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Volumn 22, Issue 9, 2013, Pages 1507-1517

Lentiviral-encoded shRNA silencing of proteoglycan decorin enhances tendon repair and regeneration within a rat model

Author keywords

Decorin; Engineered tendon; Lentivirus; Patellar tendon; Short hairpin RNA (shRNA)

Indexed keywords

COLLAGEN FIBRIL; COLLAGEN TYPE 1; DECORIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GREEN FLUORESCENT PROTEIN; LENTIVIRUS VECTOR; PROTEOGLYCAN; SHORT HAIRPIN RNA; TRANSFORMING GROWTH FACTOR BETA1; TRANSFORMING GROWTH FACTOR BETA3;

EID: 84883537501     PISSN: 09636897     EISSN: None     Source Type: Journal    
DOI: 10.3727/096368912X661292     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 56449093573 scopus 로고    scopus 로고
    • Changes in gene expression of matrix constituents with respect to passage of ligament and tendon fibroblasts
    • Almarza, A. J.; Augustine, S. M.; Woo, S. L. Changes in gene expression of matrix constituents with respect to passage of ligament and tendon fibroblasts. Ann. Biomed. Eng. 36(12): 1927-1933; 2008.
    • (2008) Ann. Biomed. Eng , vol.36 , Issue.12 , pp. 1927-1933
    • Almarza, A.J.1    Augustine, S.M.2    Woo, S.L.3
  • 3
    • 33750978402 scopus 로고    scopus 로고
    • Collagen type V enhances matrix contraction by human periodontal ligament fibroblasts seeded in three-dimensional collagen gels
    • Berendsen, A. D.; Antonius, L. J. J.; Bronckers, T. H.; Smit, X.; Frank, W.; Vincent, E. Collagen type V enhances matrix contraction by human periodontal ligament fibroblasts seeded in three-dimensional collagen gels. Matrix Biol. 25:515-522; 2006.
    • (2006) Matrix Biol , vol.25 , pp. 515-522
    • Berendsen, A.D.1    Antonius, L.J.J.2    Bronckers, T.H.3    Smit, X.4    Frank, W.5    Vincent, E.6
  • 5
    • 0031734721 scopus 로고    scopus 로고
    • Altered levels of extracellular matrix molecule mRNA in healing rabbit ligaments
    • Boykiw, R.; Sciore, P.; Reno, C; Marchuk, L.; Frank, C. B.; Hart, D. A. Altered levels of extracellular matrix molecule mRNA in healing rabbit ligaments. Matrix Biol. 17:371-378; 1998.
    • (1998) Matrix Biol , vol.17 , pp. 371-378
    • Boykiw, R.1    Sciore, P.2    Reno, C.3    Marchuk, L.4    Frank, C.B.5    Hart, D.A.6
  • 6
    • 0036905451 scopus 로고    scopus 로고
    • Collagen fibril biosynthesis in tendon: A review and recent insights
    • Canty, E. G.; Kadler, K. E. Collagen fibril biosynthesis in tendon: A review and recent insights. Comp. Biochem. Physiol. A 133:979-985; 2002.
    • (2002) Comp. Biochem. Physiol. A , vol.133 , pp. 979-985
    • Canty, E.G.1    Kadler, K.E.2
  • 7
    • 0035859929 scopus 로고    scopus 로고
    • Specific interference with gene expression induced by long, double-stranded RNA in mouse embryonal terato-carcinoma cell lines
    • Caplen, N. J.; Parrish, S.; Imani, E; Fire, A.; Morgan, R. A. Specific interference with gene expression induced by long, double-stranded RNA in mouse embryonal terato-carcinoma cell lines. Proc. Natl. Acad. Sci. USA 98:9742-9747; 2001.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9742-9747
    • Caplen, N.J.1    Parrish, S.2    Imani, E.3    Fire, A.4    Morgan, R.A.5
  • 8
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson, K. G.; Baribault, H.; Holmes, D. E; Graham, H.; Kadler, K. E.; Iozzo, R. V, Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell. Biol. 136(3):729-743; 1997.
    • (1997) J. Cell. Biol , vol.136 , Issue.3 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.E.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 9
    • 0035025639 scopus 로고    scopus 로고
    • Retroviral overexpression of decorin differentially affects the response of arterial smooth muscle cells to growth factors
    • Fischer, J. W.; Kinsella, M. G; Levkau, B.; Clowes, A. W.; Wight, T. N. Retroviral overexpression of decorin differentially affects the response of arterial smooth muscle cells to growth factors. Arterioscler. Thromb. Vase. Biol. 21:777-784; 2001.
    • (2001) Arterioscler. Thromb. Vase. Biol , vol.21 , pp. 777-784
    • Fischer, J.W.1    Kinsella, M.G.2    Levkau, B.3    Clowes, A.W.4    Wight, T.N.5
  • 11
    • 0028902155 scopus 로고
    • Rabbit medial collateral ligament scar weakness is associated with decreased collagen pyridinoline crosslink density
    • Frank, C; McDonald, D.; Wilson, J. Eyre, D.; Shrive, N. Rabbit medial collateral ligament scar weakness is associated with decreased collagen pyridinoline crosslink density. J. Orthop. Res. 13:157-165; 1995.
    • (1995) J. Orthop. Res , vol.13 , pp. 157-165
    • Frank, C.1    McDonald, D.2    Wilson, J.3    Eyre, D.4    Shrive, N.5
  • 12
    • 0021014513 scopus 로고
    • Medial collateral ligament healing: A mul-tidisciplinary assessment in rabbits
    • Frank, C; Woo, S. L.; Amiel, D.; Harwood, E; Gomez, M.; Akeson, W. Medial collateral ligament healing: A mul-tidisciplinary assessment in rabbits. Am. J. Sports Med. 11:379-389; 1983.
    • (1983) Am. J. Sports Med , vol.11 , pp. 379-389
    • Frank, C.1    Woo, S.L.2    Amiel, D.3    Harwood, E.4    Gomez, M.5    Akeson, W.6
  • 13
    • 84946031884 scopus 로고
    • Procedure for detecting outlying observations in samples
    • Grubbs, E E. Procedure for detecting outlying observations in samples. Technometrics 11:1-21; 1969.
    • (1969) Technometrics , vol.11 , pp. 1-21
    • Grubbs, E.E.1
  • 15
    • 77952550108 scopus 로고    scopus 로고
    • The role of small leucine-rich proteoglycans in collagen fibrillogenesis
    • Kalamajski, S.; Oldberg, A. The role of small leucine-rich proteoglycans in collagen fibrillogenesis. Matrix Biol. 29:248-253; 2010.
    • (2010) Matrix Biol , vol.29 , pp. 248-253
    • Kalamajski, S.1    Oldberg, A.2
  • 16
    • 3142726302 scopus 로고    scopus 로고
    • The regulated synthesis of versican, decorin, and biglycan: Extracellular matrix proteoglycans that influence cellular phenotype
    • Kinsella, M. G; Bressler, S. L.; Wight, T. N. The regulated synthesis of versican, decorin, and biglycan: Extracellular matrix proteoglycans that influence cellular phenotype. Crit. Rev. Eukaryot. Gene Expr. 14:203-234; 2004.
    • (2004) Crit. Rev. Eukaryot. Gene Expr , vol.14 , pp. 203-234
    • Kinsella, M.G.1    Bressler, S.L.2    Wight, T.N.3
  • 17
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • Kjaer, M. Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol. Rev. 84:649-698; 2004.
    • (2004) Physiol. Rev , vol.84 , pp. 649-698
    • Kjaer, M.1
  • 19
    • 0035168796 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular matrix and growth control
    • Kresse, H.; Schonherr, E. Proteoglycans of the extracellular matrix and growth control. J. Cell. Physiol. 189(3):266-274; 2001.
    • (2001) J. Cell. Physiol , vol.189 , Issue.3 , pp. 266-274
    • Kresse, H.1    Schonherr, E.2
  • 20
    • 53049090671 scopus 로고    scopus 로고
    • Mechanoactive tenogenic differentiation of human mesenchymal stem cells
    • Kuo, C. K.; Tuan, R. S. Mechanoactive tenogenic differentiation of human mesenchymal stem cells. Tissue Eng. Part A 14(10):1615-1627;2008.
    • (2008) Tissue Eng. Part A , vol.14 , Issue.10 , pp. 1615-1627
    • Kuo, C.K.1    Tuan, R.S.2
  • 21
    • 3242780860 scopus 로고    scopus 로고
    • Matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase mRNA levels are specifically altered in torn rotator cuff tendons
    • Lo, I. K.; Marchuk, L. L.; Hollinshead, R.; Hart, D. A.; Frank, C. B. Matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase mRNA levels are specifically altered in torn rotator cuff tendons. Am. J. Sports Med. 32(5):1223-1229; 2004.
    • (2004) Am. J. Sports Med , vol.32 , Issue.5 , pp. 1223-1229
    • Lo, I.K.1    Marchuk, L.L.2    Hollinshead, R.3    Hart, D.A.4    Frank, C.B.5
  • 22
    • 0033732919 scopus 로고    scopus 로고
    • Influence of decorin expression on transforming growth factor-(3-mediated collagen gel retraction and biglycan induction
    • Markmann, A.; Hausser, H.; Schonherr, E.; Kresse, H. Influence of decorin expression on transforming growth factor-(3-mediated collagen gel retraction and biglycan induction. Matrix Biol. 19(7):631-636; 2000.
    • (2000) Matrix Biol , vol.19 , Issue.7 , pp. 631-636
    • Markmann, A.1    Hausser, H.2    Schonherr, E.3    Kresse, H.4
  • 23
  • 24
    • 0034232654 scopus 로고    scopus 로고
    • Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo
    • Nakamura, N.; Hart, D. A.; Boorman, R. S.; Kaneda, Y.; Shrive, N. G.; Marchuk, L. L.; Shino, K; Ochi, T.; Frank, C. B. Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo. J. Orthop. Res. 18:517-523; 2000.
    • (2000) J. Orthop. Res , vol.18 , pp. 517-523
    • Nakamura, N.1    Hart, D.A.2    Boorman, R.S.3    Kaneda, Y.4    Shrive, N.G.5    Marchuk, L.L.6    Shino, K.7    Ochi, T.8    Frank, C.B.9
  • 25
    • 39749119235 scopus 로고    scopus 로고
    • Do colla-genases unwind triple-helical collagen before peptide bond hydrolysis? Reinterpreting experimental observations with mathematical models
    • Nerenberg, P. S.; Salsas-Escat R.; Stultz, C. M. Do colla-genases unwind triple-helical collagen before peptide bond hydrolysis? Reinterpreting experimental observations with mathematical models. Proteins 70(4):1154-1161; 2008.
    • (2008) Proteins , vol.70 , Issue.4 , pp. 1154-1161
    • Nerenberg, P.S.1    Salsas-Escat, R.2    Stultz, C.M.3
  • 26
    • 1642452660 scopus 로고    scopus 로고
    • Expression of small hairpin RNA by lentivirus-based vector confers efficient and stable gene-suppression of HIV-1 on human cells including primary non-dividing cells
    • Nishitsuji, H.; Ikeda, T.; Miyoshi, H.; Ohashi, T.; Kannagi, M.; Masuda, T. Expression of small hairpin RNA by lentivirus-based vector confers efficient and stable gene-suppression of HIV-1 on human cells including primary non-dividing cells. Microbes Infect. 6(l):76-85; 2004.
    • (2004) Microbes Infect , vol.6 , Issue.1 , pp. 76-85
    • Nishitsuji, H.1    Ikeda, T.2    Miyoshi, H.3    Ohashi, T.4    Kannagi, M.5    Masuda, T.6
  • 28
    • 70349330118 scopus 로고    scopus 로고
    • Decorin core protein (Decoron) shape complements collagen fibril surface structure and mediates its binding
    • Orge, J. P. R. O.; Eid, A.; Antipova, O.; Bella, J.; Scott, I. E. Decorin core protein (Decoron) shape complements collagen fibril surface structure and mediates its binding. PLoS One 4 (9):e7028; 2009.
    • (2009) PLoS One , vol.4 , Issue.9
    • Orge, J.P.R.O.1    Eid, A.2    Antipova, O.3    Bella, J.4    Scott, I.E.5
  • 29
    • 0141763811 scopus 로고    scopus 로고
    • The role of decorin in collagen fibrillogenesis and skin homeostasis
    • Reed, C. C; lozzo, R. V. The role of decorin in collagen fibrillogenesis and skin homeostasis. Glycoconj. J. 19:249-255; 2002.
    • (2002) Glycoconj. J , vol.19 , pp. 249-255
    • Reed, C.C.1    Lozzo, R.V.2
  • 31
    • 52049122865 scopus 로고    scopus 로고
    • Biological functions of the small leucine-rich proteoglycans: From genetics to signal trans-duct
    • Schaefer, L.; lozzo, R. V. Biological functions of the small leucine-rich proteoglycans: From genetics to signal trans-duct. J. Biol. Chem. 283:21305-21309; 2008.
    • (2008) J. Biol. Chem , vol.283 , pp. 21305-21309
    • Schaefer, L.1    Lozzo, R.V.2
  • 33
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped
    • Scott, J. E. Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications fortheir interactions with collagen. Biochemistry 35:8795-8799; 1996.
    • (1996) Implications Fortheir Interactions With Collagen. Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 34
    • 8144221077 scopus 로고    scopus 로고
    • Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
    • Scott, P. G; McEwan, P. A.; Dodd, C. M.; Bergmann, E. M.; Bishop, P. N; Bella, J. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc. Natl. Acad. Sci. USA 101(44): 15633-15638; 2004.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.44 , pp. 15633-15638
    • Scott, P.G.1    McEwan, P.A.2    Dodd, C.M.3    Bergmann, E.M.4    Bishop, P.N.5    Bella, J.6
  • 35
    • 33748755116 scopus 로고    scopus 로고
    • Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation
    • Seidler, D. G; Goldoni, S.; Agnew, C; Cardi, C; Thakur, M. L.; Owens, R. T.; McQuillan, D. L; lozzo, R. V. Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation. J. Biol. Chem. 281:26408-26418; 2006.
    • (2006) J. Biol. Chem , vol.281 , pp. 26408-26418
    • Seidler, D.G.1    Goldoni, S.2    Agnew, C.3    Cardi, C.4    Thakur, M.L.5    Owens, R.T.6    McQuillan, D.L.7    Lozzo, R.V.8
  • 36
    • 11844274558 scopus 로고    scopus 로고
    • Tendon injury and tendinopathy: Healing and repair
    • Sharma, P.; Maffulli, N. Tendon injury and tendinopathy: Healing and repair. J. Bone Joint Surg. Am. 87:187-202; 2005.
    • (2005) J. Bone Joint Surg. Am , vol.87 , pp. 187-202
    • Sharma, P.1    Maffulli, N.2
  • 37
    • 33745439465 scopus 로고    scopus 로고
    • Mechanobiology of tendon
    • Wang, J. H. C. Mechanobiology of tendon. J. Biomech. 39(9):1563-1582; 2006.
    • (2006) J. Biomech , vol.39 , Issue.9 , pp. 1563-1582
    • Wang, J.H.C.1
  • 38
    • 26444566714 scopus 로고    scopus 로고
    • Control of the collagen fibril diameter in the equine superficial digital flexor tendon in horses by decorin
    • Watanabe, T; Hosaka, Y; Yamamoto, E.; Ueda, H.; Sugawara, K; Takahashi, H.; Takehana, K. Control of the collagen fibril diameter in the equine superficial digital flexor tendon in horses by decorin. J. Vet. Med. Sci. 67(9):855-860; 2005.
    • (2005) J. Vet. Med. Sci , vol.67 , Issue.9 , pp. 855-860
    • Watanabe, T.1    Hosaka, Y.2    Yamamoto, E.3    Ueda, H.4    Sugawara, K.5    Takahashi, H.6    Takehana, K.7
  • 39
    • 0029778529 scopus 로고    scopus 로고
    • V Model structure of decorin and implications for collagen fibrillogenesis
    • Weber, I. T.; Harrison, R. W.; lozzo, R. V Model structure of decorin and implications for collagen fibrillogenesis. J. Biol. Chem. 271(50):31767-31770; 1996.
    • (1996) J. Biol. Chem , vol.271 , Issue.50 , pp. 31767-31770
    • Weber, I.T.1    Harrison, R.W.2    Lozzo, R.3
  • 41
    • 11144242752 scopus 로고    scopus 로고
    • Reduced type I collagen utilization: A pathogenic mechanism in COL5A1 halpo-insuffecient Ehlers-Danlos syndrome
    • Wenstrup, R. L; Florer, J. B.; Cole, W. G; Willing, M. C; Birk, D. E.; Reduced type I collagen utilization: A pathogenic mechanism in COL5A1 halpo-insuffecient Ehlers-Danlos syndrome. J. Cell. Biochem. 92:113-124; 2004.
    • (2004) J. Cell. Biochem , vol.92 , pp. 113-124
    • Wenstrup, R.L.1    Florer, J.B.2    Cole, W.G.3    Willing, M.C.4    Birk, D.E.5
  • 43
    • 18744413600 scopus 로고    scopus 로고
    • Tendon proteoglycans: Biochemistry and function
    • Yoon, J. H.; Halper, J. Tendon proteoglycans: Biochemistry and function. J. Musculoskelet. Neuronal Interact. 5(1): 22-34; 2005.
    • (2005) J. Musculoskelet. Neuronal Interact , vol.5 , Issue.1 , pp. 22-34
    • Yoon, J.H.1    Halper, J.2
  • 44
    • 0034737298 scopus 로고    scopus 로고
    • RNAi: Double-stranded RNA directs the ATP-dependent cleavage of mRNA to 21 to 23 nucleotide intervals
    • Zamore, P. D.; Tuschl, T.; Sharp, P. A.; Bartel, D. P. RNAi: Double-stranded RNA directs the ATP-dependent cleavage of mRNA to 21 to 23 nucleotide intervals. Cell 101:25-33; 2000.
    • (2000) Cell , vol.101 , pp. 25-33
    • Zamore, P.D.1    Tuschl, T.2    Sharp, P.A.3    Bartel, D.P.4


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