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Volumn 29, Issue 1, 2011, Pages 8-13

Thermal analysis reveals differential effects of various crosslinkers on bovine annulus fibrosis

Author keywords

calorimetry; crosslinking; degenerative disc disease; DSC; spinal disc

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; COLLAGEN; CROSS LINKING REAGENT; GENIPIN; GLUTARALDEHYDE; METHYLGLYOXAL; PROANTHOCYANIDIN; THREOSE; UNCLASSIFIED DRUG;

EID: 78649568272     PISSN: 07360266     EISSN: 1554527X     Source Type: Journal    
DOI: 10.1002/jor.21189     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 33747355707 scopus 로고    scopus 로고
    • What is intervertebral disc degeneration, and what causes it?
    • Adams MA, Roughley PJ,. 2006. What is intervertebral disc degeneration, and what causes it? Spine 31: 2151-2161.
    • (2006) Spine , vol.31 , pp. 2151-2161
    • Adams, M.A.1    Roughley, P.J.2
  • 2
    • 14844341394 scopus 로고    scopus 로고
    • Pathophysiology of lumbar disc degeneration: A review of the literature
    • Martin MD, Boxell CM, Malone DG,. 2002. Pathophysiology of lumbar disc degeneration: a review of the literature. Neurosurg Focus 13: 1-6.
    • (2002) Neurosurg Focus , vol.13 , pp. 1-6
    • Martin, M.D.1    Boxell, C.M.2    Malone, D.G.3
  • 3
    • 33645556769 scopus 로고    scopus 로고
    • Lumbar disc disorders and low-back pain: Socioeconomic factors and consequences
    • Katz JN,. 2006. Lumbar disc disorders and low-back pain: socioeconomic factors and consequences. J Bone Joint Surg Am 88 (Suppl 2): 21-24.
    • (2006) J Bone Joint Surg Am , vol.88 , Issue.SUPPL. 2 , pp. 21-24
    • Katz, J.N.1
  • 4
    • 0029564343 scopus 로고
    • Degeneration and aging affect the tensile behavior of human lumbar annulus fibrosus
    • Acaroglu ER, Iatridis JC, Setton LA, et al. 1995. Degeneration and aging affect the tensile behavior of human lumbar annulus fibrosus. Spine 20: 2690-2701.
    • (1995) Spine , vol.20 , pp. 2690-2701
    • Acaroglu, E.R.1    Iatridis, J.C.2    Setton, L.A.3
  • 5
    • 33845764307 scopus 로고    scopus 로고
    • Effects of exogenous crosslinking on in vitro tensile and compressive moduli of lumbar intervertebral discs
    • Chuang SY, Odono RM, Hedman TP,. 2007. Effects of exogenous crosslinking on in vitro tensile and compressive moduli of lumbar intervertebral discs. Clin Biomech 22: 14-20.
    • (2007) Clin Biomech , vol.22 , pp. 14-20
    • Chuang, S.Y.1    Odono, R.M.2    Hedman, T.P.3
  • 6
    • 78751570861 scopus 로고    scopus 로고
    • Optimization of protein crosslinking formulations for the treatment of degenerative disc disease
    • in press
    • Slusarewicz P, Zhu K, Kirking B, et al. 2010. Optimization of protein crosslinking formulations for the treatment of degenerative disc disease. Spine (in press).
    • (2010) Spine
    • Slusarewicz, P.1    Zhu, K.2    Kirking, B.3
  • 7
    • 33745697990 scopus 로고    scopus 로고
    • Exogenous cross-linking increases the stability of spinal motion segments
    • Hedman TP, Saito H, Vo C, et al. 2006. Exogenous cross-linking increases the stability of spinal motion segments. Spine 31: 480-485.
    • (2006) Spine , vol.31 , pp. 480-485
    • Hedman, T.P.1    Saito, H.2    Vo, C.3
  • 8
    • 0026510322 scopus 로고
    • Tissue regeneration by use of collagen-glycosaminoglycan copolymers
    • Yannas IV,. 1992. Tissue regeneration by use of collagen- glycosaminoglycan copolymers. Clin Mater 9: 179-187.
    • (1992) Clin Mater , vol.9 , pp. 179-187
    • Yannas, I.V.1
  • 11
    • 0032970552 scopus 로고    scopus 로고
    • Reconstructed human cornea produced in vitro by tissue engineering
    • Germain L, Auger FA, Grandbois E, et al. 1999. Reconstructed human cornea produced in vitro by tissue engineering. Pathobiology 67: 140-147.
    • (1999) Pathobiology , vol.67 , pp. 140-147
    • Germain, L.1    Auger, F.A.2    Grandbois, E.3
  • 12
    • 0024095910 scopus 로고
    • Structure of a collagen-GAG dermal skin substitute optimized for cultured human epidermal keratinocytes
    • Boyce ST, Christianson DJ, Hansbrough JF,. 1988. Structure of a collagen-GAG dermal skin substitute optimized for cultured human epidermal keratinocytes. J Biomed Mater Res 22: 939-957.
    • (1988) J Biomed Mater Res , vol.22 , pp. 939-957
    • Boyce, S.T.1    Christianson, D.J.2    Hansbrough, J.F.3
  • 13
    • 0030130294 scopus 로고    scopus 로고
    • Evaluation of different chemical methods for crosslinking collagen gel, films and sponges
    • Rault I, Frei V, Herbage DA-M, et al. 1996. Evaluation of different chemical methods for crosslinking collagen gel, films and sponges. J Mater Sci Mater Med 7: 221.
    • (1996) J Mater Sci Mater Med , vol.7 , pp. 221
    • Rault, I.1    Frei, V.2    Herbage, D.-M.3
  • 14
    • 0028372260 scopus 로고
    • Use of diphenylphosphorylazide for cross-linking collagen-based biomaterials
    • Petite H, Frei V, Huc A, et al. 1994. Use of diphenylphosphorylazide for cross-linking collagen-based biomaterials. J Biomed Mater Res 28: 159-165.
    • (1994) J Biomed Mater Res , vol.28 , pp. 159-165
    • Petite, H.1    Frei, V.2    Huc, A.3
  • 15
    • 0035877405 scopus 로고    scopus 로고
    • Stability of a biological tissue fixed with a naturally occurring crosslinking agent (genipin)
    • Sung HW, Liang IL, Chen CN, et al. 2001. Stability of a biological tissue fixed with a naturally occurring crosslinking agent (genipin). J Biomed Mater Res 55: 538-546.
    • (2001) J Biomed Mater Res , vol.55 , pp. 538-546
    • Sung, H.W.1    Liang, I.L.2    Chen, C.N.3
  • 16
    • 0041922601 scopus 로고    scopus 로고
    • Proanthocyanidin: A natural crosslinking reagent for stabilizing collagen matrices
    • Han B, Jaurequi J, Tang BW, et al. 2003. Proanthocyanidin: a natural crosslinking reagent for stabilizing collagen matrices. J Biomed Mater Res A 65: 118-124.
    • (2003) J Biomed Mater Res A , vol.65 , pp. 118-124
    • Han, B.1    Jaurequi, J.2    Tang, B.W.3
  • 17
    • 67649134960 scopus 로고    scopus 로고
    • Glutaraldehyde and oxidised dextran as crosslinker reagents for chitosan-based scaffolds for cartilage tissue engineering
    • Hoffmann B, Seitz D, Mencke A, et al. 2009. Glutaraldehyde and oxidised dextran as crosslinker reagents for chitosan-based scaffolds for cartilage tissue engineering. J Mater Sci Mater Med 20: 1495-1503.
    • (2009) J Mater Sci Mater Med , vol.20 , pp. 1495-1503
    • Hoffmann, B.1    Seitz, D.2    Mencke, A.3
  • 18
    • 77951258677 scopus 로고    scopus 로고
    • Kinetic characterization and comparison of various protein crosslinking reagents for matrix modification
    • Slusarewicz P, Zhu K, Hedman TP,. 2010. Kinetic characterization and comparison of various protein crosslinking reagents for matrix modification. J Mater Sci Mater Med. 21: 1175-1181.
    • (2010) J Mater Sci Mater Med. , vol.21 , pp. 1175-1181
    • Slusarewicz, P.1    Zhu, K.2    Hedman, T.P.3
  • 19
    • 0019536461 scopus 로고
    • Effect of electrical stimulation on thermal shrinkage temperature of bovine muscle collagen
    • Judge MD, Reeves ES, Aberle ED,. 1981. Effect of electrical stimulation on thermal shrinkage temperature of bovine muscle collagen. J Anim Sci 52: 530-534.
    • (1981) J Anim Sci , vol.52 , pp. 530-534
    • Judge, M.D.1    Reeves, E.S.2    Aberle, E.D.3
  • 20
    • 0002387196 scopus 로고
    • Effects of chronological age and postmortem aging on thermal shrinkage temperature of bovine intramuscular collagen
    • Judge MD, Aberle ED,. 1982. Effects of chronological age and postmortem aging on thermal shrinkage temperature of bovine intramuscular collagen. J Anim Sci 54: 68-71.
    • (1982) J Anim Sci , vol.54 , pp. 68-71
    • Judge, M.D.1    Aberle, E.D.2
  • 21
    • 0024802202 scopus 로고
    • Effect of collagen crosslinking on collagen-water interactions (a DSC investigation)
    • Kopp J, Bonnet M, Renou JP,. 1989. Effect of collagen crosslinking on collagen-water interactions (a DSC investigation). Matrix 9: 443-450.
    • (1989) Matrix , vol.9 , pp. 443-450
    • Kopp, J.1    Bonnet, M.2    Renou, J.P.3
  • 22
    • 1642369882 scopus 로고    scopus 로고
    • Studies of the collagen-like peptide (Pro-Pro-Gly)(10) confirm that the shape and position of the type i collagen denaturation endotherm is governed by the rate of helix unfolding
    • Miles CA, Bailey AJ,. 2004. Studies of the collagen-like peptide (Pro-Pro-Gly)(10) confirm that the shape and position of the type I collagen denaturation endotherm is governed by the rate of helix unfolding. J Mol Biol 337: 917-931.
    • (2004) J Mol Biol , vol.337 , pp. 917-931
    • Miles, C.A.1    Bailey, A.J.2
  • 23
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • Miles CA, Burjanadze TV, Bailey AJ,. 1995. The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry. J Mol Biol 245: 437-446.
    • (1995) J Mol Biol , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 24
    • 0033029015 scopus 로고    scopus 로고
    • Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers
    • Miles CA, Ghelashvili M,. 1999. Polymer-in-a-box mechanism for the thermal stabilization of collagen molecules in fibers. Biophys J 76: 3243-3252.
    • (1999) Biophys J , vol.76 , pp. 3243-3252
    • Miles, C.A.1    Ghelashvili, M.2
  • 25
    • 0035122037 scopus 로고    scopus 로고
    • Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking
    • Bigi A, Cojazzi G, Panzavolta S, et al. 2001. Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking. Biomaterials 22: 763-768.
    • (2001) Biomaterials , vol.22 , pp. 763-768
    • Bigi, A.1    Cojazzi, G.2    Panzavolta, S.3
  • 26
    • 0030046726 scopus 로고    scopus 로고
    • Thermal stabilization of collagen fibers by calcification
    • Kronick PL, Cooke P,. 1996. Thermal stabilization of collagen fibers by calcification. Connect Tissue Res 33: 275-282.
    • (1996) Connect Tissue Res , vol.33 , pp. 275-282
    • Kronick, P.L.1    Cooke, P.2
  • 27
    • 0037290598 scopus 로고    scopus 로고
    • Influence of different crosslinking treatments on the physical properties of collagen membranes
    • Charulatha V, Rajaram A,. 2003. Influence of different crosslinking treatments on the physical properties of collagen membranes. Biomaterials 24: 759-767.
    • (2003) Biomaterials , vol.24 , pp. 759-767
    • Charulatha, V.1    Rajaram, A.2
  • 29
    • 0028036133 scopus 로고
    • Oligomeric and polymeric procyanidins from grape seeds
    • Prieur C, Rigaud J, Cheynier V, et al. 1994. Oligomeric and polymeric procyanidins from grape seeds. Phytochemistry 26: 781-784.
    • (1994) Phytochemistry , vol.26 , pp. 781-784
    • Prieur, C.1    Rigaud, J.2    Cheynier, V.3
  • 30
    • 0029008944 scopus 로고
    • Aging and degeneration of the human intervertebral disc
    • Buckwalter JA,. 1995. Aging and degeneration of the human intervertebral disc. Spine 20: 1307-1314.
    • (1995) Spine , vol.20 , pp. 1307-1314
    • Buckwalter, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.