메뉴 건너뛰기




Volumn 30, Issue 4, 2009, Pages 431-435

In situ polymerization of tropoelastin in the absence of chemical cross-linking

Author keywords

Biomimetic material; Elasticity; Elastin; Extracellular matrix; Hydrogel; Self assembly

Indexed keywords

ABS RESINS; ANIMAL CELL CULTURE; BIOLOGICAL MATERIALS; BIOMATERIALS; BIOMIMETICS; CELL CULTURE; CELL MEMBRANES; COAGULATION; CROSSLINKING; ELASTICITY; GELATION; GLYCOPROTEINS; HYDROGELS; MICROSCOPIC EXAMINATION; MONOMERS; POLYMERS; SPHERES; TISSUE;

EID: 56449098375     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2008.10.018     Document Type: Article
Times cited : (73)

References (28)
  • 2
    • 33751434981 scopus 로고    scopus 로고
    • Stimulus responsive elastin biopolymers: applications in medicine and biotechnology
    • Chilkoti A., Christensen T., and MacKay J.A. Stimulus responsive elastin biopolymers: applications in medicine and biotechnology. Curr Opin Chem Biol 10 (2006) 652-657
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 652-657
    • Chilkoti, A.1    Christensen, T.2    MacKay, J.A.3
  • 3
    • 0034894236 scopus 로고    scopus 로고
    • Elastomeric polypentapeptides cross-linked into matrixes and fibers
    • Lee J., Macosko C.W., and Urry D.W. Elastomeric polypentapeptides cross-linked into matrixes and fibers. Biomacromolecules 2 (2001) 170-179
    • (2001) Biomacromolecules , vol.2 , pp. 170-179
    • Lee, J.1    Macosko, C.W.2    Urry, D.W.3
  • 4
    • 0346850628 scopus 로고    scopus 로고
    • Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties
    • Bellingham C.M., Lillie M.A., Gosline J.M., Wright G.M., Starcher B.C., Bailey A.J., et al. Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties. Biopolymers 70 (2003) 445-455
    • (2003) Biopolymers , vol.70 , pp. 445-455
    • Bellingham, C.M.1    Lillie, M.A.2    Gosline, J.M.3    Wright, G.M.4    Starcher, B.C.5    Bailey, A.J.6
  • 5
    • 1942468636 scopus 로고    scopus 로고
    • Synthetic elastin hydrogels derived from massive elastic assemblies of self-organized human protein monomers
    • Mithieux S.M., Rasko J.E., and Weiss A.S. Synthetic elastin hydrogels derived from massive elastic assemblies of self-organized human protein monomers. Biomaterials 25 (2004) 4921-4927
    • (2004) Biomaterials , vol.25 , pp. 4921-4927
    • Mithieux, S.M.1    Rasko, J.E.2    Weiss, A.S.3
  • 6
    • 40749109022 scopus 로고    scopus 로고
    • A biomaterial composed of collagen and solubilized elastin enhances angiogenesis and elastic fiber formation without calcification
    • Daamen W.F., Nillesen S.T., Wismans R.G., Reinhardt D.P., Hafmans T., Veerkamp J.H., et al. A biomaterial composed of collagen and solubilized elastin enhances angiogenesis and elastic fiber formation without calcification. Tissue Eng Part A 14 (2008) 349-360
    • (2008) Tissue Eng Part A , vol.14 , pp. 349-360
    • Daamen, W.F.1    Nillesen, S.T.2    Wismans, R.G.3    Reinhardt, D.P.4    Hafmans, T.5    Veerkamp, J.H.6
  • 7
    • 0034158145 scopus 로고    scopus 로고
    • Engineering the extracellular matrix: a novel approach to polymeric biomaterials. I. Control of the physical properties of artificial protein matrices designed to support adhesion of vascular endothelial cells
    • Welsh E.R., and Tirrell D.A. Engineering the extracellular matrix: a novel approach to polymeric biomaterials. I. Control of the physical properties of artificial protein matrices designed to support adhesion of vascular endothelial cells. Biomacromolecules 1 (2000) 23-30
    • (2000) Biomacromolecules , vol.1 , pp. 23-30
    • Welsh, E.R.1    Tirrell, D.A.2
  • 8
    • 33847286372 scopus 로고    scopus 로고
    • Microstructural and tensile properties of elastin-based polypeptides crosslinked with genipin and pyrroloquinoline quinone
    • Vieth S., Bellingham C.M., Keeley F.W., Hodge S.M., and Rousseau D. Microstructural and tensile properties of elastin-based polypeptides crosslinked with genipin and pyrroloquinoline quinone. Biopolymers 85 (2007) 199-206
    • (2007) Biopolymers , vol.85 , pp. 199-206
    • Vieth, S.1    Bellingham, C.M.2    Keeley, F.W.3    Hodge, S.M.4    Rousseau, D.5
  • 10
    • 0014024636 scopus 로고
    • Inhibition of the biosynthesis of the cross-links in elastin by a lathyrogen
    • O'Dell B.L., Elsden D.F., Thomas J., Partridge S.M., Smith R.H., and Palmer R. Inhibition of the biosynthesis of the cross-links in elastin by a lathyrogen. Nature 209 (1966) 401-402
    • (1966) Nature , vol.209 , pp. 401-402
    • O'Dell, B.L.1    Elsden, D.F.2    Thomas, J.3    Partridge, S.M.4    Smith, R.H.5    Palmer, R.6
  • 11
    • 0014940673 scopus 로고
    • Cross-linking of collagen and elastin. Properties of lysyl oxidase
    • Siegel R.C., Pinnell S.R., and Martin G.R. Cross-linking of collagen and elastin. Properties of lysyl oxidase. Biochemistry 9 (1970) 4486-4492
    • (1970) Biochemistry , vol.9 , pp. 4486-4492
    • Siegel, R.C.1    Pinnell, S.R.2    Martin, G.R.3
  • 12
    • 0021717224 scopus 로고
    • Elastin: relation of protein and gene structure to disease
    • Rosenbloom J. Elastin: relation of protein and gene structure to disease. Lab Invest 51 (1984) 605-623
    • (1984) Lab Invest , vol.51 , pp. 605-623
    • Rosenbloom, J.1
  • 13
    • 33747510080 scopus 로고    scopus 로고
    • Tropoelastin massively associates during coacervation to form quantized protein spheres
    • Clarke A.W., Arnspang E.C., Mithieux S.M., Korkmaz E., Braet F., and Weiss A.S. Tropoelastin massively associates during coacervation to form quantized protein spheres. Biochemistry 45 (2006) 9989-9996
    • (2006) Biochemistry , vol.45 , pp. 9989-9996
    • Clarke, A.W.1    Arnspang, E.C.2    Mithieux, S.M.3    Korkmaz, E.4    Braet, F.5    Weiss, A.S.6
  • 14
    • 36248980380 scopus 로고    scopus 로고
    • Self-assembled elastin-like polypeptide particles
    • Osborne J.L., Farmer R., and Woodhouse K.A. Self-assembled elastin-like polypeptide particles. Acta Biomater 4 (2008) 49-57
    • (2008) Acta Biomater , vol.4 , pp. 49-57
    • Osborne, J.L.1    Farmer, R.2    Woodhouse, K.A.3
  • 15
    • 33644893402 scopus 로고    scopus 로고
    • Elastic fiber formation: a dynamic view of extracellular matrix assembly using timer reporters
    • Kozel B.A., Rongish B.J., Czirok A., Zach J., Little C.D., Davis E.C., et al. Elastic fiber formation: a dynamic view of extracellular matrix assembly using timer reporters. J Cell Physiol 207 (2006) 87-96
    • (2006) J Cell Physiol , vol.207 , pp. 87-96
    • Kozel, B.A.1    Rongish, B.J.2    Czirok, A.3    Zach, J.4    Little, C.D.5    Davis, E.C.6
  • 16
    • 0033618373 scopus 로고    scopus 로고
    • Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains
    • Wu W.J., Vrhovski B., and Weiss A.S. Glycosaminoglycans mediate the coacervation of human tropoelastin through dominant charge interactions involving lysine side chains. J Biol Chem 274 (1999) 21719-21724
    • (1999) J Biol Chem , vol.274 , pp. 21719-21724
    • Wu, W.J.1    Vrhovski, B.2    Weiss, A.S.3
  • 17
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287 (2000) 252-260
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 18
    • 0030984753 scopus 로고    scopus 로고
    • Drying cells for SEM, AFM and TEM by hexamethyldisilazane: a study on hepatic endothelial cells
    • Braet F., De Zanger R., and Wisse E. Drying cells for SEM, AFM and TEM by hexamethyldisilazane: a study on hepatic endothelial cells. J Microsc 186 (1997) 84-87
    • (1997) J Microsc , vol.186 , pp. 84-87
    • Braet, F.1    De Zanger, R.2    Wisse, E.3
  • 19
    • 0030809954 scopus 로고    scopus 로고
    • Coacervation characteristics of recombinant human tropoelastin
    • Vrhovski B., Jensen S., and Weiss A.S. Coacervation characteristics of recombinant human tropoelastin. Eur J Biochem 250 (1997) 92-98
    • (1997) Eur J Biochem , vol.250 , pp. 92-98
    • Vrhovski, B.1    Jensen, S.2    Weiss, A.S.3
  • 20
    • 48449091794 scopus 로고    scopus 로고
    • Glycosaminoglycan-mediated coacervation of tropoelastin abolishes the critical concentration, accelerates coacervate formation, and facilitates spherule fusion: implications for tropoelastin microassembly
    • Tu Y., and Weiss A.S. Glycosaminoglycan-mediated coacervation of tropoelastin abolishes the critical concentration, accelerates coacervate formation, and facilitates spherule fusion: implications for tropoelastin microassembly. Biomacromolecules (2008)
    • (2008) Biomacromolecules
    • Tu, Y.1    Weiss, A.S.2
  • 21
    • 48249142845 scopus 로고    scopus 로고
    • Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus
    • Choi J.M., Hutson A.M., Estes M.K., and Prasad B.V. Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc Natl Acad Sci U S A 105 (2008) 9175-9180
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9175-9180
    • Choi, J.M.1    Hutson, A.M.2    Estes, M.K.3    Prasad, B.V.4
  • 22
    • 0032533711 scopus 로고    scopus 로고
    • Biochemistry of tropoelastin
    • Vrhovski B., and Weiss A.S. Biochemistry of tropoelastin. Eur J Biochem 258 (1998) 1-18
    • (1998) Eur J Biochem , vol.258 , pp. 1-18
    • Vrhovski, B.1    Weiss, A.S.2
  • 23
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma K., Kan L., and Wang K. Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. Biochemistry 40 (2001) 3427-3438
    • (2001) Biochemistry , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.2    Wang, K.3
  • 24
    • 36649020438 scopus 로고    scopus 로고
    • Investigating the amyloidogenic nanostructured sequences of elastin: sequence encoded by exon 28 of human tropoelastin gene
    • Bochicchio B., Pepe A., Flamia R., Lorusso M., and Tamburro A.M. Investigating the amyloidogenic nanostructured sequences of elastin: sequence encoded by exon 28 of human tropoelastin gene. Biomacromolecules 8 (2007) 3478-3486
    • (2007) Biomacromolecules , vol.8 , pp. 3478-3486
    • Bochicchio, B.1    Pepe, A.2    Flamia, R.3    Lorusso, M.4    Tamburro, A.M.5
  • 26
    • 0023926557 scopus 로고
    • Differentiating cardiac elastin, collagen and microfibrils with NaOH at the ultrastructural level
    • Dickson C.P., and Robinson T.F. Differentiating cardiac elastin, collagen and microfibrils with NaOH at the ultrastructural level. Histochemistry 89 (1988) 105-107
    • (1988) Histochemistry , vol.89 , pp. 105-107
    • Dickson, C.P.1    Robinson, T.F.2
  • 27
    • 0028030922 scopus 로고
    • Effects of a positively charged biomaterial for dermal and subcutaneous augmentation
    • Eppley B.L., Summerlin D.J., Prevel C.D., and Sadove A.M. Effects of a positively charged biomaterial for dermal and subcutaneous augmentation. Aesthetic Plast Surg 18 (1994) 413-416
    • (1994) Aesthetic Plast Surg , vol.18 , pp. 413-416
    • Eppley, B.L.1    Summerlin, D.J.2    Prevel, C.D.3    Sadove, A.M.4
  • 28
    • 1642389398 scopus 로고    scopus 로고
    • Human histology and persistence of various injectable filler substances for soft tissue augmentation
    • [discussion 367]
    • Lemperle G., Morhenn V., and Charrier U. Human histology and persistence of various injectable filler substances for soft tissue augmentation. Aesthetic Plast Surg 27 (2003) 354-366 [discussion 367]
    • (2003) Aesthetic Plast Surg , vol.27 , pp. 354-366
    • Lemperle, G.1    Morhenn, V.2    Charrier, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.