메뉴 건너뛰기




Volumn 16, Issue 5, 2010, Pages 895-903

Characterization of biocompatible collagen fibers-a promising candidate for cardiac patch

Author keywords

[No Author keywords available]

Indexed keywords

BIOMECHANICS; FIBERS; HEART; MECHANICAL PROPERTIES; STRAIN; STRESS-STRAIN CURVES; STRESSES; TENSILE STRENGTH; TISSUE ENGINEERING; TRANSMISSION ELECTRON MICROSCOPY; WEAVING;

EID: 77957377863     PISSN: 19373384     EISSN: 19373392     Source Type: Journal    
DOI: 10.1089/ten.tec.2009.0475     Document Type: Article
Times cited : (18)

References (44)
  • 1
    • 0348088612 scopus 로고
    • The flexibility of the collagen compartment of muscle
    • McCormick, R. The flexibility of the collagen compartment of muscle. Meat Sci 36, 79, 1994.
    • (1994) Meat Sci , vol.36 , pp. 79
    • McCormick, R.1
  • 2
    • 0020409091 scopus 로고
    • Characterization of intramuscular collagen in the mammalian left ventricle
    • Medugorac, I. Characterization of intramuscular collagen in the mammalian left ventricle. Basic Res Cordiol 77, 589, 1982.
    • (1982) Basic Res Cordiol , vol.77 , pp. 589
    • Medugorac, I.1
  • 3
    • 0031960548 scopus 로고    scopus 로고
    • Collagen\biomaterial for drug delivery
    • Wolfgang, F. Collagen\biomaterial for drug delivery. Eur J Pharm Biopharm 45, 113, 1998.
    • (1998) Eur J Pharm Biopharm , vol.45 , pp. 113
    • Wolfgang, F.1
  • 4
    • 33646714443 scopus 로고    scopus 로고
    • Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy
    • David, A., Carlos, H., Clemens, M.F., and Daniel, J.M. Observing growth steps of collagen self-assembly by time-lapse high-resolution atomic force microscopy. J Struct Biol 154, 232, 2006.
    • (2006) J Struct Biol , vol.154 , pp. 232
    • David, A.1    Carlos, H.2    Clemens, M.F.3    Daniel, J.M.4
  • 5
    • 77957349318 scopus 로고
    • Injectable crosslinked collagen implant material
    • U.S. Patent No. 4,582,640
    • Smestad, T., McPherson, J., and Wallace, D. Injectable crosslinked collagen implant material. U.S. Patent No. 4,582,640, 1984.
    • (1984)
    • Smestad, T.1    McPherson, J.2    Wallace, D.3
  • 6
    • 0342667417 scopus 로고
    • Collagen compositions and methods for preparation thereof
    • U.S. Patent No. 5,106,949
    • Kemp, P., Falco, L., Regan, K., and Bell, E. Collagen compositions and methods for preparation thereof. U.S. Patent No. 5,106,949, 1992.
    • (1992)
    • Kemp, P.1    Falco, L.2    Regan, K.3    Bell, E.4
  • 7
    • 0022929670 scopus 로고
    • The influence of specimen length on the tensile failure properties of tendon collagen
    • Roger, H.C. The influence of specimen length on the tensile failure properties of tendon collagen. J Biomech 19, 951, 1986.
    • (1986) J Biomech , vol.19 , pp. 951
    • Roger, H.C.1
  • 8
    • 0025109152 scopus 로고
    • In vivo evaluation and comparison of collagen, acetylated collagen and collagen=glycosaminoglycan composite films and sponges as candidate biomaterials
    • Srivastava, S., Gorham, S., French, D., Shivas, A., and Courtney, J. In vivo evaluation and comparison of collagen, acetylated collagen and collagen=glycosaminoglycan composite films and sponges as candidate biomaterials. Biomaterials 11, 155, 1990.
    • (1990) Biomaterials , vol.11 , pp. 155
    • Srivastava, S.1    Gorham, S.2    French, D.3    Shivas, A.4    Courtney, J.5
  • 9
    • 77957370865 scopus 로고
    • Chemicallymodified fiber collagen hemostatic agents
    • U.S. Patent No. 4
    • Miyata, T.,Rubin,A., and Stenzel,K. Chemicallymodified fiber collagen hemostatic agents. U.S. Patent No. 4,271,070, 1981.
    • (1981) , vol.271 , pp. 070
    • Miyata Rubin, T.A.1    Stenzel, K.2
  • 11
    • 67349248605 scopus 로고    scopus 로고
    • Extraction techniques for the decellularization of tissue engineered articular cartilage constructs
    • Elder, B.D., Eleswarapu, E.V., and Athanasiou, K.A. Extraction techniques for the decellularization of tissue engineered articular cartilage constructs. Biomaterials 30, 3749, 2009.
    • (2009) Biomaterials , vol.30 , pp. 3749
    • Elder, B.D.1    Eleswarapu, E.V.2    Athanasiou, K.A.3
  • 12
    • 23644440674 scopus 로고    scopus 로고
    • Effectiveness of three extraction techniques in the development of a decellularized bone-anterior cruciate ligament-bone graft
    • Woods, T., and Gratzer, P.F. Effectiveness of three extraction techniques in the development of a decellularized bone-anterior cruciate ligament-bone graft. Biomaterials 26, 7339, 2005.
    • (2005) Biomaterials , vol.26 , pp. 7339
    • Woods, T.1    Gratzer, P.F.2
  • 15
    • 33846463396 scopus 로고    scopus 로고
    • Purification, and refolding of recombinant collagen a1(XI) amino terminal domain splice variants
    • Warner, L.R., Blasick, C.M., Brown, R.J., and Oxford, J.T. Expression, purification, and refolding of recombinant collagen a1(XI) amino terminal domain splice variants. Protein Expr Purif 52, 403, 2007.
    • (2007) Protein Expr Purif , vol.52 , pp. 403
    • Warner, L.R.1    Blasick, C.M.2    Brown, R.J.3    Expression, T.O.J.4
  • 17
    • 0027012910 scopus 로고
    • The maceration technique in scanning electron microscopy of collagen fiber frameworks: Its application in the study of human livers
    • Ohtani, O. The maceration technique in scanning electron microscopy of collagen fiber frameworks: its application in the study of human livers. Arch Histol Cytol 55, 225, 1992.
    • (1992) Arch Histol Cytol , vol.55 , pp. 225
    • Ohtani, O.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, V. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680, 1970.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, V.1
  • 19
    • 76549246681 scopus 로고
    • The determination of hydroxyproline
    • Neuman, R.E., and Logan, M. The determination of hydroxyproline. J Biol Chem 184, 299, 1950.
    • (1950) J Biol Chem , vol.184 , pp. 299
    • Neuman, R.E.1    Logan, M.2
  • 20
    • 3442876655 scopus 로고    scopus 로고
    • Senthil kumar, M., and Sehgal, P.K. Improved collagen bilayer dressing for the controlled release of drugs
    • Sripriya, R., Senthil kumar, M., and Sehgal, P.K. Improved collagen bilayer dressing for the controlled release of drugs. J Biomed Mater Res B 70, 389, 2004.
    • (2004) J Biomed Mater Res B , vol.70 , pp. 389
    • Sripriya, R.1
  • 21
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mossman, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65, 55, 1983.
    • (1983) J Immunol Methods , vol.65 , pp. 55
    • Mossman, T.1
  • 23
    • 33947120660 scopus 로고    scopus 로고
    • Collagen bilayer dressing with ciprofloxacin, an effective system for infected wound healing
    • Sripriya, M., SenthilKumar, M., RafiuddinAhmed, M., and Sehgal, P.K. Collagen bilayer dressing with ciprofloxacin, an effective system for infected wound healing. J Biomater Sci Polym Ed 18, 335, 2007.
    • (2007) J Biomater Sci Polym Ed , vol.18 , pp. 335
    • Sripriya, M.1    Senthilkumar, M.2    Rafiuddinahmed, M.3    Sehgal, P.K.4
  • 24
    • 0032502265 scopus 로고    scopus 로고
    • Connective tissue skeleton of the human heart
    • Rossi, M., Abreu, M., and Santoro, L. Connective tissue skeleton of the human heart. Circulation 97, 934, 1998.
    • (1998) Circulation , vol.97 , pp. 934
    • Rossi, M.1    Abreu, M.2    Santoro, L.3
  • 25
    • 0030657676 scopus 로고    scopus 로고
    • Extracellular matrix remodeling in heart failure. A role for de novo angiotensin II generation
    • Weber, K. Extracellular matrix remodeling in heart failure. A role for de novo angiotensin II generation. Circulation 96, 4065, 1997.
    • (1997) Circulation , vol.96 , pp. 4065
    • Weber, K.1
  • 26
    • 20344375233 scopus 로고    scopus 로고
    • Tissue engineering of heart valves: Decellularized porcine and human valve scaffolds differ importantly in residual potential to attract monocytic cells
    • Erwin, R., Gernot, S., Marie-Theres, K., Eva, E., Birgitta, W., Barbara, D., Ernst, W., Paul, S., and Guenter, W. Tissue engineering of heart valves: decellularized porcine and human valve scaffolds differ importantly in residual potential to attract monocytic cells. Circulation 111, 2792, 2005.
    • (2005) Circulation , vol.111 , pp. 2792
    • Erwin, R.1    Gernot, S.2    Marie-Theres, K.3    Eva, E.4    Birgitta, W.5    Barbara, D.6    Ernst, W.7    Paul, S.8    Guenter, W.9
  • 27
    • 1942542453 scopus 로고    scopus 로고
    • Novel porous aortic elastin and collagen scaffolds for tissue engineering
    • Qijin, L., Kavitha, G., Dan, T.S., and Narendra R.V. Novel porous aortic elastin and collagen scaffolds for tissue engineering. Biomaterials 25, 5227, 2004.
    • (2004) Biomaterials , vol.25 , pp. 5227
    • Qijin, L.1    Kavitha, G.2    Dan, T.S.3    Narendra, R.V.4
  • 29
    • 66149083270 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy investigation of native tissue matrix modifications using a gamma irradiation process
    • Neha, B.S., Willem, F.W., Michael, M., Wendell, Q.S., and John, C.B. Fourier transform infrared spectroscopy investigation of native tissue matrix modifications using a gamma irradiation process. Tissue Eng C 15, 33, 2009.
    • (2009) Tissue Eng C , vol.15 , pp. 33
    • Neha, B.S.1    Willem, F.W.2    Michael, M.3    Wendell, Q.S.4    John, C.B.5
  • 30
    • 33846463396 scopus 로고    scopus 로고
    • Purification, and refolding of recombinant collagen-1(XI) amino terminal domain splice variants
    • Lisa, R.W., Christina, M.B., Raquel, J.B., and Julia, T.O. Expression, purification, and refolding of recombinant collagen-1(XI) amino terminal domain splice variants. Protein Expr Purif 52, 403, 2007.
    • (2007) Protein Expr Purif , vol.52 , pp. 403
    • Lisa, R.W.1    Christina, M.B.2    Raquel, J.B.3    Expression, O.J.T.4
  • 31
    • 0033850537 scopus 로고    scopus 로고
    • Expression of recombinant human type I-III collagens in the yeast Pichia pastoris
    • Myllyharju, J., Nokelainen, M., Vuorela, A., and Kivirikk, K.I. Expression of recombinant human type I-III collagens in the yeast Pichia pastoris. Biochem Soc Trans 28, 353, 2000
    • (2000) Biochem Soc Trans , vol.28 , pp. 353
    • Myllyharju, J.1    Nokelainen, M.2    Vuorela, A.3    Kivirikk, K.I.4
  • 33
    • 0002890851 scopus 로고
    • Structural investigations on poly (4-hydroxy-L-proline)-II- physicochemical and X-ray studies
    • Brahmachari, S.K., Bansal, M., Ananthanaryanan, V., and Sasisekharan, V. Structural investigations on poly (4-hydroxy-L-proline)-II-physicochemical and X-ray studies. Macromolecules 12, 23, 1978.
    • (1978) Macromolecules , vol.12 , pp. 23
    • Brahmachari, S.K.1    Bansal, M.2    Ananthanaryanan, V.3    Sasisekharan, V.4
  • 34
    • 0035013286 scopus 로고    scopus 로고
    • Contribution of tertiary amides to the conformational stability of collagen triple helices
    • Kersteen, A., and Raines, T. Contribution of tertiary amides to the conformational stability of collagen triple helices. Biopolymers 59, 24, 2001.
    • (2001) Biopolymers , vol.59 , pp. 24
    • Kersteen, A.1    Raines, T.2
  • 36
    • 0007422593 scopus 로고
    • Effect of strain rate on the fracture behaviour of collagen
    • Arumugam, V., Naresh, M.D., Somanathan, N., and Sanjeevi, R. Effect of strain rate on the fracture behaviour of collagen. J Mat Sci 27, 2649, 1992.
    • (1992) J Mat Sci , vol.27 , pp. 2649
    • Arumugam, V.1    Naresh, M.D.2    Somanathan, N.3    Sanjeevi, R.4
  • 37
    • 0026045037 scopus 로고
    • The vascularity of the rotator cuff
    • Chansky, H.A., and Innotti, I.P. The vascularity of the rotator cuff. Clin Sports Med 10, 807, 1991.
    • (1991) Clin Sports Med , vol.10 , pp. 807
    • Chansky, H.A.1    Innotti, I.P.2
  • 38
    • 0002773858 scopus 로고
    • Electron microscopy of the collagen fibril
    • Motta, P.M., and Ruggeri, A., eds Boston, MA: Kluwer Academic
    • Chapman, J.A., and Hulmes, D.J.S. Electron microscopy of the collagen fibril. In: Motta, P.M., and Ruggeri, A., eds. Ultrastructure of the Connective Tissue Matrix. Boston, MA: Kluwer Academic, 1984, pp. 1-33.
    • (1984) Ultrastructure of the Connective Tissue Matrix , pp. 1-33
    • Chapman, J.A.1    Hulmes, D.J.S.2
  • 39
    • 0002017332 scopus 로고
    • Electron microscopy investigations of the structure of collagens
    • Schmitt, F., Hall, C.E., and Janks, M.A. Electron microscopy investigations of the structure of collagens. J Cell Comp Physiol 20, 11, 1942.
    • (1942) J Cell Comp Physiol , vol.20 , pp. 11
    • Schmitt, F.1    Hall, C.E.2    Janks, M.A.3
  • 40
    • 0018568324 scopus 로고
    • Type i collagen fibrillogenesis: Initiation via reversible linear and lateral growth steps
    • Silver, F.H., Langley, K.H., and Trelstad, R.L. Type I collagen fibrillogenesis: initiation via reversible linear and lateral growth steps. Biopolymers 18, 2523, 1979.
    • (1979) Biopolymers , vol.18 , pp. 2523
    • Silver, F.H.1    Langley, K.H.2    Trelstad, R.L.3
  • 41
    • 0031692465 scopus 로고    scopus 로고
    • The collagen fibril: The almost crystalline structure
    • Prockop, D.J., and Fertala, A. The collagen fibril: the almost crystalline structure. Struct Biol 122, 111, 1998.
    • (1998) Struct Biol , vol.122 , pp. 111
    • Prockop, D.J.1    Fertala, A.2
  • 43
    • 0001113489 scopus 로고
    • A subunit model for the tropocollagen macromolecule
    • Petruska, J.A., and Hodge, A.J. A subunit model for the tropocollagen macromolecule. Proc Natl Acad Sci\USA 51, 871, 1964.
    • (1964) Proc Natl Acad Sci\USA , vol.51 , pp. 871
    • Petruska, J.A.1    Hodge, A.J.2
  • 44
    • 0035218512 scopus 로고    scopus 로고
    • A study of fibrous long spacing collagen ultrastructure and assembly by atomic force microscopy
    • Paige, M.F., Rainey, J.K., and Goh, M.C. A study of fibrous long spacing collagen ultrastructure and assembly by atomic force microscopy. Micron 32, 341, 2001.
    • (2001) Micron , vol.32 , pp. 341
    • Paige, M.F.1    Rainey, J.K.2    Goh, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.