dissociation inhibitor-mediated disruption of Rho GTPase activity impairs lens fiber cell migration, elongation and survival
    • Maddala R., Reneker L.W., Pendurthi B., and Rao P.V. Rho GDP dissociation inhibitor-mediated disruption of Rho GTPase activity impairs lens fiber cell migration, elongation and survival. Dev. Biol. 315 (2008) 217-231
    • (2008) Dev. Biol. , vol.315 , pp. 217-231
    • Maddala, R.1    Reneker, L.W.2    Pendurthi, B.3    Rao, P.V.4
  • 30
    • 4043137958 scopus 로고    scopus 로고
    • Gene expression changes during cataract progression in Sparc null mice: differential regulation of mouse globins in the lens
    • Mansergh F.C., Wride M.A., Walker V.E., Adams S., Hunter S.M., and Evans M.J. Gene expression changes during cataract progression in Sparc null mice: differential regulation of mouse globins in the lens. Mol. Vis. 10 (2004) 490-511
    • (2004) Mol. Vis. , vol.10 , pp. 490-511
    • Mansergh, F.C.1    Wride, M.A.2    Walker, V.E.3    Adams, S.4    Hunter, S.M.5    Evans, M.J.6
  • 31
    • 0031014473 scopus 로고    scopus 로고
    • Physiological properties of the normal lens
    • Mathias R.T., Rae J.L., and Baldo G.J. Physiological properties of the normal lens. Physiol. Rev. 77 (1997) 21-50
    • (1997) Physiol. Rev. , vol.77 , pp. 21-50
    • Mathias, R.T.1    Rae, J.L.2    Baldo, G.J.3
  • 34
    • 44449119580 scopus 로고    scopus 로고
    • Noninvasive measurement of protein aggregation by mutant huntingtin fragments or alpha-synuclein in the lens
    • Muchowski P.J., Ramsden R., Nguyen Q., Arnett E.E., Greiling T.M., Anderson S.K., and Clark J.I. Noninvasive measurement of protein aggregation by mutant huntingtin fragments or alpha-synuclein in the lens. J. Biol. Chem. 283 (2008) 6330-6336
    • (2008) J. Biol. Chem. , vol.283 , pp. 6330-6336
    • Muchowski, P.J.1    Ramsden, R.2    Nguyen, Q.3    Arnett, E.E.4    Greiling, T.M.5    Anderson, S.K.6    Clark, J.I.7
  • 36
    • 0033807857 scopus 로고    scopus 로고
    • Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface
    • Norose K., Lo W.K., Clark J.I., Sage E.H., and Howe C.C. Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface. Exp. Eye Res. 71 (2000) 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
  • 37
    • 0037294904 scopus 로고    scopus 로고
    • Genetics of arrhythmogenic right ventricular cardiomyopathy - status quo and future perspectives
    • Paul M., Schulze-Bahr E., Breithardt G., and Wichter T. Genetics of arrhythmogenic right ventricular cardiomyopathy - status quo and future perspectives. Z. Kardiol. 92 (2003) 128-136
    • (2003) Z. Kardiol. , vol.92 , pp. 128-136
    • Paul, M.1    Schulze-Bahr, E.2    Breithardt, G.3    Wichter, T.4
  • 38
    • 0037331246 scopus 로고    scopus 로고
    • Compromised production of extracellular matrix in mice lacking secreted protein, acidic and rich in cysteine (SPARC) leads to a reduced foreign body reaction to implanted biomaterials
    • Puolakkainen P., Bradshaw A.D., Kyriakides T.R., Reed M., Brekken R., Wight T., Bornstein P., Ratner B., and Sage E.H. Compromised production of extracellular matrix in mice lacking secreted protein, acidic and rich in cysteine (SPARC) leads to a reduced foreign body reaction to implanted biomaterials. Am. J. Pathol. 162 (2003) 627-635
    • (2003) Am. J. Pathol. , vol.162 , pp. 627-635
    • Puolakkainen, P.1    Bradshaw, A.D.2    Kyriakides, T.R.3    Reed, M.4    Brekken, R.5    Wight, T.6    Bornstein, P.7    Ratner, B.8    Sage, E.H.9
  • 40
    • 0036078786 scopus 로고    scopus 로고
    • Basal lamina of ovarian follicle regulates an inward Cl(-) current in differentiated granulosa cells
    • Qin W., Rane S.G., and Asem E.K. Basal lamina of ovarian follicle regulates an inward Cl(-) current in differentiated granulosa cells. Am. J. Physiol. Cell Physiol. 282 (2002) C34-C48
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Qin, W.1    Rane, S.G.2    Asem, E.K.3
  • 41
    • 0036172408 scopus 로고    scopus 로고
    • Rho GTPase inactivation impairs lens growth and integrity
    • Rao V., Wawrousek E., Tamm E.R., and Zigler Jr. S. Rho GTPase inactivation impairs lens growth and integrity. Lab. Invest. 82 (2002) 231-239
    • (2002) Lab. Invest. , vol.82 , pp. 231-239
    • Rao, V.1    Wawrousek, E.2    Tamm, E.R.3    Zigler Jr., S.4
  • 43
    • 0032512628 scopus 로고    scopus 로고
    • Sodium channel protein expression enhances the invasiveness of rat and human prostate cancer cells
    • Smith P., Rhodes N.P., Shortland A.P., Fraser S.P., Djamgoz M.B., Ke Y., and Foster C.S. Sodium channel protein expression enhances the invasiveness of rat and human prostate cancer cells. FEBS Lett. 423 (1998) 19-24
    • (1998) FEBS Lett. , vol.423 , pp. 19-24
    • Smith, P.1    Rhodes, N.P.2    Shortland, A.P.3    Fraser, S.P.4    Djamgoz, M.B.5    Ke, Y.6    Foster, C.S.7
  • 44
    • 33748682313 scopus 로고    scopus 로고
    • The influence of sodium-calcium exchange inhibitors on rabbit lens ion balance and transparency
    • Tamiya S., and Delamere N.A. The influence of sodium-calcium exchange inhibitors on rabbit lens ion balance and transparency. Exp. Eye Res. 83 (2006) 1089-1095
    • (2006) Exp. Eye Res. , vol.83 , pp. 1089-1095
    • Tamiya, S.1    Delamere, N.A.2
  • 45
    • 0033953871 scopus 로고    scopus 로고
    • Immediate cell signal induced by laminin in rat sertoli cells
    • Taranta A., Teti A., Stefanini M., and D'Agostino A. Immediate cell signal induced by laminin in rat sertoli cells. Matrix Biol. 19 (2000) 11-18
    • (2000) Matrix Biol. , vol.19 , pp. 11-18
    • Taranta, A.1    Teti, A.2    Stefanini, M.3    D'Agostino, A.4
  • 47
    • 24944534978 scopus 로고    scopus 로고
    • Real-time PCR for mRNA quantitation
    • Wong M.L., and Medrano J.F. Real-time PCR for mRNA quantitation. Biotechniques 39 (2005) 75-85
    • (2005) Biotechniques , vol.39 , pp. 75-85
    • Wong, M.L.1    Medrano, J.F.2
  • 49
    • 33749127461 scopus 로고    scopus 로고
    • Ras signaling is essential for lens cell proliferation and lens growth during development
    • Xie L., Overbeek P.A., and Reneker L.W. Ras signaling is essential for lens cell proliferation and lens growth during development. Dev. Biol. 298 (2006) 403-414
    • (2006) Dev. Biol. , vol.298 , pp. 403-414
    • Xie, L.1    Overbeek, P.A.2    Reneker, L.W.3
  • 50
    • 0036629346 scopus 로고    scopus 로고
    • Alterations in the lens capsule contribute to cataractogenesis in SPARC-null mice
    • Yan Q., Clark J.I., Wight T.N., and Sage E.H. Alterations in the lens capsule contribute to cataractogenesis in SPARC-null mice. J. Cell Sci. 115 (2002) 2747-2756
    • (2002) J. Cell Sci. , vol.115 , pp. 2747-2756
    • Yan, Q.1    Clark, J.I.2    Wight, T.N.3    Sage, E.H.4
  • 51
    • 0037389333 scopus 로고    scopus 로고
    • Expression of the matricellular protein SPARC in murine lens: sPARC is necessary for the structural integrity of the capsular basement membrane
    • Yan Q., Blake D., Clark J.I., and Sage E.H. Expression of the matricellular protein SPARC in murine lens: sPARC is necessary for the structural integrity of the capsular basement membrane. J. Histochem. Cytochem. 51 (2003) 503-511
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 503-511
    • Yan, Q.1    Blake, D.2    Clark, J.I.3    Sage, E.H.4
  • 52
    • 31544449337 scopus 로고    scopus 로고
    • Absence of SPARC in murine lens epithelium leads to increased deposition of laminin-1 in lens capsule
    • Yan Q., Perdue N., Blake D., and Sage E.H. Absence of SPARC in murine lens epithelium leads to increased deposition of laminin-1 in lens capsule. Invest. Ophthalmol. Vis. Sci. 46 (2005) 4652-4660
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 4652-4660
    • Yan, Q.1    Perdue, N.2    Blake, D.3    Sage, E.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.