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Volumn 25, Issue 6, 2007, Pages 537-557

The many ways to cleave hyaluronan

Author keywords

Degradation; Fragmentation; Hyaluronan; Hyaluronidase; Hydrolysis; Reactive oxygen species

Indexed keywords

DEGRADATION; ENZYME ACTIVITY; FREE RADICALS; HYDROLYSIS; TISSUE CULTURE;

EID: 34648846234     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2007.07.001     Document Type: Review
Times cited : (349)

References (148)
  • 1
    • 0032715672 scopus 로고    scopus 로고
    • Identification of radicals from hyaluronan (hyaluronic acid) and cross-linked derivatives using electron paramagnetic resonance spectroscopy
    • Al-Assaf S., Hawkins C.L., Parsons B.J., Davies M.J., and Phillips G.O. Identification of radicals from hyaluronan (hyaluronic acid) and cross-linked derivatives using electron paramagnetic resonance spectroscopy. Carbohydr Polym 38 (1999) 17-22
    • (1999) Carbohydr Polym , vol.38 , pp. 17-22
    • Al-Assaf, S.1    Hawkins, C.L.2    Parsons, B.J.3    Davies, M.J.4    Phillips, G.O.5
  • 4
    • 33646753788 scopus 로고    scopus 로고
    • Chain scission of hyaluronan by carbonate and dichloride radical anions: potential reactive oxidative species in inflammation?
    • Al-Assaf S., Navaratnam S., Parsons B.J., and Phillips G.O. Chain scission of hyaluronan by carbonate and dichloride radical anions: potential reactive oxidative species in inflammation?. Free Radic Biol Med 40 (2006) 2018-2027
    • (2006) Free Radic Biol Med , vol.40 , pp. 2018-2027
    • Al-Assaf, S.1    Navaratnam, S.2    Parsons, B.J.3    Phillips, G.O.4
  • 5
    • 33646145082 scopus 로고    scopus 로고
    • Hyaluronan oligosaccharides induce cell death through PI3-K/Akt pathway independently of NF-κB transcription factor
    • Alaniz L., Garcia M.G., Gallo-Rodriguez C., Agusti R., Sterin-Speziale N., Hajos S.E., et al. Hyaluronan oligosaccharides induce cell death through PI3-K/Akt pathway independently of NF-κB transcription factor. Glycobiology 16 (2006) 359-367
    • (2006) Glycobiology , vol.16 , pp. 359-367
    • Alaniz, L.1    Garcia, M.G.2    Gallo-Rodriguez, C.3    Agusti, R.4    Sterin-Speziale, N.5    Hajos, S.E.6
  • 6
    • 3543137857 scopus 로고    scopus 로고
    • Properties, functions, and secretion of human myeloperoxidase
    • Arnhold J. Properties, functions, and secretion of human myeloperoxidase. Biochemistry (Moscow) 69 (2004) 4-9
    • (2004) Biochemistry (Moscow) , vol.69 , pp. 4-9
    • Arnhold, J.1
  • 7
    • 84940857277 scopus 로고    scopus 로고
    • Medical application of hyaluronan
    • Garg H.G., and Hales C.A. (Eds), Elsevier, Amsterdam
    • Asari A. Medical application of hyaluronan. In: Garg H.G., and Hales C.A. (Eds). Chemistry and biology of hyaluronan (2004), Elsevier, Amsterdam 457-473
    • (2004) Chemistry and biology of hyaluronan , pp. 457-473
    • Asari, A.1
  • 9
    • 33746860809 scopus 로고    scopus 로고
    • Singlet oxygen generation by UVA light exposure of endogenous photosensitizers
    • Baier J., Maisch T., Maier M., Engel E., Landthaler M., and Baumler W. Singlet oxygen generation by UVA light exposure of endogenous photosensitizers. Biophys J 91 (2006) 1452-1459
    • (2006) Biophys J , vol.91 , pp. 1452-1459
    • Baier, J.1    Maisch, T.2    Maier, M.3    Engel, E.4    Landthaler, M.5    Baumler, W.6
  • 10
    • 84940838497 scopus 로고    scopus 로고
    • Viscoelastic properties of hyaluronan and its therapeutic use
    • Garg H.G., and Hales C.A. (Eds), Elsevier, Amsterdam
    • Balazs E.A. Viscoelastic properties of hyaluronan and its therapeutic use. In: Garg H.G., and Hales C.A. (Eds). Chemistry and biology of hyaluronan (2004), Elsevier, Amsterdam 415-455
    • (2004) Chemistry and biology of hyaluronan , pp. 415-455
    • Balazs, E.A.1
  • 11
    • 33947472566 scopus 로고
    • Alkaline degradation of amino sugars
    • BeMiller J.N., and Whistler R.L. Alkaline degradation of amino sugars. J Org Chem 27 (1962) 1161-1164
    • (1962) J Org Chem , vol.27 , pp. 1161-1164
    • BeMiller, J.N.1    Whistler, R.L.2
  • 12
    • 33747093047 scopus 로고    scopus 로고
    • Enzymatic and chemical methods for the generation of pure hyaluronan oligosaccharides with both odd and even numbers of monosaccharide units
    • Blundell C.D., and Almond A. Enzymatic and chemical methods for the generation of pure hyaluronan oligosaccharides with both odd and even numbers of monosaccharide units. Anal Biochem 353 (2006) 236-247
    • (2006) Anal Biochem , vol.353 , pp. 236-247
    • Blundell, C.D.1    Almond, A.2
  • 13
    • 1542263448 scopus 로고    scopus 로고
    • The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding
    • Blundell C.D., Mahoney D.J., Almond A., DeAngelis P.L., Kahmann J.D., Teriete P., et al. The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. J Biol Chem 278 (2003) 49261-49270
    • (2003) J Biol Chem , vol.278 , pp. 49261-49270
    • Blundell, C.D.1    Mahoney, D.J.2    Almond, A.3    DeAngelis, P.L.4    Kahmann, J.D.5    Teriete, P.6
  • 14
    • 0024214911 scopus 로고
    • Limiting viscosity number and weight average molecular weight of hyaluronate samples produced by heat degradation
    • Bottner H., Waaler T., and Wik O. Limiting viscosity number and weight average molecular weight of hyaluronate samples produced by heat degradation. Int J Biol Macromol 10 (1988) 287-291
    • (1988) Int J Biol Macromol , vol.10 , pp. 287-291
    • Bottner, H.1    Waaler, T.2    Wik, O.3
  • 15
    • 8544245730 scopus 로고    scopus 로고
    • l-ascorbic acid 6-hexadecanoate, a potent hyaluronidase inhibitor. X-ray structure and molecular modeling of enzyme-inhibitor complexes
    • Botzki A., Rigden D.J., Braun S., Nukui M., Salmen S., Hoechstetter J., et al. l-ascorbic acid 6-hexadecanoate, a potent hyaluronidase inhibitor. X-ray structure and molecular modeling of enzyme-inhibitor complexes. J Biol Chem 279 (2004) 45990-45997
    • (2004) J Biol Chem , vol.279 , pp. 45990-45997
    • Botzki, A.1    Rigden, D.J.2    Braun, S.3    Nukui, M.4    Salmen, S.5    Hoechstetter, J.6
  • 16
    • 3042692979 scopus 로고    scopus 로고
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion. J Biol Chem 279 (2004) 26991-27007
    • (2004) J Biol Chem , vol.279 , pp. 26991-27007
    • Bourguignon, L.Y.W.1    Singleton, P.A.2    Diedrich, F.3    Stern, R.4    Gilad, E.5
  • 17
    • 84940845397 scopus 로고    scopus 로고
    • Hyaluronan and scarring
    • Garg H.G., and Hales C.A. (Eds), Elsevier, Amsterdam
    • Burd A. Hyaluronan and scarring. In: Garg H.G., and Hales C.A. (Eds). Chemistry and biology of hyaluronan (2004), Elsevier, Amsterdam 367-394
    • (2004) Chemistry and biology of hyaluronan , pp. 367-394
    • Burd, A.1
  • 18
    • 0035167226 scopus 로고    scopus 로고
    • Inhibition of adhesion of Plasmodium falciparum-infected erythrocytes by structurally defined hyaluronic acid dodecasaccharides
    • Chai W., Beeson J.G., Kogelberg H., Brown G.V., and Lawson A.M. Inhibition of adhesion of Plasmodium falciparum-infected erythrocytes by structurally defined hyaluronic acid dodecasaccharides. Infect Immun 69 (2001) 420-425
    • (2001) Infect Immun , vol.69 , pp. 420-425
    • Chai, W.1    Beeson, J.G.2    Kogelberg, H.3    Brown, G.V.4    Lawson, A.M.5
  • 19
    • 0001401048 scopus 로고
    • Identity of hyaluronidase and spreading factor
    • Chain E., and Duthrie E.S. Identity of hyaluronidase and spreading factor. Br J Exp Pathol 21 (1940) 324-338
    • (1940) Br J Exp Pathol , vol.21 , pp. 324-338
    • Chain, E.1    Duthrie, E.S.2
  • 21
    • 0018364417 scopus 로고
    • Interactions of cartilage proteoglycans with hyaluronate. Inhibition of the interaction by modified oligomers of hyaluronate
    • Christner J.E., Brown M.L., and Dziewiatkowski D.D. Interactions of cartilage proteoglycans with hyaluronate. Inhibition of the interaction by modified oligomers of hyaluronate. J Biol Chem 254 (1979) 4624-4630
    • (1979) J Biol Chem , vol.254 , pp. 4624-4630
    • Christner, J.E.1    Brown, M.L.2    Dziewiatkowski, D.D.3
  • 23
    • 0041315653 scopus 로고    scopus 로고
    • Rapid chemoenzymatic synthesis of monodisperse hyaluronan oligosaccharides with immobilized enzyme reactors
    • DeAngelis P.L., Oatman L.C., and Gay D.F. Rapid chemoenzymatic synthesis of monodisperse hyaluronan oligosaccharides with immobilized enzyme reactors. J Biol Chem 278 (2003) 35199-35203
    • (2003) J Biol Chem , vol.278 , pp. 35199-35203
    • DeAngelis, P.L.1    Oatman, L.C.2    Gay, D.F.3
  • 24
    • 24644488255 scopus 로고    scopus 로고
    • Degradation of hyaluronan by ultrasonication in comparison to microwave and conventional heating
    • Dřímalová E., Velebný V., Sasinková V., Hromádková Z., and Ebringerová A. Degradation of hyaluronan by ultrasonication in comparison to microwave and conventional heating. Carbohydr Polym 61 (2005) 420-426
    • (2005) Carbohydr Polym , vol.61 , pp. 420-426
    • Dřímalová, E.1    Velebný, V.2    Sasinková, V.3    Hromádková, Z.4    Ebringerová, A.5
  • 25
    • 0002099432 scopus 로고
    • Exaltation de l'activité du virus vaccinal par les extraits de certains organs
    • Duran-Reynals F. Exaltation de l'activité du virus vaccinal par les extraits de certains organs. CR Soc Biol 99 (1928) 6-7
    • (1928) CR Soc Biol , vol.99 , pp. 6-7
    • Duran-Reynals, F.1
  • 26
    • 0001213028 scopus 로고
    • Studies on a certain spreading factor existing in bacteria and its significance for bacterial invasiveness
    • Duran-Reynals F. Studies on a certain spreading factor existing in bacteria and its significance for bacterial invasiveness. J Exp Med 58 (1933) 161-181
    • (1933) J Exp Med , vol.58 , pp. 161-181
    • Duran-Reynals, F.1
  • 27
    • 0023882065 scopus 로고
    • Immunological detection of myeloperoxidase in synovial fluid from patients with rheumatoid arthritis
    • Edwards S.W., Hughes V., Barlow J., and Bucknall R. Immunological detection of myeloperoxidase in synovial fluid from patients with rheumatoid arthritis. Biochem J 250 (1988) 81-85
    • (1988) Biochem J , vol.250 , pp. 81-85
    • Edwards, S.W.1    Hughes, V.2    Barlow, J.3    Bucknall, R.4
  • 28
    • 0026467074 scopus 로고
    • Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases
    • Farrell A.J., Blake R.M., Palmer R.M.J., and Moncada S. Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases. Ann Rheum Dis 51 (1992) 1219-1222
    • (1992) Ann Rheum Dis , vol.51 , pp. 1219-1222
    • Farrell, A.J.1    Blake, R.M.2    Palmer, R.M.J.3    Moncada, S.4
  • 29
    • 33749441307 scopus 로고    scopus 로고
    • The role of syndecans in disease and wound healing
    • Fears C.Y., and Woods A. The role of syndecans in disease and wound healing. Matrix Biol 25 (2006) 443-456
    • (2006) Matrix Biol , vol.25 , pp. 443-456
    • Fears, C.Y.1    Woods, A.2
  • 30
    • 0031000743 scopus 로고    scopus 로고
    • Degradation of hyaluronic acid by photosensitized riboflavin in vitro. Modulation of the effect by transition metals, radical quenchers, and metal chelators
    • Frati E., Khatib A.-M., Front P., Panasyuk A., Aprile F., and Mitrovic DR. Degradation of hyaluronic acid by photosensitized riboflavin in vitro. Modulation of the effect by transition metals, radical quenchers, and metal chelators. Free Radic Biol Med 22 (1997) 1139-1144
    • (1997) Free Radic Biol Med , vol.22 , pp. 1139-1144
    • Frati, E.1    Khatib, A.-M.2    Front, P.3    Panasyuk, A.4    Aprile, F.5    Mitrovic, DR.6
  • 31
    • 0031561112 scopus 로고    scopus 로고
    • Purification, cloning, and expression of human plasma hyaluronidase
    • Frost G.I., Csoka A.B., Wong T., and Stern R. Purification, cloning, and expression of human plasma hyaluronidase. Biochem Biophys Res Commun 236 (1997) 10-15
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 10-15
    • Frost, G.I.1    Csoka, A.B.2    Wong, T.3    Stern, R.4
  • 32
    • 29244479725 scopus 로고    scopus 로고
    • Microwave chemistry
    • Galema S.A. Microwave chemistry. Chem Soc Rev 26 (1997) 233-238
    • (1997) Chem Soc Rev , vol.26 , pp. 233-238
    • Galema, S.A.1
  • 33
    • 0037063999 scopus 로고    scopus 로고
    • Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway
    • Ghatak S., Misra S., and Toole B.P. Hyaluronan oligosaccharides inhibit anchorage-independent growth of tumor cells by suppressing the phosphoinositide 3-kinase/Akt cell survival pathway. J Biol Chem 277 (2002) 38013-38020
    • (2002) J Biol Chem , vol.277 , pp. 38013-38020
    • Ghatak, S.1    Misra, S.2    Toole, B.P.3
  • 34
    • 34648868733 scopus 로고
    • Evidence for the heparin nature of the nonspecific hyaluronidase inhibitor in tissue extracts and blood serum
    • Glick D., and Sylven B. Evidence for the heparin nature of the nonspecific hyaluronidase inhibitor in tissue extracts and blood serum. Science 113 (1951) 388-389
    • (1951) Science , vol.113 , pp. 388-389
    • Glick, D.1    Sylven, B.2
  • 35
    • 0020164881 scopus 로고
    • Purification and properties of hyaluronidase from human liver. Differences from and similarities to the testicular enzyme
    • Gold E.W. Purification and properties of hyaluronidase from human liver. Differences from and similarities to the testicular enzyme. Biochem J 205 (1982) 69-74
    • (1982) Biochem J , vol.205 , pp. 69-74
    • Gold, E.W.1
  • 36
    • 0023222221 scopus 로고
    • Bleomycin detectable iron in knee joints from arthritic patients
    • Gutteridge J.M.C. Bleomycin detectable iron in knee joints from arthritic patients. Biochem J 245 (1987) 415-421
    • (1987) Biochem J , vol.245 , pp. 415-421
    • Gutteridge, J.M.C.1
  • 37
    • 0019938797 scopus 로고
    • Production of superoxide, hydrogen peroxide and hydroxyl radicals by phagocytic cells: a cause of chronic inflammatory disease?
    • Halliwell B. Production of superoxide, hydrogen peroxide and hydroxyl radicals by phagocytic cells: a cause of chronic inflammatory disease?. Cell Biol Int Rep 6 (1982) 529-542
    • (1982) Cell Biol Int Rep , vol.6 , pp. 529-542
    • Halliwell, B.1
  • 38
    • 0003536299 scopus 로고
    • Halliwell B., and Gutteridge J.M.C. (Eds), Clarendon Press, Oxford
    • In: Halliwell B., and Gutteridge J.M.C. (Eds). Free radicals in biology and medicine. 2nd ed. (1989), Clarendon Press, Oxford
    • (1989) Free radicals in biology and medicine. 2nd ed.
  • 39
    • 0034961888 scopus 로고    scopus 로고
    • Role of reactive oxygen species in cell signaling pathways
    • Hancock J.T., Desikan R., and Neill S.J. Role of reactive oxygen species in cell signaling pathways. Biochem Soc Trans 29 (2001) 345-350
    • (2001) Biochem Soc Trans , vol.29 , pp. 345-350
    • Hancock, J.T.1    Desikan, R.2    Neill, S.J.3
  • 40
    • 34247154435 scopus 로고    scopus 로고
    • CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and-2
    • Harada H., and Takahashi M. CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and-2. J Biol Chem 282 (2007) 5597-5607
    • (2007) J Biol Chem , vol.282 , pp. 5597-5607
    • Harada, H.1    Takahashi, M.2
  • 41
    • 0029771603 scopus 로고    scopus 로고
    • Direct detection and identification of radicals generated during the hydroxyl radical-induced degradation of hyaluronic acid and related materials
    • Hawkins C.L., and Davies M.J. Direct detection and identification of radicals generated during the hydroxyl radical-induced degradation of hyaluronic acid and related materials. Free Rad Biol Med 21 (1996) 275-290
    • (1996) Free Rad Biol Med , vol.21 , pp. 275-290
    • Hawkins, C.L.1    Davies, M.J.2
  • 42
    • 0031864870 scopus 로고    scopus 로고
    • Degradation of hyaluronic acid, poly- and mono-saccharides, and model compounds by hypochlorite: evidence for radical intermediates and fragmentation
    • Hawkins C.L., and Davies M.J. Degradation of hyaluronic acid, poly- and mono-saccharides, and model compounds by hypochlorite: evidence for radical intermediates and fragmentation. Free Rad Biol Med 21 (1998) 1396-1410
    • (1998) Free Rad Biol Med , vol.21 , pp. 1396-1410
    • Hawkins, C.L.1    Davies, M.J.2
  • 43
    • 0141504018 scopus 로고    scopus 로고
    • The role of reactive oxygen species in homeostasis and degradation of cartilage
    • Henrotin Y.E., Bruckner P., and Pujol J.-P.L. The role of reactive oxygen species in homeostasis and degradation of cartilage. Osteoarth Cartil 11 (2003) 747-755
    • (2003) Osteoarth Cartil , vol.11 , pp. 747-755
    • Henrotin, Y.E.1    Bruckner, P.2    Pujol, J.-P.L.3
  • 44
    • 85007724277 scopus 로고
    • The relationship between spreading factor and hyaluronidase
    • Hobby G.L., Dawson M.H., Meyer K., and Chaffee E. The relationship between spreading factor and hyaluronidase. J Exp Med 73 (1941) 109-123
    • (1941) J Exp Med , vol.73 , pp. 109-123
    • Hobby, G.L.1    Dawson, M.H.2    Meyer, K.3    Chaffee, E.4
  • 45
    • 84913025421 scopus 로고
    • Transglycosylation during the mixed digestion of hyaluronic acid and chondroitin sulfate by testicular hyaluronidase
    • Hoffman P., Meyer K., and Linker A. Transglycosylation during the mixed digestion of hyaluronic acid and chondroitin sulfate by testicular hyaluronidase. J Biol Chem 219 (1956) 653-663
    • (1956) J Biol Chem , vol.219 , pp. 653-663
    • Hoffman, P.1    Meyer, K.2    Linker, A.3
  • 46
    • 0018508775 scopus 로고
    • Spin-lattice-relaxation time-T1 measurements of hyaluronic acid
    • Hofmann H., Schmut O., Sterk H., and Kopp H. Spin-lattice-relaxation time-T1 measurements of hyaluronic acid. Z Naturforsch 34c (1979) 508-511
    • (1979) Z Naturforsch , vol.34 c , pp. 508-511
    • Hofmann, H.1    Schmut, O.2    Sterk, H.3    Kopp, H.4
  • 47
    • 33947211824 scopus 로고    scopus 로고
    • Recombinant human hyaluronidase Hyal-1: insect cells versus Escherichia coli as expression system and identification of low molecular weight inhibitors
    • Hofinger E.S., Spickenreither M., Oschmann J., Bernhardt G., Rudolph R., and Buschauer A. Recombinant human hyaluronidase Hyal-1: insect cells versus Escherichia coli as expression system and identification of low molecular weight inhibitors. Glycobiology 17 (2007) 444-453
    • (2007) Glycobiology , vol.17 , pp. 444-453
    • Hofinger, E.S.1    Spickenreither, M.2    Oschmann, J.3    Bernhardt, G.4    Rudolph, R.5    Buschauer, A.6
  • 48
    • 0026500329 scopus 로고
    • Production of hydroxyl radicals from the simultaneous generation of superoxide and nitric oxide
    • Hogg N., Darley-Usmar V.M., Wilson M.T., and Moncada S. Production of hydroxyl radicals from the simultaneous generation of superoxide and nitric oxide. Biochem J 281 (1992) 419-424
    • (1992) Biochem J , vol.281 , pp. 419-424
    • Hogg, N.1    Darley-Usmar, V.M.2    Wilson, M.T.3    Moncada, S.4
  • 49
    • 0030226886 scopus 로고    scopus 로고
    • Comparison of viscoelastic substances used in phacoemulsification
    • Hutz W.W., Eckhardt H.B., and Kohnen T. Comparison of viscoelastic substances used in phacoemulsification. J Cataract Refract Surg 22 (1996) 955-959
    • (1996) J Cataract Refract Surg , vol.22 , pp. 955-959
    • Hutz, W.W.1    Eckhardt, H.B.2    Kohnen, T.3
  • 50
    • 0010214681 scopus 로고
    • Preparation by chemical degradation of hyaluronic acid, of a series of even- and odd-numbered oligosaccharides having a 2-acetamido-2-deoxy-d-glucose and a d-glucuronic acid residue, respectively, at the reducing end
    • Inoue Y., and Nagasawa K. Preparation by chemical degradation of hyaluronic acid, of a series of even- and odd-numbered oligosaccharides having a 2-acetamido-2-deoxy-d-glucose and a d-glucuronic acid residue, respectively, at the reducing end. Carbohydr Res 141 (1985) 99-110
    • (1985) Carbohydr Res , vol.141 , pp. 99-110
    • Inoue, Y.1    Nagasawa, K.2
  • 51
    • 0032714086 scopus 로고    scopus 로고
    • The reaction of hyaluronic acid and its monomers, glucuronic acid and N-acetylglucosamine, with reactive oxygen species
    • Jahn M., Baynes J.W., and Spiteller G. The reaction of hyaluronic acid and its monomers, glucuronic acid and N-acetylglucosamine, with reactive oxygen species. Carbohydr Res 321 (1999) 228-234
    • (1999) Carbohydr Res , vol.321 , pp. 228-234
    • Jahn, M.1    Baynes, J.W.2    Spiteller, G.3
  • 52
    • 8944238487 scopus 로고
    • Some simple, highly reactive, inorganic chlorine derivatives in aqueous solution
    • Jayson G.G., Parsons B.J., and Swallow A.J. Some simple, highly reactive, inorganic chlorine derivatives in aqueous solution. J Chem Soc Faraday Trans 69 (1973) 1597-1607
    • (1973) J Chem Soc Faraday Trans , vol.69 , pp. 1597-1607
    • Jayson, G.G.1    Parsons, B.J.2    Swallow, A.J.3
  • 53
    • 30244524320 scopus 로고
    • The degradation of hyaluronic acid by methanolysis
    • Jeanloz R.W., and Jeanloz D.A. The degradation of hyaluronic acid by methanolysis. Biochemistry 3 (1964) 121-123
    • (1964) Biochemistry , vol.3 , pp. 121-123
    • Jeanloz, R.W.1    Jeanloz, D.A.2
  • 54
    • 0346445147 scopus 로고    scopus 로고
    • Extracellular virulence factors of Streptococcus pneumoniae
    • Jedrzejas M.J. Extracellular virulence factors of Streptococcus pneumoniae. Front Biosci 9 (2004) 891-914
    • (2004) Front Biosci , vol.9 , pp. 891-914
    • Jedrzejas, M.J.1
  • 55
    • 4744369265 scopus 로고    scopus 로고
    • Synchronized chemoenzymatic synthesis of monodisperse hyaluronan polymers
    • Jing W., and DeAngelis P.L. Synchronized chemoenzymatic synthesis of monodisperse hyaluronan polymers. J Biol Chem 279 (2004) 42345-42349
    • (2004) J Biol Chem , vol.279 , pp. 42345-42349
    • Jing, W.1    DeAngelis, P.L.2
  • 56
    • 0141527419 scopus 로고    scopus 로고
    • Interleukin-12 release from macrophages by hyaluronan, chondroitin sulfate A and chondroitin sulfate C oligosaccharides
    • Jobe K.L., Odman-Ghazi S.O., Whalen M.M., and Vercruysse K.P. Interleukin-12 release from macrophages by hyaluronan, chondroitin sulfate A and chondroitin sulfate C oligosaccharides. Immunol Lett 89 (2003) 99-109
    • (2003) Immunol Lett , vol.89 , pp. 99-109
    • Jobe, K.L.1    Odman-Ghazi, S.O.2    Whalen, M.M.3    Vercruysse, K.P.4
  • 57
    • 33747756533 scopus 로고    scopus 로고
    • Elastogenic effects of exogenous hyaluronan oligosaccharides on vascular smooth muscle cells
    • Joddar B., and Ramamurthi A. Elastogenic effects of exogenous hyaluronan oligosaccharides on vascular smooth muscle cells. Biomaterials 27 (2006) 5698-5707
    • (2006) Biomaterials , vol.27 , pp. 5698-5707
    • Joddar, B.1    Ramamurthi, A.2
  • 58
    • 0004408525 scopus 로고
    • The sedimentation behaviour of mixtures of hyaluronic acid and albumin in the ultracentrifuge
    • Johnston J.P. The sedimentation behaviour of mixtures of hyaluronic acid and albumin in the ultracentrifuge. Biochem J 59 (1955) 620-626
    • (1955) Biochem J , vol.59 , pp. 620-626
    • Johnston, J.P.1
  • 59
    • 0024464184 scopus 로고
    • Heparin inhibits mammalian, but not leech, hyaluronidase
    • Jones C.P., and Sawyer R.T. Heparin inhibits mammalian, but not leech, hyaluronidase. Thromb Res 55 (1989) 791-796
    • (1989) Thromb Res , vol.55 , pp. 791-796
    • Jones, C.P.1    Sawyer, R.T.2
  • 61
    • 0025264362 scopus 로고
    • Action of biologically-relevant oxidizing species upon uric acid. Identification of uric acid oxidation products
    • Kaur H., and Halliwell B. Action of biologically-relevant oxidizing species upon uric acid. Identification of uric acid oxidation products. Chem Biol Interact 73 (1990) 235-247
    • (1990) Chem Biol Interact , vol.73 , pp. 235-247
    • Kaur, H.1    Halliwell, B.2
  • 62
    • 29144431510 scopus 로고    scopus 로고
    • Identification of a hyaluronidase, Hyal5, involved in penetration of mouse sperm through cumulus mass
    • Kim E., Baba D., Kimura M., Yamashita M., Kashiwabara S., and Baba T. Identification of a hyaluronidase, Hyal5, involved in penetration of mouse sperm through cumulus mass. Proc Natl Acad Sci U S A 102 (2005) 18028-18033
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18028-18033
    • Kim, E.1    Baba, D.2    Kimura, M.3    Yamashita, M.4    Kashiwabara, S.5    Baba, T.6
  • 63
    • 0003156755 scopus 로고
    • β-Eliminative degradation of carbohydrates containing uronic acid residues
    • Kiss J. β-Eliminative degradation of carbohydrates containing uronic acid residues. Adv Carbohydr Chem Biochem 29 (1974) 229-303
    • (1974) Adv Carbohydr Chem Biochem , vol.29 , pp. 229-303
    • Kiss, J.1
  • 64
    • 33845661145 scopus 로고    scopus 로고
    • Hyaluronic acid: a natural biopolymer with a broad range of biomedical and industrial applications
    • Kogan G., Soltes L., Stern R., and Gemeiner P. Hyaluronic acid: a natural biopolymer with a broad range of biomedical and industrial applications. Biotechnol Lett 29 (2007) 17-25
    • (2007) Biotechnol Lett , vol.29 , pp. 17-25
    • Kogan, G.1    Soltes, L.2    Stern, R.3    Gemeiner, P.4
  • 65
    • 34648865947 scopus 로고    scopus 로고
    • Kogan G, Šoltés L, Stern R, Schiller J, Mendichi R. Hyaluronic acid: its function and degradation in in vivo systems. In: Atta-ur-Rahman, editor. Studies in Natural Products Chemistry, Vol. 35, Bioactive Natural Products, Part D., Amsterdam: Elsevier, in press.
  • 66
    • 0028235362 scopus 로고
    • Thermodynamic considerations of the formation of reactive species from hypochlorite, superoxide and nitrogen monoxide - could nitrosyl chloride be produced by neutrophils and macrophages?
    • Koppenol WH. Thermodynamic considerations of the formation of reactive species from hypochlorite, superoxide and nitrogen monoxide - could nitrosyl chloride be produced by neutrophils and macrophages?. FEBS Lett 347 (1994) 5-8
    • (1994) FEBS Lett , vol.347 , pp. 5-8
    • Koppenol, WH.1
  • 67
    • 0029079957 scopus 로고
    • Hyaluronidases-a group of neglected enzymes
    • Kreil G. Hyaluronidases-a group of neglected enzymes. Protein Sci 4 (1995) 1666-1669
    • (1995) Protein Sci , vol.4 , pp. 1666-1669
    • Kreil, G.1
  • 69
    • 0026237128 scopus 로고
    • Photodegradation of hyaluronic acid: EPR and size exclusion chromatography study
    • Lapčík Jr. L., Chabreček P., and Staško A. Photodegradation of hyaluronic acid: EPR and size exclusion chromatography study. Biopolymers 31 (1991) 1429-1435
    • (1991) Biopolymers , vol.31 , pp. 1429-1435
    • Lapčík Jr., L.1    Chabreček, P.2    Staško, A.3
  • 71
    • 0022996075 scopus 로고
    • Human fibrinogen specifically binds hyaluronic acid
    • LeBoeuf R.D., Raja R.H., Fuller G.M., and Weigel P.H. Human fibrinogen specifically binds hyaluronic acid. J Biol Chem 261 (1986) 12586-12592
    • (1986) J Biol Chem , vol.261 , pp. 12586-12592
    • LeBoeuf, R.D.1    Raja, R.H.2    Fuller, G.M.3    Weigel, P.H.4
  • 72
    • 0035798695 scopus 로고    scopus 로고
    • Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase
    • Li S., and Jedrzejas M.J. Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase. J Biol Chem 276 (2001) 41407-41416
    • (2001) J Biol Chem , vol.276 , pp. 41407-41416
    • Li, S.1    Jedrzejas, M.J.2
  • 74
    • 0034653873 scopus 로고    scopus 로고
    • Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase
    • Li S., Kelly S.J., Lamani E., Ferraroni M., and Jedrzejas M.J. Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. EMBO J 19 (2000) 1228-1240
    • (2000) EMBO J , vol.19 , pp. 1228-1240
    • Li, S.1    Kelly, S.J.2    Lamani, E.3    Ferraroni, M.4    Jedrzejas, M.J.5
  • 75
    • 0000843601 scopus 로고
    • The production of hyaluronate oligosaccharides by leech hyaluronidase and alkali
    • Linker A., Meyer K., and Hoffman P. The production of hyaluronate oligosaccharides by leech hyaluronidase and alkali. J Biol Chem 235 (1960) 924-927
    • (1960) J Biol Chem , vol.235 , pp. 924-927
    • Linker, A.1    Meyer, K.2    Hoffman, P.3
  • 76
    • 16644390137 scopus 로고    scopus 로고
    • Inhibition of hyaluronan degradation by dextran sulphate facilitates characterization of hyaluronan synthesis: an in vitro and in vivo study
    • Lishanti U., Brownlee G.R., Stern R., and Brown T.J. Inhibition of hyaluronan degradation by dextran sulphate facilitates characterization of hyaluronan synthesis: an in vitro and in vivo study. Glycoconj J 20 (2004) 461-471
    • (2004) Glycoconj J , vol.20 , pp. 461-471
    • Lishanti, U.1    Brownlee, G.R.2    Stern, R.3    Brown, T.J.4
  • 77
    • 0028519243 scopus 로고
    • Thermal stability of sodium hyaluronate in aqueous solution
    • Lowry K.M., and Beavers E.M. Thermal stability of sodium hyaluronate in aqueous solution. J Biomed Mater Res 28 (1994) 1239-1244
    • (1994) J Biomed Mater Res , vol.28 , pp. 1239-1244
    • Lowry, K.M.1    Beavers, E.M.2
  • 78
    • 0000841594 scopus 로고
    • Use of size exclusion chromatography to study the protective effect of radical scavengers on oxygen free-radical-induced degradation of hyaluronic acid
    • Mendichi R., Audisio G., Maffei-Facino R., Carini M., Giacometti-Schieroni A., and Saibene L. Use of size exclusion chromatography to study the protective effect of radical scavengers on oxygen free-radical-induced degradation of hyaluronic acid. Int J Polym Anal Charact 1 (1995) 365-371
    • (1995) Int J Polym Anal Charact , vol.1 , pp. 365-371
    • Mendichi, R.1    Audisio, G.2    Maffei-Facino, R.3    Carini, M.4    Giacometti-Schieroni, A.5    Saibene, L.6
  • 79
    • 77956924584 scopus 로고
    • Hyaluronidases
    • Boyer P.D. (Ed), Academic Press, New York
    • Meyer K. Hyaluronidases. In: Boyer P.D. (Ed). The enzymes vol. V (1971), Academic Press, New York 307-320
    • (1971) The enzymes , vol.V , pp. 307-320
    • Meyer, K.1
  • 80
    • 34648858579 scopus 로고    scopus 로고
    • Medicinal uses of modified hyaluronate
    • Garg H.G., and Hales C.A. (Eds), Elsevier, Amsterdam
    • Miller R.J., and Avila L.Z. Medicinal uses of modified hyaluronate. In: Garg H.G., and Hales C.A. (Eds). Chemistry and biology of hyaluronan (2004), Elsevier, Amsterdam 505-528
    • (2004) Chemistry and biology of hyaluronan , pp. 505-528
    • Miller, R.J.1    Avila, L.Z.2
  • 81
    • 0036154534 scopus 로고    scopus 로고
    • Inhibitors of the hyaluronidases
    • Mio K., and Stern R. Inhibitors of the hyaluronidases. Matrix Biol 21 (2002) 31-37
    • (2002) Matrix Biol , vol.21 , pp. 31-37
    • Mio, K.1    Stern, R.2
  • 82
    • 0034693153 scopus 로고    scopus 로고
    • Evidence that the serum inhibitor of hyaluronidase may be a member of the inter-alpha-inhibitor family
    • Mio K., Carrette O., Maibach H.I., and Stern R. Evidence that the serum inhibitor of hyaluronidase may be a member of the inter-alpha-inhibitor family. J Biol Chem 275 (2000) 32413-32421
    • (2000) J Biol Chem , vol.275 , pp. 32413-32421
    • Mio, K.1    Carrette, O.2    Maibach, H.I.3    Stern, R.4
  • 83
    • 0023652716 scopus 로고
    • The reactivity of various free radicals with hyaluronic acid: steady-state and pulse radiolysis studies
    • Myint P., Deeble D.J., Beaumont P.C., Blake S.M., and Phillips G.O. The reactivity of various free radicals with hyaluronic acid: steady-state and pulse radiolysis studies. Biochim. Biophys. Acta 925 (1987) 194-202
    • (1987) Biochim. Biophys. Acta , vol.925 , pp. 194-202
    • Myint, P.1    Deeble, D.J.2    Beaumont, P.C.3    Blake, S.M.4    Phillips, G.O.5
  • 84
    • 0037172177 scopus 로고    scopus 로고
    • The rate constant of the reaction of superoxide with nitrogen monoxide: approaching the diffusion limit
    • Nauser T., and Koppenol J. The rate constant of the reaction of superoxide with nitrogen monoxide: approaching the diffusion limit. J Phys Chem A 106 (2002) 4084-4086
    • (2002) J Phys Chem A , vol.106 , pp. 4084-4086
    • Nauser, T.1    Koppenol, J.2
  • 85
    • 2642626482 scopus 로고
    • Interaction of hyaluronic acid and bovine plasma albumin
    • Niedermeier W., Gramling E., and Pigman W. Interaction of hyaluronic acid and bovine plasma albumin. Biochim Biophys Acta 130 (1966) 143-149
    • (1966) Biochim Biophys Acta , vol.130 , pp. 143-149
    • Niedermeier, W.1    Gramling, E.2    Pigman, W.3
  • 86
    • 0018813942 scopus 로고
    • Equilibrium-binding studies of pig laryngeal cartilage proteoglycans with hyaluronate oligosaccharide fractions
    • Nieduszynski I.A., Sheehan J.K., Phelps C.F., Hardingham T.E., and Muir H. Equilibrium-binding studies of pig laryngeal cartilage proteoglycans with hyaluronate oligosaccharide fractions. Biochem J 185 (1980) 107-114
    • (1980) Biochem J , vol.185 , pp. 107-114
    • Nieduszynski, I.A.1    Sheehan, J.K.2    Phelps, C.F.3    Hardingham, T.E.4    Muir, H.5
  • 87
    • 0036154206 scopus 로고    scopus 로고
    • Hyaluronan and its catabolic products in tissue injury and repair
    • Noble P.W. Hyaluronan and its catabolic products in tissue injury and repair. Matrix Biol 21 (2002) 25-29
    • (2002) Matrix Biol , vol.21 , pp. 25-29
    • Noble, P.W.1
  • 89
    • 0037345228 scopus 로고    scopus 로고
    • Comparative characterization of bovine testicular hyaluronidase and a hyaluronate lyase from Streptococcus agalactiae in pharmaceutical preparations
    • Oettl M., Hoechstetter J., Asen I., Bernhardt G., and Buschauer A. Comparative characterization of bovine testicular hyaluronidase and a hyaluronate lyase from Streptococcus agalactiae in pharmaceutical preparations. Eur J Pharm Sci 18 (2003) 267-277
    • (2003) Eur J Pharm Sci , vol.18 , pp. 267-277
    • Oettl, M.1    Hoechstetter, J.2    Asen, I.3    Bernhardt, G.4    Buschauer, A.5
  • 90
    • 14944364770 scopus 로고    scopus 로고
    • Hyaluronan oligosaccharide-induced activation of transcription factors in bovine articular chondrocytes
    • Ohno S., Im H.J., Knudson C.B., and Knudson W. Hyaluronan oligosaccharide-induced activation of transcription factors in bovine articular chondrocytes. Arthritis Rheum 52 (2005) 800-809
    • (2005) Arthritis Rheum , vol.52 , pp. 800-809
    • Ohno, S.1    Im, H.J.2    Knudson, C.B.3    Knudson, W.4
  • 91
    • 33644649149 scopus 로고    scopus 로고
    • Induction of MMP-3 by hyaluronan oligosaccharides in temporomandibular joint chondrocytes
    • Ohno S., Ohno-Nakahara M., Knudson C.B., and Knudson W. Induction of MMP-3 by hyaluronan oligosaccharides in temporomandibular joint chondrocytes. J Dent Res 84 (2005) 1005-1009
    • (2005) J Dent Res , vol.84 , pp. 1005-1009
    • Ohno, S.1    Ohno-Nakahara, M.2    Knudson, C.B.3    Knudson, W.4
  • 92
    • 0014953621 scopus 로고
    • Novel hyaluronidase from streptomyces
    • Ohya T., and Kaneko Y. Novel hyaluronidase from streptomyces. Biochim Biophys Acta 198 (1970) 607-609
    • (1970) Biochim Biophys Acta , vol.198 , pp. 607-609
    • Ohya, T.1    Kaneko, Y.2
  • 93
    • 0343923373 scopus 로고    scopus 로고
    • High-molecular-weight hyaluronan - a valuable tool in testing the antioxidative activity of amphiphilic drugs stobadine and vinpocetine
    • Orviský E., Šoltés L., and Stančíková M. High-molecular-weight hyaluronan - a valuable tool in testing the antioxidative activity of amphiphilic drugs stobadine and vinpocetine. J Pharm Biomed Anal 16 (1997) 419-424
    • (1997) J Pharm Biomed Anal , vol.16 , pp. 419-424
    • Orviský, E.1    Šoltés, L.2    Stančíková, M.3
  • 94
    • 0013364914 scopus 로고    scopus 로고
    • Comparison of the reactivity of different oxidative species (ROS) towards hyaluronan
    • Kennedy J.F., Phillips G.O., Williams P.A., and Hascall V.C. (Eds), Woodhead Publishing Ltd, Cambridge
    • Parsons B.J., Al-Assaf S., Navaratnam S., and Phillips G.O. Comparison of the reactivity of different oxidative species (ROS) towards hyaluronan. In: Kennedy J.F., Phillips G.O., Williams P.A., and Hascall V.C. (Eds). Hyaluronan: Chemical, Biochemical and Biological Aspects vol. 1 (2002), Woodhead Publishing Ltd, Cambridge 141-150
    • (2002) Hyaluronan: Chemical, Biochemical and Biological Aspects , vol.1 , pp. 141-150
    • Parsons, B.J.1    Al-Assaf, S.2    Navaratnam, S.3    Phillips, G.O.4
  • 95
    • 34548462561 scopus 로고
    • Depolymerization of hyaluronic acid by the ORD reaction
    • Pigman W., Rizvi S., and Holley H.L. Depolymerization of hyaluronic acid by the ORD reaction. Arthritis Rheum 4 (1961) 240-452
    • (1961) Arthritis Rheum , vol.4 , pp. 240-452
    • Pigman, W.1    Rizvi, S.2    Holley, H.L.3
  • 96
    • 0034674165 scopus 로고    scopus 로고
    • Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 Å resolution
    • Ponnuraj K., and Jedrzejas M.J. Mechanism of hyaluronan binding and degradation: structure of Streptococcus pneumoniae hyaluronate lyase in complex with hyaluronic acid disaccharide at 1.7 Å resolution. J Mol Biol 299 (2000) 885-895
    • (2000) J Mol Biol , vol.299 , pp. 885-895
    • Ponnuraj, K.1    Jedrzejas, M.J.2
  • 97
    • 0030801695 scopus 로고    scopus 로고
    • Effects of oxygen-derived free radicals on the molecular weight and the polydispersity of hyaluronan solutions
    • Praest B.M., Greiling H., and Kock R. Effects of oxygen-derived free radicals on the molecular weight and the polydispersity of hyaluronan solutions. Carbohydr Res 303 (1997) 153-157
    • (1997) Carbohydr Res , vol.303 , pp. 153-157
    • Praest, B.M.1    Greiling, H.2    Kock, R.3
  • 98
    • 0035836625 scopus 로고    scopus 로고
    • Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation
    • Rai S.K., Duh F.M., Vigdorovich V., Danilkovitch-Miagkova A., Lerman I., and Miller A.D. Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation. Proc Natl Acad Sci U S A 98 (2001) 4443-4448
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4443-4448
    • Rai, S.K.1    Duh, F.M.2    Vigdorovich, V.3    Danilkovitch-Miagkova, A.4    Lerman, I.5    Miller, A.D.6
  • 99
    • 0000275716 scopus 로고
    • Light scattering power of randomly cut random coils with application to the determination of depolymerization rates
    • Reed C.E., and Reed W.F. Light scattering power of randomly cut random coils with application to the determination of depolymerization rates. J Chem Phys 91 (1989) 7193-7199
    • (1989) J Chem Phys , vol.91 , pp. 7193-7199
    • Reed, C.E.1    Reed, W.F.2
  • 100
    • 0024330163 scopus 로고
    • The effects of pH on hyaluronate as observed by light scattering
    • Reed C.E., Xiao L., and Reed W.F. The effects of pH on hyaluronate as observed by light scattering. Biopolymers 28 (1989) 1981-2000
    • (1989) Biopolymers , vol.28 , pp. 1981-2000
    • Reed, C.E.1    Xiao, L.2    Reed, W.F.3
  • 101
    • 33644615557 scopus 로고    scopus 로고
    • Polysaccharide fragmentation induced by hydroxyl radicals and hypochlorite
    • Kennedy J.F., Phillips G.O., Williams P.A., and Hascall V.C. (Eds), Woodhead Publ., Ltd, Cambridge
    • Rees M.D., Hawkins C.L., and Davies M.J. Polysaccharide fragmentation induced by hydroxyl radicals and hypochlorite. In: Kennedy J.F., Phillips G.O., Williams P.A., and Hascall V.C. (Eds). Hyaluronan: chemical, biochemical and biological aspects vol. 1 (2002), Woodhead Publ., Ltd, Cambridge 151-160
    • (2002) Hyaluronan: chemical, biochemical and biological aspects , vol.1 , pp. 151-160
    • Rees, M.D.1    Hawkins, C.L.2    Davies, M.J.3
  • 102
    • 0242407243 scopus 로고    scopus 로고
    • Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation
    • Rees M.D., Hawkins C.L., and Davies M.J. Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation. J Am Chem Soc 125 (2003) 13719-13733
    • (2003) J Am Chem Soc , vol.125 , pp. 13719-13733
    • Rees, M.D.1    Hawkins, C.L.2    Davies, M.J.3
  • 103
    • 3142736372 scopus 로고    scopus 로고
    • Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates
    • Rees M.D., Hawkins C.L., and Davies M.J. Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates. Biochem J 381 (2004) 175-184
    • (2004) Biochem J , vol.381 , pp. 175-184
    • Rees, M.D.1    Hawkins, C.L.2    Davies, M.J.3
  • 105
    • 0032113092 scopus 로고    scopus 로고
    • Review: NO-synthase and nitrite-reductase components of nitric oxide cycle
    • Reutov V.P., and Sorokina E.G. Review: NO-synthase and nitrite-reductase components of nitric oxide cycle. Biochemistry (Moscow) 63 (1998) 874-884
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 874-884
    • Reutov, V.P.1    Sorokina, E.G.2
  • 106
    • 0347379849 scopus 로고    scopus 로고
    • Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action
    • Rigden D.J., and Jedrzejas M.J. Structures of Streptococcus pneumoniae hyaluronate lyase in complex with chondroitin and chondroitin sulfate disaccharides. Insights into specificity and mechanism of action. J Biol Chem 278 (2003) 50596-50606
    • (2003) J Biol Chem , vol.278 , pp. 50596-50606
    • Rigden, D.J.1    Jedrzejas, M.J.2
  • 107
    • 0027322874 scopus 로고
    • Angiogenic oligosaccharides of hyaluronan enhance the production of collagens by endothelial cells
    • Rooney P., Wang M., Kumar P., and Kumar S. Angiogenic oligosaccharides of hyaluronan enhance the production of collagens by endothelial cells. J Cell Sci 105 (1993) 213-218
    • (1993) J Cell Sci , vol.105 , pp. 213-218
    • Rooney, P.1    Wang, M.2    Kumar, P.3    Kumar, S.4
  • 108
    • 24944528735 scopus 로고    scopus 로고
    • Sulphated oligosaccharides as inhibitors of hyaluronidases from bovine testis, bee venom and Streptococcus agalactiae
    • Salmen S., Hoechstetter J., Kasbauer C., Paper DH., Bernhardt G., and Buschauer A. Sulphated oligosaccharides as inhibitors of hyaluronidases from bovine testis, bee venom and Streptococcus agalactiae. Planta Med 71 (2005) 727-732
    • (2005) Planta Med , vol.71 , pp. 727-732
    • Salmen, S.1    Hoechstetter, J.2    Kasbauer, C.3    Paper, DH.4    Bernhardt, G.5    Buschauer, A.6
  • 109
    • 0028034363 scopus 로고
    • Application of angiogenic oligosaccharides of hyaluronan increases blood vessel numbers in rat skin
    • Sattar A., Rooney P., Kumar S., Pye D., West DC., Scott I., et al. Application of angiogenic oligosaccharides of hyaluronan increases blood vessel numbers in rat skin. J Invest Dermatol 103 (1994) 576-579
    • (1994) J Invest Dermatol , vol.103 , pp. 576-579
    • Sattar, A.1    Rooney, P.2    Kumar, S.3    Pye, D.4    West, DC.5    Scott, I.6
  • 110
    • 0028390411 scopus 로고
    • The action of hypochlorous acid on the polymeric components of cartilage
    • Schiller J., Arnhold J., Grunder W., and Arnold K. The action of hypochlorous acid on the polymeric components of cartilage. Biol Chem Hoppe-Seyler 375 (1994) 167-172
    • (1994) Biol Chem Hoppe-Seyler , vol.375 , pp. 167-172
    • Schiller, J.1    Arnhold, J.2    Grunder, W.3    Arnold, K.4
  • 111
    • 0028811374 scopus 로고
    • NMR studies on the action of hypochlorous acid on native pig articular cartilage
    • Schiller J., Arnhold J., and Arnold K. NMR studies on the action of hypochlorous acid on native pig articular cartilage. Eur J Biochem 233 (1995) 7672-7676
    • (1995) Eur J Biochem , vol.233 , pp. 7672-7676
    • Schiller, J.1    Arnhold, J.2    Arnold, K.3
  • 112
    • 14044272769 scopus 로고    scopus 로고
    • Expression and purification of functionally active hyaluronan-binding domains from human cartilage link protein, aggrecan and versican: formation of ternary complexes with defined hyaluronan oligosaccharides
    • Seyfried N.T., McVey G.F., Almond A., Mahoney D.J., Dudhia J., and Day A.J. Expression and purification of functionally active hyaluronan-binding domains from human cartilage link protein, aggrecan and versican: formation of ternary complexes with defined hyaluronan oligosaccharides. J Biol Chem 280 (2005) 5435-5448
    • (2005) J Biol Chem , vol.280 , pp. 5435-5448
    • Seyfried, N.T.1    McVey, G.F.2    Almond, A.3    Mahoney, D.J.4    Dudhia, J.5    Day, A.J.6
  • 113
    • 0019179985 scopus 로고
    • Degradation process of hyaluronic acid by Streptomyces hyaluronidase
    • Shimada E., and Matsumura G. Degradation process of hyaluronic acid by Streptomyces hyaluronidase. J Biochem (Tokyo) 88 (1980) 1015-1023
    • (1980) J Biochem (Tokyo) , vol.88 , pp. 1015-1023
    • Shimada, E.1    Matsumura, G.2
  • 114
    • 84940868914 scopus 로고    scopus 로고
    • Therapeutic biomaterials from chemically modified hyaluronan
    • Garg H.G., and Hales C.A. (Eds), Elsevier, Amsterdam
    • Shu X.Z., and Prestwich GD. Therapeutic biomaterials from chemically modified hyaluronan. In: Garg H.G., and Hales C.A. (Eds). Chemistry and biology of hyaluronan (2004), Elsevier, Amsterdam 475-504
    • (2004) Chemistry and biology of hyaluronan , pp. 475-504
    • Shu, X.Z.1    Prestwich, GD.2
  • 115
    • 0027911127 scopus 로고
    • 13C NMR study of a repeating disaccharide of hyaluronan: the effects of temperature and counterion type
    • 13C NMR study of a repeating disaccharide of hyaluronan: the effects of temperature and counterion type. Carbohydr Res 242 (1993) 29-51
    • (1993) Carbohydr Res , vol.242 , pp. 29-51
    • Siciňska, W.1    Adams, B.2    Lerner, L.3
  • 116
    • 0028763770 scopus 로고
    • Synthesis of hyaluronic acid-related di-, tri-, and tetra-saccharides having an N-acetylglucosamine residue at the reducing end
    • Slaghek T.M., Nakahara Y., Ogawa T., Kamerling J.P., and Vliegenthart J.F.G. Synthesis of hyaluronic acid-related di-, tri-, and tetra-saccharides having an N-acetylglucosamine residue at the reducing end. Carbohydr Res 255 (1994) 61-85
    • (1994) Carbohydr Res , vol.255 , pp. 61-85
    • Slaghek, T.M.1    Nakahara, Y.2    Ogawa, T.3    Kamerling, J.P.4    Vliegenthart, J.F.G.5
  • 117
    • 0037174957 scopus 로고    scopus 로고
    • Angiogenic oligosaccharides of hyaluronan induce multiple signaling pathways affecting vascular endothelial cell mitogenic and wound healing responses
    • Slevin M., Kumar S., and Gaffney J. Angiogenic oligosaccharides of hyaluronan induce multiple signaling pathways affecting vascular endothelial cell mitogenic and wound healing responses. J Biol Chem 277 (2002) 41046-41059
    • (2002) J Biol Chem , vol.277 , pp. 41046-41059
    • Slevin, M.1    Kumar, S.2    Gaffney, J.3
  • 118
    • 0029879975 scopus 로고    scopus 로고
    • Insight into the distribution of molecular weights and higher-order structure of hyaluronans and some β-(1 → 3)-glucans by size exclusion chromatography
    • Šoltés L., Mislovičová D., and Sebille B. Insight into the distribution of molecular weights and higher-order structure of hyaluronans and some β-(1 → 3)-glucans by size exclusion chromatography. Biomed Chromatogr 10 (1996) 53-59
    • (1996) Biomed Chromatogr , vol.10 , pp. 53-59
    • Šoltés, L.1    Mislovičová, D.2    Sebille, B.3
  • 119
    • 0034962722 scopus 로고    scopus 로고
    • Radical degradation of high molecular weight hyaluronan: Inhibition of the reaction by ibuprofen enantiomers
    • Šoltés L., Lath D., Mendichi R., and Bystrický P. Radical degradation of high molecular weight hyaluronan: Inhibition of the reaction by ibuprofen enantiomers. Meth Find Exp Clin Pharmacol 23 (2001) 65-71
    • (2001) Meth Find Exp Clin Pharmacol , vol.23 , pp. 65-71
    • Šoltés, L.1    Lath, D.2    Mendichi, R.3    Bystrický, P.4
  • 120
    • 26044469374 scopus 로고    scopus 로고
    • Contribution of oxidative-reductive reactions to high-molecular-weight hyaluronan catabolism
    • Šoltés L., Stankovská M., Kogan G., Gemeiner P., and Stern R. Contribution of oxidative-reductive reactions to high-molecular-weight hyaluronan catabolism. Chem Biodivers 2 (2005) 1242-1245
    • (2005) Chem Biodivers , vol.2 , pp. 1242-1245
    • Šoltés, L.1    Stankovská, M.2    Kogan, G.3    Gemeiner, P.4    Stern, R.5
  • 121
    • 33644631285 scopus 로고    scopus 로고
    • Degradation of high molecular-weight hyaluronan by hydrogen peroxide in the presence of cupric ions
    • Šoltés L., Brezová V., Stankovská M., Kogan G., and Gemeiner P. Degradation of high molecular-weight hyaluronan by hydrogen peroxide in the presence of cupric ions. Carbohydr Res 341 (2006) 639-644
    • (2006) Carbohydr Res , vol.341 , pp. 639-644
    • Šoltés, L.1    Brezová, V.2    Stankovská, M.3    Kogan, G.4    Gemeiner, P.5
  • 122
    • 33750634304 scopus 로고    scopus 로고
    • Hyaluronan degradation by copper(II) chloride and ascorbate: rotational viscometric, EPR spin-trapping, and MALDI-TOF mass spectrometric investigation
    • Šoltés L., Stankovská M., Brezová V., Schiller J., Arnhold J., Kogan G., and Gemeiner P. Hyaluronan degradation by copper(II) chloride and ascorbate: rotational viscometric, EPR spin-trapping, and MALDI-TOF mass spectrometric investigation. Carbohydr Res 341 (2006) 2826-2834
    • (2006) Carbohydr Res , vol.341 , pp. 2826-2834
    • Šoltés, L.1    Stankovská, M.2    Brezová, V.3    Schiller, J.4    Arnhold, J.5    Kogan, G.6    Gemeiner, P.7
  • 123
    • 34047268579 scopus 로고    scopus 로고
    • Solution properties of high-molar-mass hyaluronans: the biopolymer degradation by ascorbate
    • Šoltés L., Valachová K., Mendichi R., Kogan G., Arnhold J., and Gemeiner P. Solution properties of high-molar-mass hyaluronans: the biopolymer degradation by ascorbate. Carbohydr Res 342 (2007) 1071-1077
    • (2007) Carbohydr Res , vol.342 , pp. 1071-1077
    • Šoltés, L.1    Valachová, K.2    Mendichi, R.3    Kogan, G.4    Arnhold, J.5    Gemeiner, P.6
  • 124
    • 33748325735 scopus 로고    scopus 로고
    • Novel 6-O-acylated vitamin C derivatives as hyaluronidase inhibitors with selectivity for bacterial lyases
    • Spickenreither M., Braun S., Bernhardt G., Dove S., and Buschauer A. Novel 6-O-acylated vitamin C derivatives as hyaluronidase inhibitors with selectivity for bacterial lyases. Bioorg Med Chem Lett 16 (2006) 5313-5316
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 5313-5316
    • Spickenreither, M.1    Braun, S.2    Bernhardt, G.3    Dove, S.4    Buschauer, A.5
  • 125
    • 33644613207 scopus 로고    scopus 로고
    • Degradation of high-molecular-weight hyaluronan: a rotational viscometry study
    • Stankovská M., Šoltés L., Lath D., Vikartovská A., Gemeiner P., Kogan G., et al. Degradation of high-molecular-weight hyaluronan: a rotational viscometry study. Biologia 60 17 (2005) 149-152
    • (2005) Biologia , vol.60 , Issue.17 , pp. 149-152
    • Stankovská, M.1    Šoltés, L.2    Lath, D.3    Vikartovská, A.4    Gemeiner, P.5    Kogan, G.6
  • 126
    • 0344668719 scopus 로고    scopus 로고
    • Devising a pathway for hyaluronan catabolism. Are we there yet?
    • Stern R. Devising a pathway for hyaluronan catabolism. Are we there yet?. Glycobiology 13 (2003) 105-115
    • (2003) Glycobiology , vol.13 , pp. 105-115
    • Stern, R.1
  • 127
    • 34648872023 scopus 로고    scopus 로고
    • A new metabolic pathway: hyaluronan catabolism
    • Stern R. A new metabolic pathway: hyaluronan catabolism. Eur J Cell Biol 83 (2004) 1-9
    • (2004) Eur J Cell Biol , vol.83 , pp. 1-9
    • Stern, R.1
  • 128
    • 33645372800 scopus 로고    scopus 로고
    • Hyaluronidases: their genomics, structures, and mechanisms of action
    • Stern R., and Jedrzejas M.J. Hyaluronidases: their genomics, structures, and mechanisms of action. Chem Rev 106 (2006) 818-839
    • (2006) Chem Rev , vol.106 , pp. 818-839
    • Stern, R.1    Jedrzejas, M.J.2
  • 129
    • 33746040501 scopus 로고    scopus 로고
    • Hyaluronan fragments: an information-rich system
    • Stern R., Asari A.A., and Sugahara K.N. Hyaluronan fragments: an information-rich system. Eur J Cell Biol 85 (2006) 699-715
    • (2006) Eur J Cell Biol , vol.85 , pp. 699-715
    • Stern, R.1    Asari, A.A.2    Sugahara, K.N.3
  • 131
    • 0037162548 scopus 로고    scopus 로고
    • Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol
    • Suzuki T., Yano K., Sugimoto S., Kitajima K., Lennarz WJ., Inoue S., et al. Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol. Proc Natl Acad Sci U S A 99 (2002) 9691-9696
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9691-9696
    • Suzuki, T.1    Yano, K.2    Sugimoto, S.3    Kitajima, K.4    Lennarz, WJ.5    Inoue, S.6
  • 132
    • 10744221425 scopus 로고    scopus 로고
    • Structure of the regulatory hyaluronan binding domain in the inflammatory leukocyte homing receptor CD44
    • Teriete P., Banerji S., Noble M., Blundell C.D., Wright A.J., Pickford A.R., et al. Structure of the regulatory hyaluronan binding domain in the inflammatory leukocyte homing receptor CD44. Mol Cell 13 (2004) 483-496
    • (2004) Mol Cell , vol.13 , pp. 483-496
    • Teriete, P.1    Banerji, S.2    Noble, M.3    Blundell, C.D.4    Wright, A.J.5    Pickford, A.R.6
  • 133
    • 0034663808 scopus 로고    scopus 로고
    • Oligosaccharides of hyaluronan are potent activators of dendritic cells
    • Termeer C., Hennies J., Voith U., Ahrens T., Weiss J.M., Prehm P., et al. Oligosaccharides of hyaluronan are potent activators of dendritic cells. J Immunol 165 (2000) 1863-1870
    • (2000) J Immunol , vol.165 , pp. 1863-1870
    • Termeer, C.1    Hennies, J.2    Voith, U.3    Ahrens, T.4    Weiss, J.M.5    Prehm, P.6
  • 134
    • 16244380777 scopus 로고    scopus 로고
    • Syndecans: new kids on the signaling block
    • Tkachenko E., Rhodes J.M., and Simons M. Syndecans: new kids on the signaling block. Circ Res 96 (2005) 488-500
    • (2005) Circ Res , vol.96 , pp. 488-500
    • Tkachenko, E.1    Rhodes, J.M.2    Simons, M.3
  • 135
    • 0029232537 scopus 로고
    • Hydrolytic degradation of hyaluronic acid
    • Tokita Y., and Okamoto A. Hydrolytic degradation of hyaluronic acid. Polym Degrad Stab 48 (1995) 269-273
    • (1995) Polym Degrad Stab , vol.48 , pp. 269-273
    • Tokita, Y.1    Okamoto, A.2
  • 136
    • 0018874090 scopus 로고
    • Interactions between the carbohydrate chains of hyaluronate and chondroitin sulphate
    • Turley E.A., and Roth S. Interactions between the carbohydrate chains of hyaluronate and chondroitin sulphate. Nature 283 (1980) 268-271
    • (1980) Nature , vol.283 , pp. 268-271
    • Turley, E.A.1    Roth, S.2
  • 137
    • 0028831967 scopus 로고
    • Absolute and empirical determination of the enzymic activity and kinetic investigation of the action of hyaluronidase on hyaluronan using viscosimetry
    • Vercruysse K.P., Lauwers A.R., and Demeester J.M. Absolute and empirical determination of the enzymic activity and kinetic investigation of the action of hyaluronidase on hyaluronan using viscosimetry. Biochem J 306 (1995) 153-160
    • (1995) Biochem J , vol.306 , pp. 153-160
    • Vercruysse, K.P.1    Lauwers, A.R.2    Demeester, J.M.3
  • 139
    • 1542789741 scopus 로고
    • Fenton's reagent revisited
    • Walling C. Fenton's reagent revisited. Acc Chem Res 8 (1975) 125-131
    • (1975) Acc Chem Res , vol.8 , pp. 125-131
    • Walling, C.1
  • 140
    • 0007565643 scopus 로고
    • Oxidation processes. XVI. The autoxidation of ascorbic acid
    • Weissberger A., LuValle J.E., and Thomas Jr. D.S. Oxidation processes. XVI. The autoxidation of ascorbic acid. J Am Chem Soc 65 (1943) 1934-1939
    • (1943) J Am Chem Soc , vol.65 , pp. 1934-1939
    • Weissberger, A.1    LuValle, J.E.2    Thomas Jr., D.S.3
  • 141
    • 2142650671 scopus 로고
    • Isolation of the aldobionic acid of umbilical cord hyaluronic acid
    • Weissmann B., Rapport M.M., Linker A., and Meyer K. Isolation of the aldobionic acid of umbilical cord hyaluronic acid. J Biol Chem 205 (1953) 205-211
    • (1953) J Biol Chem , vol.205 , pp. 205-211
    • Weissmann, B.1    Rapport, M.M.2    Linker, A.3    Meyer, K.4
  • 142
    • 0000109353 scopus 로고
    • Isolation of oligosaccharides enzymatically produced from hyaluronic acid
    • Weissmann B., Meyer K., Sampson P., and Linker A. Isolation of oligosaccharides enzymatically produced from hyaluronic acid. J Biol Chem 208 (1954) 417-429
    • (1954) J Biol Chem , vol.208 , pp. 417-429
    • Weissmann, B.1    Meyer, K.2    Sampson, P.3    Linker, A.4
  • 143
    • 0021834944 scopus 로고
    • Angiogenesis induced by degradation products of hyaluronic acid
    • West D.C., Hampson I.N., Arnold F., and Kumar S. Angiogenesis induced by degradation products of hyaluronic acid. Science 228 (1985) 1324-1326
    • (1985) Science , vol.228 , pp. 1324-1326
    • West, D.C.1    Hampson, I.N.2    Arnold, F.3    Kumar, S.4
  • 144
    • 0001136497 scopus 로고
    • Alkaline degradation of polysaccharides
    • Whistler R.L., and BeMiller J.N. Alkaline degradation of polysaccharides. Adv Carbohydr Chem 13 (1958) 289-329
    • (1958) Adv Carbohydr Chem , vol.13 , pp. 289-329
    • Whistler, R.L.1    BeMiller, J.N.2
  • 146
    • 0037053313 scopus 로고    scopus 로고
    • Effect of hyaluronan oligosaccharides on the expression of heat shock protein 72
    • Xu H., Ito T., Tawada A., Maeda H., Yamanokuchi H., Isahara K., et al. Effect of hyaluronan oligosaccharides on the expression of heat shock protein 72. J Biol Chem 277 (2002) 17308-17314
    • (2002) J Biol Chem , vol.277 , pp. 17308-17314
    • Xu, H.1    Ito, T.2    Tawada, A.3    Maeda, H.4    Yamanokuchi, H.5    Isahara, K.6
  • 147
  • 148
    • 0035806079 scopus 로고    scopus 로고
    • β-Elimination of glucosyluronic residues during methylation of an acidic polysaccharide from Erwinia chrysantemi CU 643
    • Yang B.Y., and Montgomery R. β-Elimination of glucosyluronic residues during methylation of an acidic polysaccharide from Erwinia chrysantemi CU 643. Carbohydr Res 332 (2001) 317-323
    • (2001) Carbohydr Res , vol.332 , pp. 317-323
    • Yang, B.Y.1    Montgomery, R.2


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