메뉴 건너뛰기




Volumn 3, Issue 2, 2005, Pages 67-82

Tissue heart valve mineralization: Review of calcification mechanisms and strategies for prevention

Author keywords

Bioprostheses; Calcification; Cardiovascular; Crosslinking; Heart valves

Indexed keywords

ALKALINE PHOSPHATASE; AMINO ACID; ANTICOAGULANT AGENT; BISPHOSPHONIC ACID DERIVATIVE; CYANAMIDE; GLUTARALDEHYDE; MATRIX METALLOPROTEINASE; METAL ION; OLEIC ACID;

EID: 28244484330     PISSN: 17226899     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (36)

References (130)
  • 3
    • 0033572873 scopus 로고    scopus 로고
    • Tissue heart valves: Current challenges and future research perspectives
    • Founder's Award, 25th Annual Meeting of the Society for Biomaterials, perspectives. Providence, RI, April 28-May 2, 1999
    • Schoen FJ, Levy RJ. Founder's Award, 25th Annual Meeting of the Society for Biomaterials, perspectives. Providence, RI, April 28-May 2, 1999. Tissue heart valves: current challenges and future research perspectives. J Biomed Mater Res 1999; 47: 439-65.
    • (1999) J Biomed Mater Res , vol.47 , pp. 439-465
    • Schoen, F.J.1    Levy, R.J.2
  • 4
    • 0026478157 scopus 로고
    • Heart valve bioprostheses: Antimineralization
    • Schoen FJ, Levy RJ. Heart valve bioprostheses: antimineralization. Eur J Cardiothorac Surg 1992; 6 (suppl 1): S91-3.
    • (1992) Eur J Cardiothorac Surg , vol.6 , Issue.SUPPL. 1
    • Schoen, F.J.1    Levy, R.J.2
  • 5
    • 0023324430 scopus 로고
    • Cardiac valve prostheses: Review of clinical status and contemporary biomaterials issues
    • Schoen FJ. Cardiac valve prostheses: review of clinical status and contemporary biomaterials issues. J Biomed Mater Res 1987; 21 (suppl): S91-117.
    • (1987) J Biomed Mater Res , vol.21 , Issue.SUPPL.
    • Schoen, F.J.1
  • 6
  • 8
    • 0022553873 scopus 로고
    • Calcification of bovine pericardium used in cardiac valve bioprostheses. Implications for the mechanisms of bioprosthetic tissue mineralization
    • Schoen FJ, Tsao JW, Levy RJ. Calcification of bovine pericardium used in cardiac valve bioprostheses. Implications for the mechanisms of bioprosthetic tissue mineralization. Am J Pathol 1986; 123: 134-45.
    • (1986) Am J Pathol , vol.123 , pp. 134-145
    • Schoen, F.J.1    Tsao, J.W.2    Levy, R.J.3
  • 9
    • 0019670403 scopus 로고
    • Structure and classification of cuspal tears and perforations in porcine bioprosthetic cardiac valves implanted in patients
    • Ishihara T, Ferrans VJ, Boyce SW, Jones M, Roberts WC. Structure and classification of cuspal tears and perforations in porcine bioprosthetic cardiac valves implanted in patients. Am J Cardiol 1981; 48: 665-78.
    • (1981) Am J Cardiol , vol.48 , pp. 665-678
    • Ishihara, T.1    Ferrans, V.J.2    Boyce, S.W.3    Jones, M.4    Roberts, W.C.5
  • 10
    • 0021489009 scopus 로고
    • Toxic reactions evoked by glutaraldehyde-fixed pericardium and cardiac valve tissue bioprosthesis
    • Gendler E, Gendler S, Nimni ME. Toxic reactions evoked by glutaraldehyde-fixed pericardium and cardiac valve tissue bioprosthesis. J Biomed Mater Res 1984; 18: 727-36.
    • (1984) J Biomed Mater Res , vol.18 , pp. 727-736
    • Gendler, E.1    Gendler, S.2    Nimni, M.E.3
  • 12
    • 0031106845 scopus 로고    scopus 로고
    • Differential calcification of cusps and aortic wall failed stented porcine bioprosthetic valves
    • Biedrzycki LM, Lerner E, Levy RJ, Schoen FJ. Differential calcification of cusps and aortic wall failed stented porcine bioprosthetic valves. J Biomed Mater Res 1997; 34: 411-5.
    • (1997) J Biomed Mater Res , vol.34 , pp. 411-415
    • Biedrzycki, L.M.1    Lerner, E.2    Levy, R.J.3    Schoen, F.J.4
  • 13
    • 0030907873 scopus 로고    scopus 로고
    • Increased cellular expression of matrix proteins that regulate mineralization is associated with calcification of native human and porcine xenograft bioprosthetic heart valves
    • Srivatsa SS, Harrity PJ, Maercklein PB, et al. Increased cellular expression of matrix proteins that regulate mineralization is associated with calcification of native human and porcine xenograft bioprosthetic heart valves. J Clin Invest 1997; 99: 996-1009.
    • (1997) J Clin Invest , vol.99 , pp. 996-1009
    • Srivatsa, S.S.1    Harrity, P.J.2    Maercklein, P.B.3
  • 14
    • 0026203845 scopus 로고
    • Initiation of mineralization in bioprosthetic heart valves: Studies of alkaline phosphatase activity and its inhibition by AlC13 or FeCl3 preincubations
    • Levy RJ, Schoen FJ, Flowers WB, Staelin ST. Initiation of mineralization in bioprosthetic heart valves: studies of alkaline phosphatase activity and its inhibition by AlC13 or FeCl3 preincubations. J Biomed Mater Res 1991; 25: 905-35.Gabby
    • (1991) J Biomed Mater Res , vol.25 , pp. 905-935
    • Levy, R.J.1    Schoen, F.J.2    Flowers, W.B.3    Staelin, S.T.4
  • 15
    • 0023883141 scopus 로고
    • Do heart valve bioprostheses degenerate for metabolic or mechanical reasons?
    • Gabbay S, Kadam P, Factor S, Cheung TK. Do heart valve bioprostheses degenerate for metabolic or mechanical reasons? J Thorac Cardiovasc Surg 1988; 95: 208-15.
    • (1988) J Thorac Cardiovasc Surg , vol.95 , pp. 208-215
    • Gabbay, S.1    Kadam, P.2    Factor, S.3    Cheung, T.K.4
  • 16
    • 0025486278 scopus 로고
    • Biochemical changes and cytotoxicity associated with the degradation of polymeric glutaraldehyde derived crosslinks
    • Huang LL, Cheung DT, Nimni ME. Biochemical changes and cytotoxicity associated with the degradation of polymeric glutaraldehyde derived crosslinks. J Biomed Mater Res 1990; 24: 1185-201.
    • (1990) J Biomed Mater Res , vol.24 , pp. 1185-1201
    • Huang, L.L.1    Cheung, D.T.2    Nimni, M.E.3
  • 17
    • 8244241105 scopus 로고    scopus 로고
    • Factors which affect the calcification of tissue-derived bioprostheses
    • Nimni ME, Myers D, Ertl D, Han B. Factors which affect the calcification of tissue-derived bioprostheses. J Biomed Mater Res 1997; 35: 531-7.
    • (1997) J Biomed Mater Res , vol.35 , pp. 531-537
    • Nimni, M.E.1    Myers, D.2    Ertl, D.3    Han, B.4
  • 18
    • 0030111405 scopus 로고    scopus 로고
    • Glutaraldehyde as a fixative in bioprostheses and drug delivery matrices
    • Jayakrishnan A, Jameela SR. Glutaraldehyde as a fixative in bioprostheses and drug delivery matrices. Biomaterials 1996; 17: 471-84.
    • (1996) Biomaterials , vol.17 , pp. 471-484
    • Jayakrishnan, A.1    Jameela, S.R.2
  • 19
    • 0024764134 scopus 로고
    • Toxic effects of aldehydes released from fixed pericardium on bovine aortic endothelial cells
    • Eybl E, Griesmacher A, Grimm M, Wolner E. Toxic effects of aldehydes released from fixed pericardium on bovine aortic endothelial cells. J Biomed Mater Res 1989; 23: 1355-65.
    • (1989) J Biomed Mater Res , vol.23 , pp. 1355-1365
    • Eybl, E.1    Griesmacher, A.2    Grimm, M.3    Wolner, E.4
  • 20
    • 0022609901 scopus 로고
    • Calcification of subcutaneously implanted type I collagen sponges. Effects of formaldehyde and glutaraldehyde pretreatments
    • Levy RJ, Schoen FJ, Sherman FS, Nichols J, Hawley MA, Lund SA. Calcification of subcutaneously implanted type I collagen sponges. Effects of formaldehyde and glutaraldehyde pretreatments. Am J Pathol 1986; 122: 71-82.
    • (1986) Am J Pathol , vol.122 , pp. 71-82
    • Levy, R.J.1    Schoen, F.J.2    Sherman, F.S.3    Nichols, J.4    Hawley, M.A.5    Lund, S.A.6
  • 21
    • 0023184262 scopus 로고
    • The role of glutaraldehyde-induced cross-links in calcification of bovine pericardium used in cardiac valve bioprostheses
    • Golomb G, Schoen FJ, Smith MS, Linden J, Dixon M, Levy RJ. The role of glutaraldehyde-induced cross-links in calcification of bovine pericardium used in cardiac valve bioprostheses. Am J Pathol 1987; 127: 122-30.
    • (1987) Am J Pathol , vol.127 , pp. 122-130
    • Golomb, G.1    Schoen, F.J.2    Smith, M.S.3    Linden, J.4    Dixon, M.5    Levy, R.J.6
  • 22
    • 0348014763 scopus 로고    scopus 로고
    • Isolation of intact aortic valve scaffolds for heart-valve bioprostheses: Extracellular matrix structure, prevention from calcification, and cell repopulation features
    • Spina M, Ortolani F, Messlemani AE, et al. Isolation of intact aortic valve scaffolds for heart-valve bioprostheses: extracellular matrix structure, prevention from calcification, and cell repopulation features. J Biomed Mater Res A 2003; 67: 1338-50.
    • (2003) J Biomed Mater Res A , vol.67 , pp. 1338-1350
    • Spina, M.1    Ortolani, F.2    Messlemani, A.E.3
  • 23
    • 0037086721 scopus 로고    scopus 로고
    • Cells, rather than extracellular matrix, nucleate apatite in glutaraldehyde-treated vascular tissue
    • Kim KM. Cells, rather than extracellular matrix, nucleate apatite in glutaraldehyde-treated vascular tissue. J Biomed Mater Res 2002; 59: 639-45.
    • (2002) J Biomed Mater Res , vol.59 , pp. 639-645
    • Kim, K.M.1
  • 24
    • 0035067454 scopus 로고    scopus 로고
    • Cellular mechanism of calcification and its prevention in glutaraldehyde treated vascular tissue
    • Kim KM. Cellular mechanism of calcification and its prevention in glutaraldehyde treated vascular tissue. Z Kardiol 2001; 90 (suppl 3): S99-105.
    • (2001) Z Kardiol , vol.90 , Issue.SUPPL. 3
    • Kim, K.M.1
  • 25
    • 0033037008 scopus 로고    scopus 로고
    • Role of glutaraldehyde in calcification of porcine aortic valve fibroblasts
    • Kim KM, Herrera GA, Battarbee HD. Role of glutaraldehyde in calcification of porcine aortic valve fibroblasts. Am J Pathol 1999; 154: 843-52.
    • (1999) Am J Pathol , vol.154 , pp. 843-852
    • Kim, K.M.1    Herrera, G.A.2    Battarbee, H.D.3
  • 26
    • 0031049725 scopus 로고    scopus 로고
    • Matrix vesicles promote mineralization in a gelatin gel
    • Boskey AL, Boyan BD, Schwartz Z. Matrix vesicles promote mineralization in a gelatin gel. Calcif Tissue Int 1997; 60: 309-15.
    • (1997) Calcif Tissue Int , vol.60 , pp. 309-315
    • Boskey, A.L.1    Boyan, B.D.2    Schwartz, Z.3
  • 27
    • 0030425363 scopus 로고    scopus 로고
    • Matrix proteins and mineralization: An overview
    • Boskey AL. Matrix proteins and mineralization: an overview. Connect Tissue Res 1997; 35: 357-63.
    • (1997) Connect Tissue Res , vol.35 , pp. 357-363
    • Boskey, A.L.1
  • 28
    • 0029061758 scopus 로고
    • Molecular biology of matrix vesicles
    • Anderson HC. Molecular biology of matrix vesicles. Clin Orthop 1995; 31: 266-80.
    • (1995) Clin Orthop , vol.31 , pp. 266-280
    • Anderson, H.C.1
  • 29
    • 0017282062 scopus 로고
    • Calcification of matrix vesicles in human aortic valve and aortic media
    • Kim KM. Calcification of matrix vesicles in human aortic valve and aortic media. Fed Proc 1976; 35: 156-62.
    • (1976) Fed Proc , vol.35 , pp. 156-162
    • Kim, K.M.1
  • 30
    • 0022966729 scopus 로고
    • Bioprosthetic heart valve calcification: Clinical features, pathobiology and prospects for prevention
    • Levy RJ, Schoen FJ, Golomb G. Bioprosthetic heart valve calcification: clinical features, pathobiology and prospects for prevention. CRC Crit Rev Biocompat 1986; 2: 147-87.
    • (1986) CRC Crit Rev Biocompat , vol.2 , pp. 147-187
    • Levy, R.J.1    Schoen, F.J.2    Golomb, G.3
  • 32
    • 0035002811 scopus 로고    scopus 로고
    • Tissue characterization and calcification potential of commercial bioprosthetic heart valves
    • Cunanan CM, Cabiling CM, Dinh TT, et al. Tissue characterization and calcification potential of commercial bioprosthetic heart valves. Ann Thorac Surg 2001; 7 (suppl): S417-21.
    • (2001) Ann Thorac Surg , vol.7 , Issue.SUPPL.
    • Cunanan, C.M.1    Cabiling, C.M.2    Dinh, T.T.3
  • 33
    • 0031915517 scopus 로고    scopus 로고
    • Role of lipid in calcification of porcine pulmonary and aortic valves
    • Chanda J, Kuribayashi R, Abe T. Role of lipid in calcification of porcine pulmonary and aortic valves. J Thorac Cardiovasc Surg 1998; 115: 259-61.
    • (1998) J Thorac Cardiovasc Surg , vol.115 , pp. 259-261
    • Chanda, J.1    Kuribayashi, R.2    Abe, T.3
  • 35
    • 0028141555 scopus 로고
    • Inhibition of the calcification of porcine valve tissue by selective lipid removal
    • Jorge-Herrero E, Fernandez P, de la Torre N. Inhibition of the calcification of porcine valve tissue by selective lipid removal. Biomaterials 1994; 15: 815-20.
    • (1994) Biomaterials , vol.15 , pp. 815-820
    • Jorge-Herrero, E.1    Fernandez, P.2    De La Torre, N.3
  • 36
    • 0025762330 scopus 로고
    • Study of the calcification of bovine pericardium: Analysis of the implication of lipids and proteoglycans
    • Jorge-Herrero E, Fernandez P, Gutierrez M, Castillo OJ. Study of the calcification of bovine pericardium: analysis of the implication of lipids and proteoglycans. Biomaterials 1991; 12: 683-9.
    • (1991) Biomaterials , vol.12 , pp. 683-689
    • Jorge-Herrero, E.1    Fernandez, P.2    Gutierrez, M.3    Castillo, O.J.4
  • 37
    • 0032433142 scopus 로고    scopus 로고
    • Biomineralization: Conflicts, challenges, and opportunities
    • Boskey AL. Biomineralization: Conflicts, challenges, and opportunities. J Cell Biochem 1998; 30-31 (suppl): S83-91.
    • (1998) J Cell Biochem , vol.30-31 , Issue.SUPPL.
    • Boskey, A.L.1
  • 38
    • 0032776760 scopus 로고    scopus 로고
    • Noncollagenous bone matrix proteins, calcification, and thrombosis in carotid artery atherosclerosis
    • Bini A, Mann KG, Kudryk BJ, Schoen FJ. Noncollagenous bone matrix proteins, calcification, and thrombosis in carotid artery atherosclerosis. Arterioscler Thromb Vasc Biol 1999; 19: 1852-61.
    • (1999) Arterioscler Thromb Vasc Biol , vol.19 , pp. 1852-1861
    • Bini, A.1    Mann, K.G.2    Kudryk, B.J.3    Schoen, F.J.4
  • 39
    • 0034968385 scopus 로고    scopus 로고
    • Arterial calcification: A review of mechanisms, animal models, and the prospects for therapy
    • Wallin R, Wajih N, Greenwood GT, Sane DC. Arterial calcification: a review of mechanisms, animal models, and the prospects for therapy. Med Res Rev 2001; 21: 274-301.
    • (2001) Med Res Rev , vol.21 , pp. 274-301
    • Wallin, R.1    Wajih, N.2    Greenwood, G.T.3    Sane, D.C.4
  • 41
    • 0028360832 scopus 로고
    • High expression of genes for calcification-regulating proteins in human atherosclerotic plaques
    • Shanahan CM, Cary NR, Metcalfe JC, Weissberg PL. High expression of genes for calcification-regulating proteins in human atherosclerotic plaques. J Clin Invest 1994; 93: 2393-402.
    • (1994) J Clin Invest , vol.93 , pp. 2393-2402
    • Shanahan, C.M.1    Cary, N.R.2    Metcalfe, J.C.3    Weissberg, P.L.4
  • 43
    • 0031867174 scopus 로고    scopus 로고
    • Noncollagenous matrix proteins controlling mineralization: Possible role in pathologic calcification of vascular tissue
    • Donley GE, Fitzpatrick LA. Noncollagenous matrix proteins controlling mineralization: Possible role in pathologic calcification of vascular tissue. Trends Cardiovasc Med 1998; 8: 199-206.
    • (1998) Trends Cardiovasc Med , vol.8 , pp. 199-206
    • Donley, G.E.1    Fitzpatrick, L.A.2
  • 44
    • 8244251431 scopus 로고    scopus 로고
    • Identification of specific calcium-binding noncollagenous proteins associated with glutaraldehyde-preserved bovine pericardium in the rat subdermal model
    • Gura TA, Wright KL, Veis A, Webb CL. Identification of specific calcium-binding noncollagenous proteins associated with glutaraldehyde-preserved bovine pericardium in the rat subdermal model. J Biomed Mater Res 1997; 35: 483-95.
    • (1997) J Biomed Mater Res , vol.35 , pp. 483-495
    • Gura, T.A.1    Wright, K.L.2    Veis, A.3    Webb, C.L.4
  • 45
    • 0035011006 scopus 로고    scopus 로고
    • Protein adsorption of calcified and noncalcified valvular bioprostheses after human implantation
    • Shen M, Carpentier SM, Berrebi AJ, Chen L, Martinet B, Carpentier A. Protein adsorption of calcified and noncalcified valvular bioprostheses after human implantation. Ann Thorac Surg 2001; 71 (suppl): S406-7.
    • (2001) Ann Thorac Surg , vol.71 , Issue.SUPPL.
    • Shen, M.1    Carpentier, S.M.2    Berrebi, A.J.3    Chen, L.4    Martinet, B.5    Carpentier, A.6
  • 46
    • 0342526194 scopus 로고    scopus 로고
    • Protein adsorption in glutaraldehyde-preserved bovine pericardium and porcine valve tissues
    • Shen M, Carpentier SM, Cambillau M, Chen L, Martinet B, Carpentier A. Protein adsorption in glutaraldehyde-preserved bovine pericardium and porcine valve tissues. Ann Thorac Surg 2001; 71 (suppl): S408-9.
    • (2001) Ann Thorac Surg , vol.71 , Issue.SUPPL.
    • Shen, M.1    Carpentier, S.M.2    Cambillau, M.3    Chen, L.4    Martinet, B.5    Carpentier, A.6
  • 47
    • 3042766119 scopus 로고    scopus 로고
    • Living artificial heart valve alternatives: A review
    • Flanagan TC, Pandit A. Living artificial heart valve alternatives: a review. Eur Cell Mater 2003; 6: 28-45.
    • (2003) Eur Cell Mater , vol.6 , pp. 28-45
    • Flanagan, T.C.1    Pandit, A.2
  • 48
    • 3142710221 scopus 로고    scopus 로고
    • Glycosaminoglycans and proteoglycans in normal mitral valve leaflets and chordae: Association with regions of tensile and compressive loading
    • Grande-Allen KJ, Calabro A, Gupta V, Wight TN, Hascall VC, Vesely I. Glycosaminoglycans and proteoglycans in normal mitral valve leaflets and chordae: association with regions of tensile and compressive loading. Glycobiology 2004; 14: 621-33.
    • (2004) Glycobiology , vol.14 , pp. 621-633
    • Grande-Allen, K.J.1    Calabro, A.2    Gupta, V.3    Wight, T.N.4    Hascall, V.C.5    Vesely, I.6
  • 50
    • 0032937211 scopus 로고    scopus 로고
    • Mechanisms of bioprosthetic heart valve failure: Fatigue causes collagen denaturation and glycosaminoglycan loss
    • Vyavahare N, Ogle M, Schoen FJ, et al. Mechanisms of bioprosthetic heart valve failure: Fatigue causes collagen denaturation and glycosaminoglycan loss. J Biomed Mater Res 1999; 46: 44-50.
    • (1999) J Biomed Mater Res , vol.46 , pp. 44-50
    • Vyavahare, N.1    Ogle, M.2    Schoen, F.J.3
  • 51
    • 0024330489 scopus 로고
    • Bovine pericardial proteoglycan: Biochemical, immunochemical and ultrastructural studies
    • Simionescu D, Iozzo RV, Kefalides NA. Bovine pericardial proteoglycan: biochemical, immunochemical and ultrastructural studies. Matrix 1989; 9: 301-10.
    • (1989) Matrix , vol.9 , pp. 301-310
    • Simionescu, D.1    Iozzo, R.V.2    Kefalides, N.A.3
  • 52
    • 0022544569 scopus 로고
    • The effects of proteoglycans from different cartilage types on in vitro hydroxyapatite proliferation
    • Chen CC, Boskey AL. The effects of proteoglycans from different cartilage types on in vitro hydroxyapatite proliferation. Calcif Tissue Int 1986; 39: 324-7.
    • (1986) Calcif Tissue Int , vol.39 , pp. 324-327
    • Chen, C.C.1    Boskey, A.L.2
  • 53
    • 0021839435 scopus 로고
    • Inhibition of hydroxyapatite formation in collagen gels by chondroitin sulphate
    • Hunter GK, Allen BL, Grynpas MD, Cheng PT. Inhibition of hydroxyapatite formation in collagen gels by chondroitin sulphate. Biochem J 1985; 228: 463-9.
    • (1985) Biochem J , vol.228 , pp. 463-469
    • Hunter, G.K.1    Allen, B.L.2    Grynpas, M.D.3    Cheng, P.T.4
  • 54
    • 0026801022 scopus 로고
    • Inhibition of calcification in vivo by acyl azide cross-linking of a collagen-glycosaminoglycan sponge
    • Anselme K, Petite H, Herbage D. Inhibition of calcification in vivo by acyl azide cross-linking of a collagen-glycosaminoglycan sponge. Matrix 1992; 12: 264-73.
    • (1992) Matrix , vol.12 , pp. 264-273
    • Anselme, K.1    Petite, H.2    Herbage, D.3
  • 55
    • 0030130654 scopus 로고    scopus 로고
    • Chondroitin-6-sulphate incorporated into collagen gels for the growth of human keratinocytes: The effect of cross-linking agents and diamines
    • Hanthamrongwit M, Reid WH, Grant MH. Chondroitin-6-sulphate incorporated into collagen gels for the growth of human keratinocytes: the effect of cross-linking agents and diamines. Biomaterials 1996; 17: 775-80.
    • (1996) Biomaterials , vol.17 , pp. 775-780
    • Hanthamrongwit, M.1    Reid, W.H.2    Grant, M.H.3
  • 56
    • 0033135497 scopus 로고    scopus 로고
    • Preparation and characterization of porous crosslinked collagenous matrices containing bioavailable chondroitin sulphate
    • Pieper JS, Oosterhof A, Dijkstra PJ, Veerkamp JH, van Kuppevelt TH. Preparation and characterization of porous crosslinked collagenous matrices containing bioavailable chondroitin sulphate. Biomaterials 1999; 20: 847-58.
    • (1999) Biomaterials , vol.20 , pp. 847-858
    • Pieper, J.S.1    Oosterhof, A.2    Dijkstra, P.J.3    Veerkamp, J.H.4    Van Kuppevelt, T.H.5
  • 57
    • 0035885543 scopus 로고    scopus 로고
    • Periodate-mediated glycosaminoglycan stabilization in bioprosthetic heart valves
    • Lovekamp J, Vyavahare N. Periodate-mediated glycosaminoglycan stabilization in bioprosthetic heart valves. J Biomed Mater Res 2001; 56: 478-86.
    • (2001) J Biomed Mater Res , vol.56 , pp. 478-486
    • Lovekamp, J.1    Vyavahare, N.2
  • 58
    • 1542328784 scopus 로고    scopus 로고
    • Effects of periodate and chondroitin 4-sulfate on proteoglycan stabilization of ostrich pericardium. Inhibition of calcification in subcutaneous implants in rats
    • Arenaz B, Maestro MM, Fernandez P, et al. Effects of periodate and chondroitin 4-sulfate on proteoglycan stabilization of ostrich pericardium. Inhibition of calcification in subcutaneous implants in rats. Biomaterials 2004; 25: 3359-68.
    • (2004) Biomaterials , vol.25 , pp. 3359-3368
    • Arenaz, B.1    Maestro, M.M.2    Fernandez, P.3
  • 59
    • 12944328005 scopus 로고    scopus 로고
    • Phosphate is a specific signal for induction of osteopontin gene expression
    • Beck GR, Jr., Zerler B, Moran E. Phosphate is a specific signal for induction of osteopontin gene expression. Proc Natl Acad Sci USA 2000; 97: 8352-7.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8352-8357
    • Beck Jr., G.R.1    Zerler, B.2    Moran, E.3
  • 60
    • 0029200915 scopus 로고
    • A new method for in vitro calcification using acrylamide gel and bovine serum
    • Taira T, Iijima M, Moriwaki Y, Kuboki Y. A new method for in vitro calcification using acrylamide gel and bovine serum. Connect Tissue Res 1995; 33: 185-92.
    • (1995) Connect Tissue Res , vol.33 , pp. 185-192
    • Taira, T.1    Iijima, M.2    Moriwaki, Y.3    Kuboki, Y.4
  • 61
    • 0028951807 scopus 로고
    • Mineralization of alkaline phosphatase-complexed collagen implants in the rat in relation to serum inorganic phosphate
    • van den BT, Oosting J, Everts V, Beertsen W. Mineralization of alkaline phosphatase-complexed collagen implants in the rat in relation to serum inorganic phosphate. J Bone Miner Res 1995; 10: 616-24.
    • (1995) J Bone Miner Res , vol.10 , pp. 616-624
    • Van Den, B.T.1    Oosting, J.2    Everts, V.3    Beertsen, W.4
  • 62
    • 0034083435 scopus 로고    scopus 로고
    • Synergistic effect of released aspirin/heparin for preventing bovine pericardial calcification
    • Vasudev SC, Chandy T, Sharma CP, Mohanty M, Umasankar PR. Synergistic effect of released aspirin/heparin for preventing bovine pericardial calcification. Artif Organs 2000; 24: 129-36.
    • (2000) Artif Organs , vol.24 , pp. 129-136
    • Vasudev, S.C.1    Chandy, T.2    Sharma, C.P.3    Mohanty, M.4    Umasankar, P.R.5
  • 63
    • 0035235907 scopus 로고    scopus 로고
    • Structural studies on MMPs and TIMPs
    • Bode W, Maskos K. Structural studies on MMPs and TIMPs. Methods Mol Biol 2001; 151: 45-77.
    • (2001) Methods Mol Biol , vol.151 , pp. 45-77
    • Bode, W.1    Maskos, K.2
  • 65
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 1998; 12: 1075-95.
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 66
    • 0030810640 scopus 로고    scopus 로고
    • Matrix metalloproteinases in skin
    • Kahari VM, Saarialho KU. Matrix metalloproteinases in skin. Exp Dermatol 1997; 6: 199-213.
    • (1997) Exp Dermatol , vol.6 , pp. 199-213
    • Kahari, V.M.1    Saarialho, K.U.2
  • 67
    • 0347383841 scopus 로고    scopus 로고
    • Extra-cellular matrix degrading enzymes are active in porcine stentless aortic bioprosthetic heart valves
    • Simionescu DT, Lovekamp JJ, Vyavahare NR. Extra-cellular matrix degrading enzymes are active in porcine stentless aortic bioprosthetic heart valves. J Biomed Mater Res A 2003; 66: 755-63.
    • (2003) J Biomed Mater Res A , vol.66 , pp. 755-763
    • Simionescu, D.T.1    Lovekamp, J.J.2    Vyavahare, N.R.3
  • 68
    • 0030293571 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the pathology of natural and bioprosthetic cardiac valves
    • Simionescu A, Simionescu D, Deac RF. Matrix metalloproteinases in the pathology of natural and bioprosthetic cardiac valves. Cardiovasc Pathol 1996; 5: 323-32.
    • (1996) Cardiovasc Pathol , vol.5 , pp. 323-332
    • Simionescu, A.1    Simionescu, D.2    Deac, R.F.3
  • 69
    • 0035989724 scopus 로고    scopus 로고
    • Gelatinases in soft tissue biomaterials. Analysis of different crosslinking agents
    • Calero P, Jorge-Herrero E, Turnay J, et al. Gelatinases in soft tissue biomaterials. Analysis of different crosslinking agents. Biomaterials 2002; 23: 3473-8.
    • (2002) Biomaterials , vol.23 , pp. 3473-3478
    • Calero, P.1    Jorge-Herrero, E.2    Turnay, J.3
  • 70
    • 0029361194 scopus 로고
    • Cytocompatibility of calf pericardium treated by glutaraldehyde and by the acyl azide methods in an organotypic culture model
    • Petite H, Duval JL, Frei V, Abdul-Malak N, Sigot-Luizard MF, Herbage D. Cytocompatibility of calf pericardium treated by glutaraldehyde and by the acyl azide methods in an organotypic culture model. Biomaterials 1995; 16: 1003-8.
    • (1995) Biomaterials , vol.16 , pp. 1003-1008
    • Petite, H.1    Duval, J.L.2    Frei, V.3    Abdul-Malak, N.4    Sigot-Luizard, M.F.5    Herbage, D.6
  • 71
    • 0028372260 scopus 로고
    • Use of diphenylphosphorylazide for cross-linking collagen-based biomaterials
    • Petite H, Frei V, Hue A, Herbage D. Use of diphenylphosphorylazide for cross-linking collagen-based biomaterials. J Biomed Mater Res 1994; 28: 159-65.
    • (1994) J Biomed Mater Res , vol.28 , pp. 159-165
    • Petite, H.1    Frei, V.2    Hue, A.3    Herbage, D.4
  • 72
    • 0019434294 scopus 로고
    • Calcific deposits developing in a bovine pericardial bioprosthetic valve 3 days after implantation
    • Ishihara T, Ferrans VJ, Jones M, Cabin HS, Roberts WC. Calcific deposits developing in a bovine pericardial bioprosthetic valve 3 days after implantation. Circulation 1981; 63: 718-23.
    • (1981) Circulation , vol.63 , pp. 718-723
    • Ishihara, T.1    Ferrans, V.J.2    Jones, M.3    Cabin, H.S.4    Roberts, W.C.5
  • 74
    • 0141737644 scopus 로고    scopus 로고
    • The evolution of bioprosthetic heart valve design and its impact on durability
    • Vesely I. The evolution of bioprosthetic heart valve design and its impact on durability. Cardiovasc Pathol 2003; 12: 277-86.
    • (2003) Cardiovasc Pathol , vol.12 , pp. 277-286
    • Vesely, I.1
  • 75
    • 0030916350 scopus 로고    scopus 로고
    • In vivo and in vitro models of calcification in porcine aortic valve cusps
    • Mako WJ, Vesely I. In vivo and in vitro models of calcification in porcine aortic valve cusps. J Heart Valve Dis 1997; 6: 316-23.
    • (1997) J Heart Valve Dis , vol.6 , pp. 316-323
    • Mako, W.J.1    Vesely, I.2
  • 76
    • 0034921430 scopus 로고    scopus 로고
    • Tissue damage and calcification may be independent mechanisms of bioprosthetic heart valve failure
    • Vesely I, Barber JE, Ratliff NB. Tissue damage and calcification may be independent mechanisms of bioprosthetic heart valve failure. J Heart Valve Dis 2001; 10: 471-7.
    • (2001) J Heart Valve Dis , vol.10 , pp. 471-477
    • Vesely, I.1    Barber, J.E.2    Ratliff, N.B.3
  • 77
    • 0035056885 scopus 로고    scopus 로고
    • Primary tissue failure of bioprostheses: New evidence from in vitro tests
    • Deiwick M, Glasmacher B, Pettenazzo E, et al. Primary tissue failure of bioprostheses: new evidence from in vitro tests. Thorac Cardiovasc Surg 2001; 49: 78-83.
    • (2001) Thorac Cardiovasc Surg , vol.49 , pp. 78-83
    • Deiwick, M.1    Glasmacher, B.2    Pettenazzo, E.3
  • 78
    • 0035076049 scopus 로고    scopus 로고
    • Dynamic in vitro calcification of bioprosthetic porcine valves: Evidence of apatite crystallization
    • Pettenazzo E, Deiwick M, Thiene G, et al. Dynamic in vitro calcification of bioprosthetic porcine valves: evidence of apatite crystallization. J Thorac Cardiovasc Surg 2001; 121: 500-9.
    • (2001) J Thorac Cardiovasc Surg , vol.121 , pp. 500-509
    • Pettenazzo, E.1    Deiwick, M.2    Thiene, G.3
  • 79
    • 0032465772 scopus 로고    scopus 로고
    • In vitro testing of bioprostheses: Influence of mechanical stresses and lipids on calcification
    • Deiwick M, Glasmacher B, Baba HA, et al. In vitro testing of bioprostheses: influence of mechanical stresses and lipids on calcification. Ann Thorac Surg 1998; 66 (suppl): S206-11.
    • (1998) Ann Thorac Surg , vol.66 , Issue.SUPPL.
    • Deiwick, M.1    Glasmacher, B.2    Baba, H.A.3
  • 80
    • 0033151357 scopus 로고    scopus 로고
    • Mechanical loading of bovine pericardium accelerates enzymatic degradation
    • Ellsmere JC, Khanna RA, Lee JM. Mechanical loading of bovine pericardium accelerates enzymatic degradation. Biomaterials 1999; 20: 1143-50.
    • (1999) Biomaterials , vol.20 , pp. 1143-1150
    • Ellsmere, J.C.1    Khanna, R.A.2    Lee, J.M.3
  • 81
    • 0031034966 scopus 로고    scopus 로고
    • Methods for the treatment of collagenous tissues for bioprostheses
    • Khor E. Methods for the treatment of collagenous tissues for bioprostheses. Biomaterials 1997; 18: 95-105.
    • (1997) Biomaterials , vol.18 , pp. 95-105
    • Khor, E.1
  • 82
    • 0023364007 scopus 로고
    • Chemically modified collagen: A natural biomaterial for tissue replacement
    • Nimni ME, Cheung D, Strates B, Kodama M, Sheikh K. Chemically modified collagen: a natural biomaterial for tissue replacement. J Biomed Mater Res 1987; 21: 741-71.
    • (1987) J Biomed Mater Res , vol.21 , pp. 741-771
    • Nimni, M.E.1    Cheung, D.2    Strates, B.3    Kodama, M.4    Sheikh, K.5
  • 83
    • 9844260057 scopus 로고    scopus 로고
    • Altered mechanical properties in aortic elastic tissue using glutaraldehyde/solvent solutions of various dielectric constant
    • Gratzer PF, Lee JM. Altered mechanical properties in aortic elastic tissue using glutaraldehyde/solvent solutions of various dielectric constant. J Biomed Mater Res 1997; 37: 497-507.
    • (1997) J Biomed Mater Res , vol.37 , pp. 497-507
    • Gratzer, P.F.1    Lee, J.M.2
  • 84
    • 0030222089 scopus 로고    scopus 로고
    • Solvent environment modulates effects of glutaraldehyde crosslinking on tissue-derived biomaterials
    • Gratzer PF, Pereira CA, Lee JM. Solvent environment modulates effects of glutaraldehyde crosslinking on tissue-derived biomaterials. J Biomed Mater Res 1996; 31: 533-43.
    • (1996) J Biomed Mater Res , vol.31 , pp. 533-543
    • Gratzer, P.F.1    Pereira, C.A.2    Lee, J.M.3
  • 85
    • 0025663941 scopus 로고
    • Mechanism of crosslinking of proteins by glutaraldehyde. IV: In vitro and in vivo stability of a crosslinked collagen matrix
    • Cheung DT, Tong D, Perelman N, Ertl D, Nimni ME. Mechanism of crosslinking of proteins by glutaraldehyde. IV: In vitro and in vivo stability of a crosslinked collagen matrix. Connect Tissue Res 1990; 25: 27-34.
    • (1990) Connect Tissue Res , vol.25 , pp. 27-34
    • Cheung, D.T.1    Tong, D.2    Perelman, N.3    Ertl, D.4    Nimni, M.E.5
  • 86
    • 0021998324 scopus 로고
    • Mechanism of crosslinking of proteins by glutaraldehyde III. Reaction with collagen in tissues
    • Cheung DT, Perelman N, Ko EC, Nimni ME. Mechanism of crosslinking of proteins by glutaraldehyde III. Reaction with collagen in tissues. Connect Tissue Res 1985; 13: 109-15.
    • (1985) Connect Tissue Res , vol.13 , pp. 109-115
    • Cheung, D.T.1    Perelman, N.2    Ko, E.C.3    Nimni, M.E.4
  • 87
    • 0008525297 scopus 로고    scopus 로고
    • In vitro degradation of dermal sheep collagen cross-linked using a water-soluble carbodiimide
    • Olde DL, Dijkstra PJ, van LM, van WP, Nieuwenhuis P, Feijen J. In vitro degradation of dermal sheep collagen cross-linked using a water-soluble carbodiimide. Biomaterials 1996; 17: 679-84.
    • (1996) Biomaterials , vol.17 , pp. 679-684
    • Olde, D.L.1    Dijkstra, P.J.2    Van, L.M.3    Van, W.P.4    Nieuwenhuis, P.5    Feijen, J.6
  • 88
    • 0030130673 scopus 로고    scopus 로고
    • Cross-linking of dermal sheep collagen using a water-soluble carbodiimide
    • Olde Damink LH, Dijkstra PJ, et al. Cross-linking of dermal sheep collagen using a water-soluble carbodiimide. Biomaterials 1996; 17: 765-73.
    • (1996) Biomaterials , vol.17 , pp. 765-773
    • Olde Damink, L.H.1    Dijkstra, P.J.2
  • 90
    • 0033105226 scopus 로고    scopus 로고
    • Influence of different chemical cross-linking treatments on the properties of bovine pericardium and collagen
    • Jorge-Herrero E, Fernandez P, Turnay J, et al. Influence of different chemical cross-linking treatments on the properties of bovine pericardium and collagen. Biomaterials 1999; 20: 539-45.
    • (1999) Biomaterials , vol.20 , pp. 539-545
    • Jorge-Herrero, E.1    Fernandez, P.2    Turnay, J.3
  • 91
    • 0028455041 scopus 로고
    • Fixation of bioprosthetic tissues with monofunctional and multifunctional polyepoxy compounds
    • Tu R, Shen SH, Lin D, et al. Fixation of bioprosthetic tissues with monofunctional and multifunctional polyepoxy compounds. J Biomed Mater Res 1994; 28: 677-84.
    • (1994) J Biomed Mater Res , vol.28 , pp. 677-684
    • Tu, R.1    Shen, S.H.2    Lin, D.3
  • 92
    • 0028450616 scopus 로고
    • Characterization of a polyepoxy compound fixed porcine heart valve bioprosthesis
    • Shen SH, Sung HW, Tu R, et al. Characterization of a polyepoxy compound fixed porcine heart valve bioprosthesis. J Appl Biomater 1994; 5: 159-62.
    • (1994) J Appl Biomater , vol.5 , pp. 159-162
    • Shen, S.H.1    Sung, H.W.2    Tu, R.3
  • 93
    • 0002431356 scopus 로고
    • Photooxidation of amino acids in the presence of methylene blue
    • Weil L, Gordon W, Buchert A. Photooxidation of amino acids in the presence of methylene blue. Arch Biochem Biophys 1951; 33: 90-109.
    • (1951) Arch Biochem Biophys , vol.33 , pp. 90-109
    • Weil, L.1    Gordon, W.2    Buchert, A.3
  • 94
    • 0037841809 scopus 로고    scopus 로고
    • Porcine stentless bioprostheses: Prevention of aortic wall calcification by dye-mediated photo-oxidation
    • Meuris B, Phillips R, Moore MA, Flameng W. Porcine stentless bioprostheses: prevention of aortic wall calcification by dye-mediated photo-oxidation. Artif Organs 2003; 27: 537-43.
    • (2003) Artif Organs , vol.27 , pp. 537-543
    • Meuris, B.1    Phillips, R.2    Moore, M.A.3    Flameng, W.4
  • 96
    • 0035003786 scopus 로고    scopus 로고
    • Calcification characteristics of porcine stented valves in a juvenile sheep model
    • Flameng WJ, Ozaki S, Yperman J, et al. Calcification characteristics of porcine stented valves in a juvenile sheep model. Ann Thorac Surg 2001; 7 (suppl): S401-5.
    • (2001) Ann Thorac Surg , vol.7 , Issue.SUPPL.
    • Flameng, W.J.1    Ozaki, S.2    Yperman, J.3
  • 97
    • 0031037094 scopus 로고    scopus 로고
    • Prevention of bioprosthetic heart valve calcification by ethanol preincubation
    • Vyavahare N, Hirsch D, Lerner E, et al. Prevention of bioprosthetic heart valve calcification by ethanol preincubation. Circulation 1997; 95: 479-88.
    • (1997) Circulation , vol.95 , pp. 479-488
    • Vyavahare, N.1    Hirsch, D.2    Lerner, E.3
  • 98
    • 20244374227 scopus 로고    scopus 로고
    • Refinement of the alpha aminooleic acid bioprosthetic valve anticalcification technique
    • Gott JP, Girardot MN, Girardot JM, et al. Refinement of the alpha aminooleic acid bioprosthetic valve anticalcification technique. Ann Thorac Surg 1997; 64: 50-8.
    • (1997) Ann Thorac Surg , vol.64 , pp. 50-58
    • Gott, J.P.1    Girardot, M.N.2    Girardot, J.M.3
  • 99
    • 0026546806 scopus 로고
    • Calcification of porcine valves: A successful new method of antimineralization
    • Gott JP, Pan C, Dorsey LM, et al. Calcification of porcine valves: a successful new method of antimineralization. Ann Thorac Surg 1992; 53: 207-15.
    • (1992) Ann Thorac Surg , vol.53 , pp. 207-215
    • Gott, J.P.1    Pan, C.2    Dorsey, L.M.3
  • 100
    • 0028645663 scopus 로고
    • Effect of 2-amino oleic acid exposure conditions on the inhibition of calcification of glutaraldehyde cross-linked porcine aortic valves
    • Chen W, Kim JD, Schoen FJ, Levy RJ. Effect of 2-amino oleic acid exposure conditions on the inhibition of calcification of glutaraldehyde cross-linked porcine aortic valves. J Biomed Mater Res 1994; 28: 1485-95.
    • (1994) J Biomed Mater Res , vol.28 , pp. 1485-1495
    • Chen, W.1    Kim, J.D.2    Schoen, F.J.3    Levy, R.J.4
  • 101
    • 0025449552 scopus 로고
    • 3+ binding studies and metallic cation effects on bioprosthetic heart valve calcification in the rat subdermal model
    • 3+ binding studies and metallic cation effects on bioprosthetic heart valve calcification in the rat subdermal model [see comments]. ASAIO Trans 1990; 36: 56-9.
    • (1990) ASAIO Trans , vol.36 , pp. 56-59
    • Webb, C.L.1    Flowers, W.E.2    Boyd, J.3    Rosenthal, E.L.4    Schoen, F.J.5    Levy, R.J.6
  • 105
    • 0023270006 scopus 로고
    • Prevention of leaflet calcification of bioprosthetic heart valves with diphosphonate injection therapy. Experimental studies of optimal dosages and therapeutic durations
    • Levy RJ, Schoen FJ, Lund SA, Smith MS. Prevention of leaflet calcification of bioprosthetic heart valves with diphosphonate injection therapy. Experimental studies of optimal dosages and therapeutic durations. J Thorac Cardiovasc Surg 1987; 94: 551-7.
    • (1987) J Thorac Cardiovasc Surg , vol.94 , pp. 551-557
    • Levy, R.J.1    Schoen, F.J.2    Lund, S.A.3    Smith, M.S.4
  • 106
    • 0022753544 scopus 로고
    • Inhibition of bioprosthetic heart valve calcification by sustained local delivery of Ca and Na diphosphonate via controlled release matrices
    • Golomb G, Dixon M, Smith MS, Schoen FJ, Levy RJ. Inhibition of bioprosthetic heart valve calcification by sustained local delivery of Ca and Na diphosphonate via controlled release matrices. ASAIO Trans 1986; 32: 587-90.
    • (1986) ASAIO Trans , vol.32 , pp. 587-590
    • Golomb, G.1    Dixon, M.2    Smith, M.S.3    Schoen, F.J.4    Levy, R.J.5
  • 107
    • 0022177375 scopus 로고
    • Local controlled-release of diphosphonates from ethylenevinylacetate matrices prevents bioprosthetic heart valve calcification
    • Levy RJ, Golomb G, Wolfrum J, Lund SA, Schoen FJ, Langer R. Local controlled-release of diphosphonates from ethylenevinylacetate matrices prevents bioprosthetic heart valve calcification. Trans Am Soc Artif Intern Organs 1985; 31: 459-63.
    • (1985) Trans Am Soc Artif Intern Organs , vol.31 , pp. 459-463
    • Levy, R.J.1    Golomb, G.2    Wolfrum, J.3    Lund, S.A.4    Schoen, F.J.5    Langer, R.6
  • 108
    • 0034908894 scopus 로고    scopus 로고
    • Bisphosphonate derivatized polyurethanes resist calcification
    • lOS.Alferiev I, Vyavahare N, Song C, et al. Bisphosphonate derivatized polyurethanes resist calcification. Biomaterials 2001; 22: 2683-93.
    • (2001) Biomaterials , vol.22 , pp. 2683-2693
    • Alferiev, I.1    Vyavahare, N.2    Song, C.3
  • 109
    • 0021972264 scopus 로고
    • Inhibition by diphosphonate compounds of calcification of porcine bioprosthetic heart valve cusps implanted subcutaneously in rats
    • Levy RJ, Hawley MA, Schoen FJ, Lund SA, Liu PY. Inhibition by diphosphonate compounds of calcification of porcine bioprosthetic heart valve cusps implanted subcutaneously in rats. Circulation 1985; 71: 349-56.
    • (1985) Circulation , vol.71 , pp. 349-356
    • Levy, R.J.1    Hawley, M.A.2    Schoen, F.J.3    Lund, S.A.4    Liu, P.Y.5
  • 110
    • 0023378514 scopus 로고
    • Inhibition of bioprosthetic heart valve calcification with covalently bound aminopropanehydroxydiphosphonate
    • Webb CL, Benedict JJ, Schoen FJ, Linden JA, Levy RJ. Inhibition of bioprosthetic heart valve calcification with covalently bound aminopropanehydroxydiphosphonate. ASAIO Trans 1987; 33: 592-5.
    • (1987) ASAIO Trans , vol.33 , pp. 592-595
    • Webb, C.L.1    Benedict, J.J.2    Schoen, F.J.3    Linden, J.A.4    Levy, R.J.5
  • 111
    • 0036010376 scopus 로고    scopus 로고
    • In vivo evaluation of cellular and acellular bovine pericardia fixed with a naturally occurring crosslinking agent (genipin)
    • Chang Y, Tsai CC, Liang HC, Sung HW. In vivo evaluation of cellular and acellular bovine pericardia fixed with a naturally occurring crosslinking agent (genipin). Biomaterials 2002; 23: 2447-57.
    • (2002) Biomaterials , vol.23 , pp. 2447-2457
    • Chang, Y.1    Tsai, C.C.2    Liang, H.C.3    Sung, H.W.4
  • 112
    • 3042730535 scopus 로고    scopus 로고
    • Acellular bovine pericardia with distinct porous structures fixed with genipin as an extracellular matrix
    • Chang Y, Lee MH, Liang HC, Hsu CK, Sung HW. Acellular bovine pericardia with distinct porous structures fixed with genipin as an extracellular matrix. Tissue Eng 2004; 10: 881-92.
    • (2004) Tissue Eng , vol.10 , pp. 881-892
    • Chang, Y.1    Lee, M.H.2    Liang, H.C.3    Hsu, C.K.4    Sung, H.W.5
  • 113
    • 0029278594 scopus 로고
    • HMDC crosslinking of bovine pericardial tissue: A potential role of the solvent environment in the design of bioprosthetic materials
    • HS.Naimark WA, Pereira CA, Tsang K, Lee JM. HMDC crosslinking of bovine pericardial tissue: a potential role of the solvent environment in the design of bioprosthetic materials. J Mater Sci Mater Med 1995; 6: 235-41.
    • (1995) J Mater Sci Mater Med , vol.6 , pp. 235-241
    • Naimark, W.A.1    Pereira, C.A.2    Tsang, K.3    Lee, J.M.4
  • 115
    • 0031908378 scopus 로고    scopus 로고
    • The chemical protecting group concept applied in crosslinking of natural tissues with glutaraldehyde acetals
    • Goissis G, Yoshioka SA, Braile DM, Ramirez VD. The chemical protecting group concept applied in crosslinking of natural tissues with glutaraldehyde acetals. Artif Organs 1998; 22: 210-4.
    • (1998) Artif Organs , vol.22 , pp. 210-214
    • Goissis, G.1    Yoshioka, S.A.2    Braile, D.M.3    Ramirez, V.D.4
  • 116
    • 0033082384 scopus 로고    scopus 로고
    • Polyethylene glycol-grafted bovine pericardium: A novel hybrid tissue resistant to calcification
    • Vasudev SC, Chandy T. Polyethylene glycol-grafted bovine pericardium: a novel hybrid tissue resistant to calcification. J Mater Sci Mater Med 1999; 10: 121-8.
    • (1999) J Mater Sci Mater Med , vol.10 , pp. 121-128
    • Vasudev, S.C.1    Chandy, T.2
  • 117
    • 0033621692 scopus 로고    scopus 로고
    • Effects of double cross-linking technique on the enzymatic degradation and calcification of bovine pericardia
    • Vasudev SC, Chandy T, Sharma CP, Mohanty M, Umasankar PR. Effects of double cross-linking technique on the enzymatic degradation and calcification of bovine pericardia. J Biomater Appl 2000; 14: 273-95.
    • (2000) J Biomater Appl , vol.14 , pp. 273-295
    • Vasudev, S.C.1    Chandy, T.2    Sharma, C.P.3    Mohanty, M.4    Umasankar, P.R.5
  • 119
    • 0030813013 scopus 로고    scopus 로고
    • Glutaraldehyde detoxification of aortic wall tissue: A promising perspective for emerging bioprosthetic valve concepts
    • Zilla P, Fullard L, Trescony P, et al. Glutaraldehyde detoxification of aortic wall tissue: a promising perspective for emerging bioprosthetic valve concepts. J Heart Valve Dis 1997; 6: 510-20.
    • (1997) J Heart Valve Dis , vol.6 , pp. 510-520
    • Zilla, P.1    Fullard, L.2    Trescony, P.3
  • 120
    • 0025762330 scopus 로고
    • Study of the calcification of bovine pericardium: Analysis of the implication of lipids and proteoglycans
    • Jorge-Herrero E, Fernandez P, Gutierrez M, Castillo-Olivares JL. Study of the calcification of bovine pericardium: analysis of the implication of lipids and proteoglycans. Biomaterials 1991; 12: 683-9.
    • (1991) Biomaterials , vol.12 , pp. 683-689
    • Jorge-Herrero, E.1    Fernandez, P.2    Gutierrez, M.3    Castillo-Olivares, J.L.4
  • 122
    • 0032486506 scopus 로고    scopus 로고
    • Changes in serum conditioning profiles of glutaraldehyde-crosslinked collagen sponges after their treatment with calcification inhibitors
    • Santin M, Motta A, Cannas M. Changes in serum conditioning profiles of glutaraldehyde-crosslinked collagen sponges after their treatment with calcification inhibitors. J Biomed Mater Res 1998; 40: 434-41.
    • (1998) J Biomed Mater Res , vol.40 , pp. 434-441
    • Santin, M.1    Motta, A.2    Cannas, M.3
  • 123
    • 0037383606 scopus 로고    scopus 로고
    • Calcification resistance with aluminum-ethanol treated porcine aortic valve bioprostheses in juvenile sheep
    • Ogle MF, Kelly SJ, Bianco RW, Levy RJ. Calcification resistance with aluminum-ethanol treated porcine aortic valve bioprostheses in juvenile sheep. Ann Thorac Surg 2003; 75: 1267-73.
    • (2003) Ann Thorac Surg , vol.75 , pp. 1267-1273
    • Ogle, M.F.1    Kelly, S.J.2    Bianco, R.W.3    Levy, R.J.4
  • 125
    • 0032828674 scopus 로고    scopus 로고
    • Heparin coupling in inhibition of calcification of vascular bioprostheses
    • Chanda J, Kuribayashi R, Abe T. Heparin coupling in inhibition of calcification of vascular bioprostheses. Biomaterials 1999; 20: 1753-7.
    • (1999) Biomaterials , vol.20 , pp. 1753-1757
    • Chanda, J.1    Kuribayashi, R.2    Abe, T.3
  • 126
    • 0036120603 scopus 로고    scopus 로고
    • Optimization of diamine bridges in glutaraldehyde treated bioprosthetic aortic wall tissue
    • Huma P, Bezuidenhout D, Torrianni M, Hendriks M, Zilla P. Optimization of diamine bridges in glutaraldehyde treated bioprosthetic aortic wall tissue. Biomaterials 2002; 23: 2099-103.
    • (2002) Biomaterials , vol.23 , pp. 2099-2103
    • Huma, P.1    Bezuidenhout, D.2    Torrianni, M.3    Hendriks, M.4    Zilla, P.5
  • 127
    • 0030826302 scopus 로고    scopus 로고
    • High glutaraldehyde concentrations reduce rather than increase the calcification of aortic wall tissue
    • Zilla P, Weissenstein C, Bracher M, et al. High glutaraldehyde concentrations reduce rather than increase the calcification of aortic wall tissue. J Heart Valve Dis 1997; 6: 502-9.
    • (1997) J Heart Valve Dis , vol.6 , pp. 502-509
    • Zilla, P.1    Weissenstein, C.2    Bracher, M.3
  • 128
    • 4744349906 scopus 로고    scopus 로고
    • Tannic acid treatment enhances biostability and reduces calcification of glutaraldehyde fixed aortic wall
    • Isenburg JC, Simionescu DT, Vyavahare NR. Tannic acid treatment enhances biostability and reduces calcification of glutaraldehyde fixed aortic wall. Biomaterials 2005; 26: 1237-45.
    • (2005) Biomaterials , vol.26 , pp. 1237-1245
    • Isenburg, J.C.1    Simionescu, D.T.2    Vyavahare, N.R.3
  • 129
    • 1242317755 scopus 로고    scopus 로고
    • Elastin stabilization in cardiovascular implants: Improved resistance to enzymatic degradation by treatment with tannic acid
    • Isenburg JC, Simionescu DT, Vyavahare NR. Elastin stabilization in cardiovascular implants: improved resistance to enzymatic degradation by treatment with tannic acid. Biomaterials 2004; 25: 3293-302.
    • (2004) Biomaterials , vol.25 , pp. 3293-3302
    • Isenburg, J.C.1    Simionescu, D.T.2    Vyavahare, N.R.3
  • 130
    • 0032534628 scopus 로고    scopus 로고
    • Biocompatibility study of a biological tissue fixed with a naturally occurring crosslinking reagent
    • Huang LL, Sung HW, Tsai CC, Huang DM. Biocompatibility study of a biological tissue fixed with a naturally occurring crosslinking reagent. J Biomed Mater Res 1998; 42: 568-76.
    • (1998) J Biomed Mater Res , vol.42 , pp. 568-576
    • Huang, L.L.1    Sung, H.W.2    Tsai, C.C.3    Huang, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.