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Volumn 183, Issue 1, 2013, Pages 247-256

Intracellularly-retained decorin lacking the C-terminal ear repeat causes ER stress: A cell-based etiological mechanism for congenital stromal corneal dystrophy

Author keywords

[No Author keywords available]

Indexed keywords

DECORIN;

EID: 84879368222     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2013.04.001     Document Type: Article
Times cited : (25)

References (42)
  • 1
    • 85194376827 scopus 로고    scopus 로고
    • Collagens, suprastructures, and collagen fibril assembly
    • R.P. Mecham, Springer New York
    • D.E. Birk, and P. Bruckner Collagens, suprastructures, and collagen fibril assembly R.P. Mecham, The Extracellular Matrix: an Overview 2011 Springer New York 77 115
    • (2011) The Extracellular Matrix: An Overview , pp. 77-115
    • Birk, D.E.1    Bruckner, P.2
  • 2
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans: Functional network of interactive proteins
    • R.V. Iozzo The biology of the small leucine-rich proteoglycans: functional network of interactive proteins J Biol Chem 274 1999 18843 18846
    • (1999) J Biol Chem , vol.274 , pp. 18843-18846
    • Iozzo, R.V.1
  • 4
    • 77956637386 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Emerging concepts and future directions
    • R.V. Iozzo, and N. Karamanos Proteoglycans in health and disease: emerging concepts and future directions FEBS J 277 2010 3863
    • (2010) FEBS J , vol.277 , pp. 3863
    • Iozzo, R.V.1    Karamanos, N.2
  • 5
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • R.V. Iozzo, and L. Schaefer Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans FEBS J 277 2010 3864 3875
    • (2010) FEBS J , vol.277 , pp. 3864-3875
    • Iozzo, R.V.1    Schaefer, L.2
  • 7
    • 81355127411 scopus 로고    scopus 로고
    • A novel mutation of the decorin gene identified in a Korean family with congenital hereditary stromal dystrophy
    • J.H. Kim, J.M. Ko, I. Lee, J.Y. Kim, M.J. Kim, and H. Tchah A novel mutation of the decorin gene identified in a Korean family with congenital hereditary stromal dystrophy Cornea 30 2011 1473 1477
    • (2011) Cornea , vol.30 , pp. 1473-1477
    • Kim, J.H.1    Ko, J.M.2    Lee, I.3    Kim, J.Y.4    Kim, M.J.5    Tchah, H.6
  • 8
    • 33748850603 scopus 로고    scopus 로고
    • A second decorin frame shift mutation in a family with congenital stromal corneal dystrophy
    • E. Rødahl, R. Van Ginderdeuren, P.M. Knappskog, C. Bredrup, and H. Boman A second decorin frame shift mutation in a family with congenital stromal corneal dystrophy Am J Ophthalmol 142 2006 520 521
    • (2006) Am J Ophthalmol , vol.142 , pp. 520-521
    • Rødahl, E.1    Van Ginderdeuren, R.2    Knappskog, P.M.3    Bredrup, C.4    Boman, H.5
  • 10
    • 80055005154 scopus 로고    scopus 로고
    • Pathophysiological mechanisms of autosomal dominant congenital stromal corneal dystrophy: C-terminal-truncated decorin results in abnormal matrix assembly and altered expression of small leucine-rich proteoglycans
    • S. Chen, M. Sun, X. Meng, R.V. Iozzo, W.W. Kao, and D.E. Birk Pathophysiological mechanisms of autosomal dominant congenital stromal corneal dystrophy: C-terminal-truncated decorin results in abnormal matrix assembly and altered expression of small leucine-rich proteoglycans Am J Pathol 179 2011 2409 2419
    • (2011) Am J Pathol , vol.179 , pp. 2409-2419
    • Chen, S.1    Sun, M.2    Meng, X.3    Iozzo, R.V.4    Kao, W.W.5    Birk, D.E.6
  • 11
    • 52049122865 scopus 로고    scopus 로고
    • Biological functions of the small leucine-rich proteoglycans: From genetics to signal transduction
    • L. Schaefer, and R.V. Iozzo Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction J Biol Chem 283 2008 21305 21309
    • (2008) J Biol Chem , vol.283 , pp. 21305-21309
    • Schaefer, L.1    Iozzo, R.V.2
  • 12
    • 0030986608 scopus 로고    scopus 로고
    • The family of the small leucine-rich proteoglycans: Key regulators of matrix assembly and cellular growth
    • R.V. Iozzo The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth Crit Rev Biochem Mol Biol 32 1997 141 174
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 141-174
    • Iozzo, R.V.1
  • 13
    • 79956368992 scopus 로고    scopus 로고
    • Focus on molecules: Decorin
    • S. Chen, and D.E. Birk Focus on molecules: decorin Exp Eye Res 92 2010 444 445
    • (2010) Exp Eye Res , vol.92 , pp. 444-445
    • Chen, S.1    Birk, D.E.2
  • 15
    • 34447536155 scopus 로고    scopus 로고
    • The decorin sequence SYIRIADTNIT binds collagen type i
    • S. Kalamajski, A. Aspberg, and A. Oldberg The decorin sequence SYIRIADTNIT binds collagen type I J Biol Chem 282 2007 16062 16067
    • (2007) J Biol Chem , vol.282 , pp. 16062-16067
    • Kalamajski, S.1    Aspberg, A.2    Oldberg, A.3
  • 16
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope
    • M. Santra, C.C. Reed, and R.V. Iozzo Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope J Biol Chem 277 2002 35671 35681
    • (2002) J Biol Chem , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 17
    • 84857479041 scopus 로고    scopus 로고
    • The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-β-dependent signaling, and inhibits TGF-β-dependent fibrotic response in skeletal muscles
    • C. Cabello-Verrugio, C. Santander, C. Cofré, M.J. Acuña, F. Melo, and E. Brandan The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-β-dependent signaling, and inhibits TGF-β-dependent fibrotic response in skeletal muscles J Biol Chem 287 2012 6773 6787
    • (2012) J Biol Chem , vol.287 , pp. 6773-6787
    • Cabello-Verrugio, C.1    Santander, C.2    Cofré, C.3    Acuña, M.J.4    Melo, F.5    Brandan, E.6
  • 18
    • 79959865250 scopus 로고    scopus 로고
    • Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity
    • C. Vial, J. Gutiérrez, C. Santander, D. Cabrera, and E. Brandan Decorin interacts with connective tissue growth factor (CTGF)/CCN2 by LRR12 inhibiting its biological activity J Biol Chem 286 2011 24242 24252
    • (2011) J Biol Chem , vol.286 , pp. 24242-24252
    • Vial, C.1    Gutiérrez, J.2    Santander, C.3    Cabrera, D.4    Brandan, E.5
  • 20
    • 33747781400 scopus 로고    scopus 로고
    • Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans
    • P.A. McEwan, P.G. Scott, P.N. Bishop, and J. Bella Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans J Struct Biol 155 2006 294 305
    • (2006) J Struct Biol , vol.155 , pp. 294-305
    • McEwan, P.A.1    Scott, P.G.2    Bishop, P.N.3    Bella, J.4
  • 21
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • K.G. Danielson, H. Baribault, D.F. Holmes, H. Graham, K.E. Kadler, and R.V. Iozzo Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility J Cell Biol 136 1997 729 743
    • (1997) J Cell Biol , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 22
    • 77149168134 scopus 로고    scopus 로고
    • Fibromodulin regulates collagen fibrillogenesis during peripheral corneal development
    • S. Chen, A. Oldberg, S. Chakravarti, and D.E. Birk Fibromodulin regulates collagen fibrillogenesis during peripheral corneal development Dev Dyn 239 2010 844 854
    • (2010) Dev Dyn , vol.239 , pp. 844-854
    • Chen, S.1    Oldberg, A.2    Chakravarti, S.3    Birk, D.E.4
  • 23
    • 0023873382 scopus 로고
    • Collagen type i and type v are present in the same fibril in the avian corneal stroma
    • D.E. Birk, J.M. Fitch, J.P. Babiarz, and T.F. Linsenmayer Collagen type I and type V are present in the same fibril in the avian corneal stroma J Cell Biol 106 1988 999 1008
    • (1988) J Cell Biol , vol.106 , pp. 999-1008
    • Birk, D.E.1    Fitch, J.M.2    Babiarz, J.P.3    Linsenmayer, T.F.4
  • 24
    • 0028090059 scopus 로고
    • The murine decorin: Complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation
    • T. Scholzen, M. Solursh, S. Suzuki, R. Reiter, J.L. Morgan, A.M. Buchberg, L.D. Siracusa, and R.V. Iozzo The murine decorin: complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation J Biol Chem 269 1994 28270 28281
    • (1994) J Biol Chem , vol.269 , pp. 28270-28281
    • Scholzen, T.1    Solursh, M.2    Suzuki, S.3    Reiter, R.4    Morgan, J.L.5    Buchberg, A.M.6    Siracusa, L.D.7    Iozzo, R.V.8
  • 25
    • 0029382434 scopus 로고
    • Antisera and cDNA probes to human and certain animal model bone matrix noncollagenous proteins
    • L.W. Fisher, J.T. Stubbs 3rd, and M.F. Young Antisera and cDNA probes to human and certain animal model bone matrix noncollagenous proteins Acta Orthop Scand Suppl 266 1995 61 65
    • (1995) Acta Orthop Scand Suppl , vol.266 , pp. 61-65
    • Fisher, L.W.1    Stubbs III, J.T.2    Young, M.F.3
  • 27
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin
    • E. Brandan, C. Retamal, C. Cabello-Verrugio, and M.P. Marzolo The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin J Biol Chem 281 2006 31562 31571
    • (2006) J Biol Chem , vol.281 , pp. 31562-31571
    • Brandan, E.1    Retamal, C.2    Cabello-Verrugio, C.3    Marzolo, M.P.4
  • 28
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • P. Walter, and D. Ron The unfolded protein response: from stress pathway to homeostatic regulation Science 334 2011 1081 1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 29
    • 77954354827 scopus 로고    scopus 로고
    • In vivo cellular adaptation to ER stress: Survival strategies with double-edged consequences
    • K.Y. Tsang, D. Chan, J.F. Bateman, and K.S. Cheah In vivo cellular adaptation to ER stress: survival strategies with double-edged consequences J Cell Sci 123 2010 2145 2154
    • (2010) J Cell Sci , vol.123 , pp. 2145-2154
    • Tsang, K.Y.1    Chan, D.2    Bateman, J.F.3    Cheah, K.S.4
  • 30
    • 0024550294 scopus 로고
    • Deduced protein sequence of bone small proteoglycan i (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species
    • L.W. Fisher, J.D. Termine, and M.F. Young Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species J Biol Chem 264 1989 4571 4576
    • (1989) J Biol Chem , vol.264 , pp. 4571-4576
    • Fisher, L.W.1    Termine, J.D.2    Young, M.F.3
  • 31
    • 77955842202 scopus 로고    scopus 로고
    • The molecular basis of corneal transparency
    • J.R. Hassell, and D.E. Birk The molecular basis of corneal transparency Exp Eye Res 91 2010 326 335
    • (2010) Exp Eye Res , vol.91 , pp. 326-335
    • Hassell, J.R.1    Birk, D.E.2
  • 32
    • 0037484283 scopus 로고    scopus 로고
    • Keratocan-deficient mice display alterations in corneal structure
    • C.Y. Liu, D.E. Birk, J.R. Hassell, B. Kane, and W.W. Kao Keratocan-deficient mice display alterations in corneal structure J Biol Chem 278 2003 21672 21677
    • (2003) J Biol Chem , vol.278 , pp. 21672-21677
    • Liu, C.Y.1    Birk, D.E.2    Hassell, J.R.3    Kane, B.4    Kao, W.W.5
  • 33
    • 33748316797 scopus 로고    scopus 로고
    • Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea
    • S. Chakravarti, G. Zhang, I. Chervoneva, L. Roberts, and D.E. Birk Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea Dev Dyn 235 2006 2493 2506
    • (2006) Dev Dyn , vol.235 , pp. 2493-2506
    • Chakravarti, S.1    Zhang, G.2    Chervoneva, I.3    Roberts, L.4    Birk, D.E.5
  • 34
    • 84877691193 scopus 로고    scopus 로고
    • The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly
    • S. Chen, and D.E. Birk The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly FEBS J 280 2013 2120 2137
    • (2013) FEBS J , vol.280 , pp. 2120-2137
    • Chen, S.1    Birk, D.E.2
  • 35
    • 0033208952 scopus 로고    scopus 로고
    • Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperones
    • S.R. Lamandé, and J.F. Bateman Procollagen folding and assembly: the role of endoplasmic reticulum enzymes and molecular chaperones Semin Cell Dev Biol 10 1999 455 464
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 455-464
    • Lamandé, S.R.1    Bateman, J.F.2
  • 36
    • 41749116397 scopus 로고    scopus 로고
    • Procollagen triple helix assembly: An unconventional chaperone-assisted folding paradigm
    • E. Makareeva, and S. Leikin Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm PLoS One 2 2007 e1029
    • (2007) PLoS One , vol.2 , pp. 1029
    • Makareeva, E.1    Leikin, S.2
  • 40
    • 0029863286 scopus 로고    scopus 로고
    • Amino-terminal deletions in the decorin core protein leads to the biosynthesis of proteoglycans with shorter glycosaminoglycan chains
    • A. Oldberg, P. Antonsson, J. Moses, and L.A. Fransson Amino-terminal deletions in the decorin core protein leads to the biosynthesis of proteoglycans with shorter glycosaminoglycan chains FEBS Lett 386 1996 29 32
    • (1996) FEBS Lett , vol.386 , pp. 29-32
    • Oldberg, A.1    Antonsson, P.2    Moses, J.3    Fransson, L.A.4
  • 41
    • 6344228681 scopus 로고    scopus 로고
    • N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21
    • Y.B. Zhou, F. Liu, Z.D. Zhu, H. Zhu, X. Zhang, Z.Q. Wang, J.H. Liu, and Z.G. Han N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21 FEBS Lett 576 2004 401 407
    • (2004) FEBS Lett , vol.576 , pp. 401-407
    • Zhou, Y.B.1    Liu, F.2    Zhu, Z.D.3    Zhu, H.4    Zhang, X.5    Wang, Z.Q.6    Liu, J.H.7    Han, Z.G.8
  • 42
    • 84872015409 scopus 로고    scopus 로고
    • A novel decorin gene mutation in congenital hereditary stromal dystrophy: A Korean family
    • J.H. Lee, C.S. Ki, E.S. Chung, and T.Y. Chung A novel decorin gene mutation in congenital hereditary stromal dystrophy: a Korean family Korean J Ophthalmol 26 2012 301 305
    • (2012) Korean J Ophthalmol , vol.26 , pp. 301-305
    • Lee, J.H.1    Ki, C.S.2    Chung, E.S.3    Chung, T.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.