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Volumn 27, Issue 12, 2006, Pages 2627-2636

Fabrication and characterization of heparin functionalized membrane-mimetic assemblies

Author keywords

Anticoagulant; Antithrombogenic; Biomimetics; Heparin; Membrane mimetic

Indexed keywords

BLOOD; CHARACTERIZATION; CHEMICAL MODIFICATION; MATHEMATICAL MODELS; ORGANIC POLYMERS; THIN FILMS;

EID: 30944436469     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2005.10.032     Document Type: Article
Times cited : (20)

References (39)
  • 1
    • 0002806921 scopus 로고
    • Preparation of heparin and its use in the first clinical cases
    • C.H. Best Preparation of heparin and its use in the first clinical cases Circulation 19 1 1959 79 86
    • (1959) Circulation , vol.19 , Issue.1 , pp. 79-86
    • Best, C.H.1
  • 2
    • 0024460632 scopus 로고
    • Biochemistry of heparin antithrombin interactions, and the physiologic role of this natural anticoagulant mechanism
    • R.D. Rosenberg Biochemistry of heparin antithrombin interactions, and the physiologic role of this natural anticoagulant mechanism Am J Med 87 3B 1989 2S 9S
    • (1989) Am J Med , vol.87 , Issue.3 B
    • Rosenberg, R.D.1
  • 3
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • M.C. Bourin, and U. Lindahl Glycosaminoglycans and the regulation of blood coagulation Biochem J 289 1993 313 330
    • (1993) Biochem J , vol.289 , pp. 313-330
    • Bourin, M.C.1    Lindahl, U.2
  • 4
    • 0019163952 scopus 로고
    • The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin
    • R.E. Jordan, G.M. Oosta, W.T. Gardner, and R.D. Rosenberg The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin J Biol Chem 255 21 1980 10081 10090
    • (1980) J Biol Chem , vol.255 , Issue.21 , pp. 10081-10090
    • Jordan, R.E.1    Oosta, G.M.2    Gardner, W.T.3    Rosenberg, R.D.4
  • 5
    • 0018749685 scopus 로고
    • Fractionation of low molecular weight heparin species and their interaction with antithrombin
    • D. Beeler, R. Rosenberg, and R. Jordan Fractionation of low molecular weight heparin species and their interaction with antithrombin J Biol Chem 254 8 1979 2902 2913
    • (1979) J Biol Chem , vol.254 , Issue.8 , pp. 2902-2913
    • Beeler, D.1    Rosenberg, R.2    Jordan, R.3
  • 6
    • 0020086302 scopus 로고
    • Measurement of the heparin enhanced-antithrombin III/thrombin reaction rate in the presence of synthetic substrate
    • M.J. Griffith Measurement of the heparin enhanced-antithrombin III/thrombin reaction rate in the presence of synthetic substrate Thromb Res 25 3 1982 245 253
    • (1982) Thromb Res , vol.25 , Issue.3 , pp. 245-253
    • Griffith, M.J.1
  • 7
    • 0020314265 scopus 로고
    • Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin
    • M.J. Griffith Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin J Biol Chem 257 13 1982 7360 7365
    • (1982) J Biol Chem , vol.257 , Issue.13 , pp. 7360-7365
    • Griffith, M.J.1
  • 8
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • S.T. Olson, and I. Bjork Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects J Biol Chem 266 10 1991 6353 6364
    • (1991) J Biol Chem , vol.266 , Issue.10 , pp. 6353-6364
    • Olson, S.T.1    Bjork, I.2
  • 9
    • 0031081697 scopus 로고    scopus 로고
    • Mechanism of thrombin inhibition by antithrombin and heparin cofactor II in the presence of heparin
    • R.M. Maaroufi, M. Jozefowicz, J. Tapon-Bretaudiere, and A.M. Fischer Mechanism of thrombin inhibition by antithrombin and heparin cofactor II in the presence of heparin Biomaterials 18 3 1997 203 211
    • (1997) Biomaterials , vol.18 , Issue.3 , pp. 203-211
    • Maaroufi, R.M.1    Jozefowicz, M.2    Tapon-Bretaudiere, J.3    Fischer, A.M.4
  • 11
    • 0024110681 scopus 로고
    • Heparin immobilization onto segmented polyurethane-urea surfaces - Effect of hydrophilic spacers
    • K.D. Park, T. Okano, C. Nojiri, and S.W. Kim Heparin immobilization onto segmented polyurethane-urea surfaces - effect of hydrophilic spacers J Biomed Mater Res 22 11 1988 977 992
    • (1988) J Biomed Mater Res , vol.22 , Issue.11 , pp. 977-992
    • Park, K.D.1    Okano, T.2    Nojiri, C.3    Kim, S.W.4
  • 12
    • 0023698889 scopus 로고
    • Suppression mechanisms for thrombus formation on heparin-immobilized segmented polyurethane-ureas
    • C. Nojiri, T. Okano, K.D. Park, and S.W. Kim Suppression mechanisms for thrombus formation on heparin-immobilized segmented polyurethane-ureas ASAIO Trans 34 3 1988 386 398
    • (1988) ASAIO Trans , vol.34 , Issue.3 , pp. 386-398
    • Nojiri, C.1    Okano, T.2    Park, K.D.3    Kim, S.W.4
  • 13
    • 0020178563 scopus 로고
    • The antiplatelet activity of immobilized prostacyclin
    • C.D. Ebert, E.S. Lee, and S.W. Kim The antiplatelet activity of immobilized prostacyclin J Biomed Mater Res 16 5 1982 629 638
    • (1982) J Biomed Mater Res , vol.16 , Issue.5 , pp. 629-638
    • Ebert, C.D.1    Lee, E.S.2    Kim, S.W.3
  • 14
    • 0026498456 scopus 로고
    • Binding kinetics of thrombin and antithrombin III with immobilized heparin using a spacer
    • Y. Byun, H.A. Jacobs, and S.W. Kim Binding kinetics of thrombin and antithrombin III with immobilized heparin using a spacer ASAIO J 38 3 1992 M649 M653
    • (1992) ASAIO J , vol.38 , Issue.3
    • Byun, Y.1    Jacobs, H.A.2    Kim, S.W.3
  • 15
    • 80051989001 scopus 로고
    • Heparin surface immobilization through hydrophilic spacers: Thrombin and antithrombin III binding kinetics
    • Y. Byun, H.A. Jacobs, and S.W. Kim Heparin surface immobilization through hydrophilic spacers: thrombin and antithrombin III binding kinetics J Biomater Sci Polym Ed 6 1 1994 1 13
    • (1994) J Biomater Sci Polym Ed , vol.6 , Issue.1 , pp. 1-13
    • Byun, Y.1    Jacobs, H.A.2    Kim, S.W.3
  • 16
    • 0037059135 scopus 로고    scopus 로고
    • Functional reconstitution of thrombomodulin within a substrate-supported membrane-mimetic polymer film
    • J. Feng, P-Y. Tseng, K.M. Faucher, J.M. Orban, L. Sun X-, and E.L. Chaikof Functional reconstitution of thrombomodulin within a substrate-supported membrane-mimetic polymer film Langmuir 18 2002 9907 9913
    • (2002) Langmuir , vol.18 , pp. 9907-9913
    • Feng, J.1    Tseng, P.-Y.2    Faucher, K.M.3    Orban, J.M.4    Sun -, X.L.5    Chaikof, E.L.6
  • 17
    • 0344088270 scopus 로고    scopus 로고
    • Fabrication and characterization of glycocalyx-mimetic surfaces
    • K.M. Faucher, X.-L. Sun, and E.L. Chaikof Fabrication and characterization of glycocalyx-mimetic surfaces Langmuir 19 2003 1664 1670
    • (2003) Langmuir , vol.19 , pp. 1664-1670
    • Faucher, K.M.1    Sun, X.-L.2    Chaikof, E.L.3
  • 18
    • 0032977838 scopus 로고    scopus 로고
    • Cytomimetic biomaterials. 3. Preparation and transport studies of an alginate/amphiphilic copolymer/polymerized phospholipid film
    • J.H. Chon, K.G. Marra, and E.L. Chaikof Cytomimetic biomaterials. 3. Preparation and transport studies of an alginate/amphiphilic copolymer/polymerized phospholipid film J Biomater Sci Polym Ed 10 1 1999 95 107
    • (1999) J Biomater Sci Polym Ed , vol.10 , Issue.1 , pp. 95-107
    • Chon, J.H.1    Marra, K.G.2    Chaikof, E.L.3
  • 20
    • 0033737733 scopus 로고    scopus 로고
    • Cytomimetic biomaterials. 4. In-situ photopolymerization of phospholipids on an alkylated surface
    • J.M. Orban, K.M. Faucher, R.A. Dluhy, and E.L. Chaikof Cytomimetic biomaterials. 4. In-situ photopolymerization of phospholipids on an alkylated surface Macromolecules 33 2000 4205
    • (2000) Macromolecules , vol.33 , pp. 4205
    • Orban, J.M.1    Faucher, K.M.2    Dluhy, R.A.3    Chaikof, E.L.4
  • 21
    • 0031250267 scopus 로고    scopus 로고
    • Cytomimetic biomaterials. 1. In-situ polymerization of phospholipids on an alkylated surface
    • K.G. Marra, T.M. Winger, S.R. Hanson, and E.L. Chaikof Cytomimetic biomaterials. 1. In-situ polymerization of phospholipids on an alkylated surface Macromolecules 30 1997 6483 6487
    • (1997) Macromolecules , vol.30 , pp. 6483-6487
    • Marra, K.G.1    Winger, T.M.2    Hanson, S.R.3    Chaikof, E.L.4
  • 22
    • 0034808898 scopus 로고    scopus 로고
    • Synthesis and terminal functionalization of a polymerizable phosphatidylethanolamine
    • X.-L. Sun, H. Liu, J.M. Orban, L. Sun, and E.L. Chaikof Synthesis and terminal functionalization of a polymerizable phosphatidylethanolamine Bioconjug Chem 12 5 2001 673 677
    • (2001) Bioconjug Chem , vol.12 , Issue.5 , pp. 673-677
    • Sun, X.-L.1    Liu, H.2    Orban, J.M.3    Sun, L.4    Chaikof, E.L.5
  • 23
    • 77956990599 scopus 로고
    • Spectrophotometric determination of avidin and biotin
    • N.M. Green Spectrophotometric determination of avidin and biotin Methods Enzymol 18A 1970 418
    • (1970) Methods Enzymol , vol.18 , pp. 418
    • Green, N.M.1
  • 24
    • 0020314265 scopus 로고
    • The heparin-enhanced antithrombin III/thrombin reaction is saturable with respect to both thrombin and antithrombin III
    • M.J. Griffith The heparin-enhanced antithrombin III/thrombin reaction is saturable with respect to both thrombin and antithrombin III J Biol Chem 257 23 1982 7360 7365
    • (1982) J Biol Chem , vol.257 , Issue.23 , pp. 7360-7365
    • Griffith, M.J.1
  • 25
    • 0020325434 scopus 로고
    • The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin
    • C.H. Pletcher, and G.L. Nelsestuen The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin J Biol Chem 257 10 1982 5342 5345
    • (1982) J Biol Chem , vol.257 , Issue.10 , pp. 5342-5345
    • Pletcher, C.H.1    Nelsestuen, G.L.2
  • 27
    • 0019139542 scopus 로고
    • The binding of low molecular weight heparin to hemostatic enzymes
    • R.E. Jordan, G.M. Oosta, W.T. Gardner, and R.D. Rosenberg The binding of low molecular weight heparin to hemostatic enzymes J Biol Chem 255 21 1980 10073 10080
    • (1980) J Biol Chem , vol.255 , Issue.21 , pp. 10073-10080
    • Jordan, R.E.1    Oosta, G.M.2    Gardner, W.T.3    Rosenberg, R.D.4
  • 28
    • 0034600280 scopus 로고    scopus 로고
    • Quantification of tight binding to surface-immobilized phospholipid vesicles using surface plasmon resonance: Binding constant of phospholipase A2
    • L.S. Jung, J.S. Shumaker-Parry, C.T. Campbell, S.S. Yee, and M.H. Gelb Quantification of tight binding to surface-immobilized phospholipid vesicles using surface plasmon resonance: binding constant of phospholipase A2 J Am Chem Soc 122 2000 4177 4184
    • (2000) J Am Chem Soc , vol.122 , pp. 4177-4184
    • Jung, L.S.1    Shumaker-Parry, J.S.2    Campbell, C.T.3    Yee, S.S.4    Gelb, M.H.5
  • 29
    • 0032638067 scopus 로고    scopus 로고
    • Surface plasmon resonance measurement of binding and dissociation of wild-type and mutant streptavidin on mixed biotin-containing alkylthiolate monolayers
    • L.S. Jung, K.E. Nelson, C.T. Campbell, P.S. Stayton, S.S. Yee, and V.P. Luna Surface plasmon resonance measurement of binding and dissociation of wild-type and mutant streptavidin on mixed biotin-containing alkylthiolate monolayers Sensor Actuator B54 1999 137 144
    • (1999) Sensor Actuator , vol.54 , pp. 137-144
    • Jung, L.S.1    Nelson, K.E.2    Campbell, C.T.3    Stayton, P.S.4    Yee, S.S.5    Luna, V.P.6
  • 30
    • 36449009386 scopus 로고
    • Molecular recognition at a self-assembled monolayers: Optimization of surface functionalization
    • J. Spinke, M. Liley, F.J. Schmitt, J.H. Guder, L. Angermaier, and W. Knoll Molecular recognition at a self-assembled monolayers: optimization of surface functionalization J Chem Phys 99 9 1993 7012 7019
    • (1993) J Chem Phys , vol.99 , Issue.9 , pp. 7012-7019
    • Spinke, J.1    Liley, M.2    Schmitt, F.J.3    Guder, J.H.4    Angermaier, L.5    Knoll, W.6
  • 31
    • 0027627864 scopus 로고
    • Molecular recognition at self-assembled monolayers: The construction of multicomponent multilayers
    • J. Spinke, M. Liley, J.H. Guder, L. Angermaier, and W. Knoll Molecular recognition at self-assembled monolayers: the construction of multicomponent multilayers Langmuir 9 7 1993 1821 1825
    • (1993) Langmuir , vol.9 , Issue.7 , pp. 1821-1825
    • Spinke, J.1    Liley, M.2    Guder, J.H.3    Angermaier, L.4    Knoll, W.5
  • 33
    • 0015956518 scopus 로고
    • Theory of the kinetics of reactions catalyzed by enzymes attached to membranes
    • T. Kobayashi, and K.J. Laidler Theory of the kinetics of reactions catalyzed by enzymes attached to membranes Biotechnol Bioeng 16 1 1974 77 97
    • (1974) Biotechnol Bioeng , vol.16 , Issue.1 , pp. 77-97
    • Kobayashi, T.1    Laidler, K.J.2
  • 34
    • 0018814280 scopus 로고
    • The kinetics of immobilized enzyme systems
    • K.J. Laidler, and P.S. Bunting The kinetics of immobilized enzyme systems Methods Enzymol 64 1980 227 248
    • (1980) Methods Enzymol , vol.64 , pp. 227-248
    • Laidler, K.J.1    Bunting, P.S.2
  • 35
    • 0025600894 scopus 로고
    • The effects of shear rate on the enzymatic activity of the tissue factor-factor VIIa complex
    • C. Gemmell, Y. Nemerson, and V. Turitto The effects of shear rate on the enzymatic activity of the tissue factor-factor VIIa complex Microvasc Res 40 3 1990 327 340
    • (1990) Microvasc Res , vol.40 , Issue.3 , pp. 327-340
    • Gemmell, C.1    Nemerson, Y.2    Turitto, V.3
  • 36
    • 3442881347 scopus 로고    scopus 로고
    • Measurement of enzyme kinetics using microscale steady-state kinetic analysis
    • N.J. Gleason, and J.D. Carbeck Measurement of enzyme kinetics using microscale steady-state kinetic analysis Langmuir 20 15 2004 6374 6381
    • (2004) Langmuir , vol.20 , Issue.15 , pp. 6374-6381
    • Gleason, N.J.1    Carbeck, J.D.2
  • 37
    • 0020697148 scopus 로고
    • Heparin cofactor activities in a family with hereditary antithrombin III deficiency: Evidence for a second heparin cofactor in human plasma
    • M.J. Griffith, T. Carraway, G.C. White, and F.A. Dombrose Heparin cofactor activities in a family with hereditary antithrombin III deficiency: evidence for a second heparin cofactor in human plasma Blood 61 1 1983 111 118
    • (1983) Blood , vol.61 , Issue.1 , pp. 111-118
    • Griffith, M.J.1    Carraway, T.2    White, G.C.3    Dombrose, F.A.4
  • 38
    • 0018869509 scopus 로고
    • Some properties of antithrombin-III and its concentration in human plasma
    • G. Murano, L. Williams, M. Miller-Andersson, D.L. Aronson, and C. King Some properties of antithrombin-III and its concentration in human plasma Thromb Res 18 1-2 1980 259 262
    • (1980) Thromb Res , vol.18 , Issue.1-2 , pp. 259-262
    • Murano, G.1    Williams, L.2    Miller-Andersson, M.3    Aronson, D.L.4    King, C.5
  • 39
    • 0023930337 scopus 로고
    • Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Linkage of protease-inhibitor-heparin interactions in the reaction with thrombin
    • S.T. Olson Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Linkage of protease-inhibitor-heparin interactions in the reaction with thrombin J Biol Chem 263 4 1988 1698 1708
    • (1988) J Biol Chem , vol.263 , Issue.4 , pp. 1698-1708
    • Olson, S.T.1


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