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Volumn 4, Issue , 2002, Pages 109-128

Denaturation of collagen via heating: An irreversible rate process

Author keywords

Arrhenius behavior; Biothermomechanics; Kinetics; Thermal damage

Indexed keywords

COLLAGEN;

EID: 0036405394     PISSN: 15239829     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.bioeng.4.101001.131546     Document Type: Review
Times cited : (199)

References (48)
  • 2
    • 0002050426 scopus 로고
    • Conformational transitions of proteins in water and in aqueous mixtures
    • New York: Marcel Dekker
    • Brandts JF. 1969. Conformational transitions of proteins in water and in aqueous mixtures. In Structure and Stability of Biological Macromolecule. New York: Marcel Dekker
    • (1969) Structure and Stability of Biological Macromolecule
    • Brandts, J.F.1
  • 3
    • 0020348367 scopus 로고
    • Stability of proteins: Proteins which do not present a single cooperative system
    • ed. CB Anfinsen, JT Edsall, FM Richards. New York: Academic
    • Privalov PL. 1982. Stability of proteins: Proteins which do not present a single cooperative system. In Advances in Protein Chemistry, ed. CB Anfinsen, JT Edsall, FM Richards, pp. 1-104. New York: Academic
    • (1982) Advances in Protein Chemistry , pp. 1-104
    • Privalov, P.L.1
  • 4
    • 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. Molec. Biol. 245:437-46
    • (1995) J. Molec. Biol. , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 6
    • 0020454986 scopus 로고
    • Influence of collagen denaturation on the chemorheological properties of skin, assessed by differential scanning calorimetry and hydrothermal isometric tension measurement
    • Le Lous M, Flandin F, Herbage D, Allain JC. 1982. Influence of collagen denaturation on the chemorheological properties of skin, assessed by differential scanning calorimetry and hydrothermal isometric tension measurement. Biochim. Biophys. Acta 717:295-300
    • (1982) Biochim. Biophys. Acta , vol.717 , pp. 295-300
    • Le Lous, M.1    Flandin, F.2    Herbage, D.3    Allain, J.C.4
  • 7
    • 0015228624 scopus 로고
    • Reversible and irreversible denaturation of collagen fibers
    • Hörmann H, Schlebusch H. 1971. Reversible and irreversible denaturation of collagen fibers. Biochemistry 10:932-37
    • (1971) Biochemistry , vol.10 , pp. 932-937
    • Hörmann, H.1    Schlebusch, H.2
  • 8
    • 0026910230 scopus 로고
    • Water content alters viscoelastic behaviour of the normal adolescent rabbit medial collateral ligament
    • Chimich D, Shrive N, Frank C, Marchuk L, Bray R. 1992. Water content alters viscoelastic behaviour of the normal adolescent rabbit medial collateral ligament. J. Biomech. 25:831-37
    • (1992) J. Biomech. , vol.25 , pp. 831-837
    • Chimich, D.1    Shrive, N.2    Frank, C.3    Marchuk, L.4    Bray, R.5
  • 9
    • 0031060035 scopus 로고    scopus 로고
    • The state of tissue hydration determines the strain-rate sensitive stiffness of human patellar tendon
    • Haut TL, Haut RC. 1997. The state of tissue hydration determines the strain-rate sensitive stiffness of human patellar tendon. J. Biomech. 30:79-81
    • (1997) J. Biomech. , vol.30 , pp. 79-81
    • Haut, T.L.1    Haut, R.C.2
  • 10
    • 0000108164 scopus 로고
    • Rate of shrinkage of tendon collagen - Heat, entropy, and free energy of activation of the shrinkage of untreated tendon. Effect of acid, salt, pickle, and tannage on the activation of tendon collagen
    • Weir CE. 1949. Rate of shrinkage of tendon collagen - Heat, entropy, and free energy of activation of the shrinkage of untreated tendon. Effect of acid, salt, pickle, and tannage on the activation of tendon collagen. J. Am. Leather Chem. Assoc. 44:108-40
    • (1949) J. Am. Leather Chem. Assoc. , vol.44 , pp. 108-140
    • Weir, C.E.1
  • 11
    • 0016347158 scopus 로고
    • Effect of hydration upon the thermal stability of tropocollagen and its dependence on the presence of neutral salts
    • Luescher M, Rueff M, Schindler P. 1974. Effect of hydration upon the thermal stability of tropocollagen and its dependence on the presence of neutral salts. Polymers 13:2489-503
    • (1974) Polymers , vol.13 , pp. 2489-2503
    • Luescher, M.1    Rueff, M.2    Schindler, P.3
  • 12
    • 0011119678 scopus 로고
    • "Incipient shrinkage" of collagen and gelatin
    • Pankhurst K. 1947. "Incipient shrinkage" of collagen and gelatin. Nature 159:538
    • (1947) Nature , vol.159 , pp. 538
    • Pankhurst, K.1
  • 13
    • 0027376116 scopus 로고
    • Kinetics of collagen denaturation in mammalian lens capsules studied by differential scanning calorimetry
    • Miles CA. 1993. Kinetics of collagen denaturation in mammalian lens capsules studied by differential scanning calorimetry. Int. J. Biol. Macromol. 15:265-71
    • (1993) Int. J. Biol. Macromol. , vol.15 , pp. 265-271
    • Miles, C.A.1
  • 14
    • 0024831978 scopus 로고
    • Changes in birefringence as markers of thermal damage in tissues
    • Thomsen S, Pearce JA, Cheong W-F. 1989. Changes in birefringence as markers of thermal damage in tissues. IEEE Trans. Biomed. Eng. 36:1174-79
    • (1989) IEEE Trans. Biomed. Eng. , vol.36 , pp. 1174-1179
    • Thomsen, S.1    Pearce, J.A.2    Cheong, W.-F.3
  • 15
    • 0000114542 scopus 로고
    • The native and denatured state of soluble collagen
    • Boedtker H, Doty P. 1956. The native and denatured state of soluble collagen. J. Am. Chem. Soc. 78:4267-80
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 4267-4280
    • Boedtker, H.1    Doty, P.2
  • 16
    • 85010248732 scopus 로고
    • The thermal denaturation of collagen in solution and its structural implications
    • Burge RE, Hynes RD. 1959. The thermal denaturation of collagen in solution and its structural implications. J. Mol. Biol. 1:155-64
    • (1959) J. Mol. Biol. , vol.1 , pp. 155-164
    • Burge, R.E.1    Hynes, R.D.2
  • 17
    • 0032103901 scopus 로고    scopus 로고
    • Heat-induced changes in the mechanics of a collagenous tissue: Isothermal isotonic shrinkage
    • Chen SS, Wright NT, Humphrey JD. 1998. Heat-induced changes in the mechanics of a collagenous tissue: Isothermal isotonic shrinkage. ASME J. Biomech. Eng. 120:382-88
    • (1998) ASME J. Biomech. Eng. , vol.120 , pp. 382-388
    • Chen, S.S.1    Wright, N.T.2    Humphrey, J.D.3
  • 18
    • 0011119679 scopus 로고    scopus 로고
    • Modeling of the local heating of nonperfused tissue with directionally dependent thermal diffusivity and heat-induced damage
    • HTD, BED. New York: ASME
    • Davis SE, Chadrasekhar T, Wright NT. 2000. Modeling of the local heating of nonperfused tissue with directionally dependent thermal diffusivity and heat-induced damage. Adv. Heat and Mass Transfer in Biotechnology, HTD-Vol. 368, BED-Vol. 47, pp. 75-82. New York: ASME
    • (2000) Adv. Heat and Mass Transfer in Biotechnology , vol.47 , pp. 75-82
    • Davis, S.E.1    Chadrasekhar, T.2    Wright, N.T.3
  • 20
    • 0017405694 scopus 로고
    • Cellular responses to combinations of hyperthermia and radiation
    • Dewey DC, Hopwood LE, Sapareto SA, Gerweck LE. 1977. Cellular responses to combinations of hyperthermia and radiation. Radiology 123:463-74
    • (1977) Radiology , vol.123 , pp. 463-474
    • Dewey, D.C.1    Hopwood, L.E.2    Sapareto, S.A.3    Gerweck, L.E.4
  • 21
    • 0002473798 scopus 로고
    • Rate process analysis of thermal damage
    • ed. AJ Welch, MJC van Gemert. New York: Plenum
    • Pearce J, Thomsen S. 1995. Rate process analysis of thermal damage. In Optical-Thermal Response of Laser-Irradiated Tissue, ed. AJ Welch, MJC van Gemert, pp. 561-606. New York: Plenum
    • (1995) Optical-Thermal Response of Laser-Irradiated Tissue , pp. 561-606
    • Pearce, J.1    Thomsen, S.2
  • 22
    • 0032005301 scopus 로고    scopus 로고
    • Time-temperature equivalence in heat-induced cell damage and protein denaturation
    • Wright NT, Chen SS, Humphrey JD. 1998. Time-temperature equivalence in heat-induced cell damage and protein denaturation. ASME J. Biomech. Eng. 120:22-26
    • (1998) ASME J. Biomech. Eng. , vol.120 , pp. 22-26
    • Wright, N.T.1    Chen, S.S.2    Humphrey, J.D.3
  • 23
    • 0000445232 scopus 로고
    • The thermoelastic behavior of isolated aortic strips of the dog
    • Lawton RW. 1954. The thermoelastic behavior of isolated aortic strips of the dog. Circ. Res. 2:344-53
    • (1954) Circ. Res. , vol.2 , pp. 344-353
    • Lawton, R.W.1
  • 26
    • 0031578633 scopus 로고    scopus 로고
    • Heat-induced changes in the mechanics of a collagenous tissue: Pseudoelastic behavior at 37°C
    • Chen SS, Humphrey JD. 1998. Heat-induced changes in the mechanics of a collagenous tissue: Pseudoelastic behavior at 37°C. J. Biomech. 31:211-16
    • (1998) J. Biomech. , vol.31 , pp. 211-216
    • Chen, S.S.1    Humphrey, J.D.2
  • 28
    • 0030956754 scopus 로고    scopus 로고
    • Quantitative measurements of linear birefringence during heating of native collagen
    • Maitland DJ, Walsh JT. 1997. Quantitative measurements of linear birefringence during heating of native collagen. Lasers Surg. Med. 20:310-18
    • (1997) Lasers Surg. Med. , vol.20 , pp. 310-318
    • Maitland, D.J.1    Walsh, J.T.2
  • 29
    • 0030221206 scopus 로고    scopus 로고
    • Dynamics of temperature dependent optical properties of tissue: Dependence on thermally induced alteration
    • Agah R, Gandjbakhche AH, Motamedi M, Nossal R, Bonner RF. 1996. Dynamics of temperature dependent optical properties of tissue: Dependence on thermally induced alteration. IEEE Trans. Biomed. Eng. 43:839-46
    • (1996) IEEE Trans. Biomed. Eng. , vol.43 , pp. 839-846
    • Agah, R.1    Gandjbakhche, A.H.2    Motamedi, M.3    Nossal, R.4    Bonner, R.F.5
  • 30
    • 84953656097 scopus 로고
    • Studies of thermal injury. II. The relative importance of time and surface temperature in the causation of cutaneous burns
    • Moritz AR, Henriques FC. 1947. Studies of thermal injury. II. The relative importance of time and surface temperature in the causation of cutaneous burns. Am. J. Pathol. 23:695-720
    • (1947) Am. J. Pathol. , vol.23 , pp. 695-720
    • Moritz, A.R.1    Henriques, F.C.2
  • 32
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz JM. 1992. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61:921-35
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 33
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • Lepock JR, Ritchie KP, Kolios MC, Rodahl AM, Heinze KA, Kruuv J. 1992. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry 311:12706-12
    • (1992) Biochemistry , vol.311 , pp. 12706-12712
    • Lepock, J.R.1    Ritchie, K.P.2    Kolios, M.C.3    Rodahl, A.M.4    Heinze, K.A.5    Kruuv, J.6
  • 34
    • 0001032438 scopus 로고
    • Phase transitions in collagen and gelatin systems
    • Flory PJ, Garrett RR. 1958. Phase transitions in collagen and gelatin systems. J. Am. Chem. Soc. 80:4836-35
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 4836-4935
    • Flory, P.J.1    Garrett, R.R.2
  • 35
    • 0033029015 scopus 로고    scopus 로고
    • Polymerin-a-box mechanism for the thermal stabilization of collagen molecules in fibers
    • Miles CA, Ghelashvili M. 1999. Polymerin-a-box mechanism for the thermal stabilization of collagen molecules in fibers. Biophys. J. 76:3243-52
    • (1999) Biophys. J. , vol.76 , pp. 3243-3252
    • Miles, C.A.1    Ghelashvili, M.2
  • 36
    • 0001780742 scopus 로고
    • The shrinkage temperature of collagen fibers isolated from the tail tendons of rats of various ages and from different places of the same tendon
    • Chvapil M, Jensovsky L. 1963. The shrinkage temperature of collagen fibers isolated from the tail tendons of rats of various ages and from different places of the same tendon. Gerontologia 1:18-29
    • (1963) Gerontologia , vol.1 , pp. 18-29
    • Chvapil, M.1    Jensovsky, L.2
  • 38
    • 0025393383 scopus 로고
    • Calorimetric study of vitrification of denatured collagen
    • Tsereteli GI, Smirnova OI. 1990. Calorimetric study of vitrification of denatured collagen. Biofizika 35:217-21
    • (1990) Biofizika , vol.35 , pp. 217-221
    • Tsereteli, G.I.1    Smirnova, O.I.2
  • 39
    • 84984821750 scopus 로고
    • Studies of thermal injury V: The predictability and the significance of thermally induced rate processes leading to irreversible epidermal injury
    • Henriques FC Jr. 1947. Studies of thermal injury V: The predictability and the significance of thermally induced rate processes leading to irreversible epidermal injury. Arch. Pathol. 43:489-502
    • (1947) Arch. Pathol. , vol.43 , pp. 489-502
    • Henriques F.C., Jr.1
  • 40
    • 0027247296 scopus 로고
    • Kinetics for birefringence changes in thermally coagulated rat skin collagen
    • Pearce J, Thomsen S, Vijverberg H, McMurray T. 1993. Kinetics for birefringence changes in thermally coagulated rat skin collagen. Proc. SPIE 1876:180-86
    • (1993) Proc. SPIE , vol.1876 , pp. 180-186
    • Pearce, J.1    Thomsen, S.2    Vijverberg, H.3    McMurray, T.4
  • 41
    • 0016137496 scopus 로고
    • Development of criterion for skin burns
    • Takata A. 1974. Development of criterion for skin burns. Aerosp. Med. 45(6):634-37
    • (1974) Aerosp. Med. , vol.45 , Issue.6 , pp. 634-637
    • Takata, A.1
  • 43
    • 0029394954 scopus 로고
    • Analysis of thermal injury process based on enzyme deactivation mechanisms
    • Xu YS, Quan RZ. 1995. Analysis of thermal injury process based on enzyme deactivation mechanisms. ASME J. Biomech. Eng. 117:462-65
    • (1995) ASME J. Biomech. Eng. , vol.117 , pp. 462-465
    • Xu, Y.S.1    Quan, R.Z.2
  • 44
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry R, Eyring H. 1954. Conformation changes of proteins. J. Phys. Chem. 58:110-20
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 45
    • 0019436410 scopus 로고
    • Thermal stability of reconstituted collagen fibrils. Shrinkage characteristics upon in vitro maturation
    • Danielsen CC. 1981. Thermal stability of reconstituted collagen fibrils. Shrinkage characteristics upon in vitro maturation. Mech. Ageing Dev. 15:269-78
    • (1981) Mech. Ageing Dev. , vol.15 , pp. 269-278
    • Danielsen, C.C.1
  • 46
    • 0026035150 scopus 로고
    • Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase
    • Galisteo ML, Mateo PL, Sanchez-Ruiz JM. 1991. Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase. Biochemistry 30:2061-66
    • (1991) Biochemistry , vol.30 , pp. 2061-2066
    • Galisteo, M.L.1    Mateo, P.L.2    Sanchez-Ruiz, J.M.3
  • 47
    • 0032190595 scopus 로고    scopus 로고
    • Phenomenological evolution equations for heat-induced shrinkage of a collagenous tissue
    • Chen SS, Wright NT, Humphrey JD. 1998. Phenomenological evolution equations for heat-induced shrinkage of a collagenous tissue. IEEE Trans. Biomed. Eng. 45:1234-40
    • (1998) IEEE Trans. Biomed. Eng. , vol.45 , pp. 1234-1240
    • Chen, S.S.1    Wright, N.T.2    Humphrey, J.D.3
  • 48
    • 0035118457 scopus 로고    scopus 로고
    • Thermal stability of collagen fibers in ethylene glycol
    • Miles CA, Burjanadze TV. 2001. Thermal stability of collagen fibers in ethylene glycol. Biophys. J. 80:1480-86
    • (2001) Biophys. J. , vol.80 , pp. 1480-1486
    • Miles, C.A.1    Burjanadze, T.V.2


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