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Volumn 25, Issue 2, 2008, Pages 101-109

Isoenzyme-specific differences in the degradation of hyaluronic acid by mammalian-type hyaluronidases

Author keywords

Bee venom hyaluronidase; Bovine testicular hyaluronidase; Capillary zone electrophoresis; Human Hyal 1; Human PH 20

Indexed keywords

BEE VENOM; HYALURONIC ACID; HYALURONIDASE; ISOENZYME; OLIGOSACCHARIDE; RECOMBINANT ENZYME; RECOMBINANT HYALURONIDASE; UNCLASSIFIED DRUG;

EID: 39049159150     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-007-9058-8     Document Type: Article
Times cited : (33)

References (39)
  • 1
    • 77956924584 scopus 로고
    • Hyaluronidases
    • Academic New York
    • Meyer, K.: Hyaluronidases. In: Boyer, P.D. (ed.) In: The Enzymes, 3rd edn., 5, pp. 307-320. Academic, New York (1971)
    • (1971) The Enzymes., 3rd Edn., 5 , pp. 307-320
    • Meyer, K.1    Boyer, P.D.2
  • 3
    • 0032508626 scopus 로고    scopus 로고
    • Hyaluronidase and its substrate hyaluronan: Biochemistry, biological activities and therapeutic uses
    • Menzel, E.J., Farr, C.: Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses. Cancer Lett. 131, 3-11 (1998)
    • (1998) Cancer Lett. , vol.131 , pp. 3-11
    • Menzel, E.J.1    Farr, C.2
  • 4
    • 33947211824 scopus 로고    scopus 로고
    • Human hyaluronidase Hyal-1: Insect cells versus E. coli as expression system and identification of low molecular weight inhibitors
    • Hofinger, E.S.A., Spickenreither, M., Oschmann, J., Rudolph, R., Bernhardt, G., Buschauer, A.: Human hyaluronidase Hyal-1: insect cells versus E. coli as expression system and identification of low molecular weight inhibitors. Glycobiology 17, 444-453 (2007)
    • (2007) Glycobiology , vol.17 , pp. 444-453
    • Hofinger, E.S.A.1    Spickenreither, M.2    Oschmann, J.3    Rudolph, R.4    Bernhardt, G.5    Buschauer, A.6
  • 6
    • 10644275944 scopus 로고    scopus 로고
    • Expression and characterization of a soluble, active form of the Jaagsiekte sheep retrovirus receptor, Hyal2
    • Vigdorovich, V., Strong, R.K., Miller, A.D.: Expression and characterization of a soluble, active form of the Jaagsiekte sheep retrovirus receptor, Hyal2. J. Virol. 79, 79-86 (2005)
    • (2005) J. Virol. , vol.79 , pp. 79-86
    • Vigdorovich, V.1    Strong, R.K.2    Miller, A.D.3
  • 7
    • 0035202490 scopus 로고    scopus 로고
    • The dual functions of GPI-anchored PH-20: Hyaluronidase and intracellular signaling
    • Cherr, G.N., Yudin, A.I., Overstreet, J.W.: The dual functions of GPI-anchored PH-20: hyaluronidase and intracellular signaling. Matrix Biol. 20, 515-525 (2001)
    • (2001) Matrix Biol. , vol.20 , pp. 515-525
    • Cherr, G.N.1    Yudin, A.I.2    Overstreet, J.W.3
  • 8
    • 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., Buschauer, A.: Comparative characterization of bovine testicular hyaluronidase and a hyaluronate lyase from Streptococcus agalactiae in pharmaceutical preparations. Eur. J. Pharm. Sci. 18, 267-277 (2003)
    • (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
  • 9
    • 0001688498 scopus 로고
    • The transglycosylative action of testicular hyaluronidase
    • Weissmann, B.: The transglycosylative action of testicular hyaluronidase. J. Biol. Chem. 216, 783-794 (1955)
    • (1955) J. Biol. Chem. , vol.216 , pp. 783-794
    • Weissmann, B.1
  • 10
    • 0028244342 scopus 로고
    • Characterization of hydrolysis and transglycosylation by testicular hyaluronidase using ion-spray mass spectrometry
    • Takagaki, K., Nakamura, T., Izumi, J., Saito, H., Endo, M.: Characterization of hydrolysis and transglycosylation by testicular hyaluronidase using ion-spray mass spectrometry. Biochemistry 33, 6503-6507 (1994)
    • (1994) Biochemistry , vol.33 , pp. 6503-6507
    • Takagaki, K.1    Nakamura, T.2    Izumi, J.3    Saito, H.4    Endo, M.5
  • 11
    • 0013914879 scopus 로고
    • Colorimetric method for determination of serum hyaluronidase activity
    • Bonner, W.M.J., Cantey, E.Y.: Colorimetric method for determination of serum hyaluronidase activity. Clin. Chim. Acta 13, 746-752 (1966)
    • (1966) Clin. Chim. Acta , vol.13 , pp. 746-752
    • Bonner, W.M.J.1    Cantey, E.Y.2
  • 12
    • 0032508523 scopus 로고    scopus 로고
    • Pharmacokinetics and tissue distribution of bovine testicular hyaluronidase and vinblastine in mice: An attempt to optimize the mode of adjuvant hyaluronidase administration in cancer chemotherapy
    • Muckenschnabel, I., Bernhardt, G., Spruss, T., Buschauer, A.: Pharmacokinetics and tissue distribution of bovine testicular hyaluronidase and vinblastine in mice: an attempt to optimize the mode of adjuvant hyaluronidase administration in cancer chemotherapy. Cancer Lett. 131, 71-84 (1998)
    • (1998) Cancer Lett. , vol.131 , pp. 71-84
    • Muckenschnabel, I.1    Bernhardt, G.2    Spruss, T.3    Buschauer, A.4
  • 13
    • 0034076116 scopus 로고    scopus 로고
    • Rat Sperm 2B1 Glycoprotein (PH20) contains a C-terminal sequence motif for attachment of a glycosyl phosphatidylinositol anchor. Effects of endoproteolytic cleavage on hyaluronidase activity
    • Seaton, G.J., Hall, L., Jones, R.: Rat Sperm 2B1 Glycoprotein (PH20) contains a C-terminal sequence motif for attachment of a glycosyl phosphatidylinositol anchor. Effects of endoproteolytic cleavage on hyaluronidase activity. Biol. Reprod. 62, 1667-1676 (2000)
    • (2000) Biol. Reprod. , vol.62 , pp. 1667-1676
    • Seaton, G.J.1    Hall, L.2    Jones, R.3
  • 14
    • 0016429897 scopus 로고
    • Properties of testicular hyaluronidase of the honey bee and oriental hornet: Comparison with insect venom and mammalian hyaluronidases
    • Allalouf, D., Ber, A., Ishay, J.: Properties of testicular hyaluronidase of the honey bee and oriental hornet: comparison with insect venom and mammalian hyaluronidases. Comp. Biochem. Physiol. B. 50, 331-337 (1975)
    • (1975) Comp. Biochem. Physiol. B. , vol.50 , pp. 331-337
    • Allalouf, D.1    Ber, A.2    Ishay, J.3
  • 15
    • 0000846238 scopus 로고
    • A turbidimetric method for the assay of hyaluronidase
    • Dorfman, A., Ott, M.L.: A turbidimetric method for the assay of hyaluronidase. J. Biol. Chem. 172, 367-375 (1948)
    • (1948) J. Biol. Chem. , vol.172 , pp. 367-375
    • Dorfman, A.1    Ott, M.L.2
  • 16
    • 0016802421 scopus 로고
    • Mechanism of action of bovine testicular hyaluronidase. Mapping of the active site
    • Highsmith, S., Garvin, J.H., Jr, Chipman, D.M.: Mechanism of action of bovine testicular hyaluronidase. Mapping of the active site. J. Biol. Chem. 250, 7473-7480 (1975)
    • (1975) J. Biol. Chem. , vol.250 , pp. 7473-7480
    • Highsmith, S.1    Garvin Jr., J.H.2    Chipman, D.M.3
  • 17
    • 0041039937 scopus 로고    scopus 로고
    • The hyaluronidase gene HYAL1 maps to chromosome 3p21.2-p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus
    • Csoka, T.B., Frost, G.I., Heng, H.H., Scherer, S.W., Mohapatra, G., Stern, R.: The hyaluronidase gene HYAL1 maps to chromosome 3p21.2-p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus. Genomics 48, 63-70 (1998)
    • (1998) Genomics , vol.48 , pp. 63-70
    • Csoka, T.B.1    Frost, G.I.2    Heng, H.H.3    Scherer, S.W.4    Mohapatra, G.5    Stern, R.6
  • 18
    • 0028052222 scopus 로고
    • A microplate assay for hyaluronidase and hyaluronidase inhibitors
    • Tung, J., Mark, G.E., Hollis, G.F.: A microplate assay for hyaluronidase and hyaluronidase inhibitors. Anal. Biochem. 223, 149-152 (1994)
    • (1994) Anal. Biochem. , vol.223 , pp. 149-152
    • Tung, J.1    Mark, G.E.2    Hollis, G.F.3
  • 19
    • 0020164881 scopus 로고
    • Purification and properties of hyaluronidase from human liver
    • Gold, E.W.: Purification and properties of hyaluronidase from human liver. Biochem. J. 205, 69-74 (1982)
    • (1982) Biochem. J. , vol.205 , pp. 69-74
    • Gold, E.W.1
  • 20
    • 0027180070 scopus 로고
    • Purification and characterization of human serum hyaluronidase
    • Afify, A., Stern, M., Guntenhoner, M., Stern, R.: Purification and characterization of human serum hyaluronidase. Arch. Biochem. Biophys. 305, 434-441 (1993)
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 434-441
    • Afify, A.1    Stern, M.2    Guntenhoner, M.3    Stern, R.4
  • 21
  • 22
    • 23444445895 scopus 로고    scopus 로고
    • Hyaluronan metabolism: A major paradox in cancer biology
    • Stern, R.: Hyaluronan metabolism: a major paradox in cancer biology. Pathol. Biol. 53, 372-382 (2005)
    • (2005) Pathol. Biol. , vol.53 , pp. 372-382
    • Stern, R.1
  • 23
    • 0032508502 scopus 로고    scopus 로고
    • Quantitation of hyaluronidases by the Morgan-Elson reaction: Comparison of the enzyme activities in the plasma of tumor patients and healthy volunteers
    • Muckenschnabel, I., Bernhardt, G., Spruss, T., Dietl, B., Buschauer, A.: Quantitation of hyaluronidases by the Morgan-Elson reaction: comparison of the enzyme activities in the plasma of tumor patients and healthy volunteers. Cancer Lett. 131, 13-20 (1998)
    • (1998) Cancer Lett. , vol.131 , pp. 13-20
    • Muckenschnabel, I.1    Bernhardt, G.2    Spruss, T.3    Dietl, B.4    Buschauer, A.5
  • 24
    • 33746385042 scopus 로고
    • The role of mucoid polysaccharide (hyaluronic acid) in the virulence of group a hemolytic streptococci
    • Kass, E.H., Seastone, C.V.: The role of mucoid polysaccharide (hyaluronic acid) in the virulence of group A hemolytic streptococci. J. Exp. Med. 79, 319-330 (1944)
    • (1944) J. Exp. Med. , vol.79 , pp. 319-330
    • Kass, E.H.1    Seastone, C.V.2
  • 25
    • 0001476522 scopus 로고
    • The biological significance of hyaluronic acid and hyaluronidases
    • Meyer, K.: The biological significance of hyaluronic acid and hyaluronidases. Physiol. Rev. 27, 335-359 (1947)
    • (1947) Physiol. Rev. , vol.27 , pp. 335-359
    • Meyer, K.1
  • 26
    • 84965081885 scopus 로고
    • The international standard for hyaluronidase
    • Humphrey, J.H.: The international standard for hyaluronidase. Bull. World Health Organ. 16, 291-294 (1957)
    • (1957) Bull. World Health Organ. , vol.16 , pp. 291-294
    • Humphrey, J.H.1
  • 27
    • 34548752817 scopus 로고    scopus 로고
    • Kinetics of Hyal-1 and PH-20 hyaluronidases: Comparison of minimal substrates and analysis of the transglycosylation reaction
    • (in press) DOI 10.1093/glycob/cwm070 (2007)
    • Hofinger, E.S.A., Bernhardt, G., Buschauer, A.: Kinetics of Hyal-1 and PH-20 hyaluronidases: comparison of minimal substrates and analysis of the transglycosylation reaction. Glycobiology (in press) DOI 10.1093/glycob/cwm070 (2007)
    • Glycobiology
    • Hofinger, E.S.A.1    Bernhardt, G.2    Buschauer, A.3
  • 29
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • Reissig, J., Strominger, J., Leloir, L.: A modified colorimetric method for the estimation of N-acetylamino sugars. J. Biol. Chem. 217, 959-966 (1955)
    • (1955) J. Biol. Chem. , vol.217 , pp. 959-966
    • Reissig, J.1    Strominger, J.2    Leloir, L.3
  • 30
    • 0001615705 scopus 로고
    • Turbidimetric measurement of acid mucopolysaccharides and hyaluronidase activity
    • Di Ferrante, N.: Turbidimetric measurement of acid mucopolysaccharides and hyaluronidase activity. J. Biol. Chem. 220, 303-306 (1956)
    • (1956) J. Biol. Chem. , vol.220 , pp. 303-306
    • Di Ferrante, N.1
  • 31
    • 0031450024 scopus 로고    scopus 로고
    • Analysis of glycosaminoglycans and their oligosaccharide fragments by capillary electrophoresis
    • Grimshaw, J.: Analysis of glycosaminoglycans and their oligosaccharide fragments by capillary electrophoresis. Electrophoresis 18, 2408-2414 (1997)
    • (1997) Electrophoresis , vol.18 , pp. 2408-2414
    • Grimshaw, J.1
  • 32
    • 0019832429 scopus 로고
    • A recommended procedure for the estimation of bovine testicular hyaluronidase in the presence of human serum
    • Gacesa, P., Savitsky, M.J., Dodgson, K.S., Olavesen, A.H.: A recommended procedure for the estimation of bovine testicular hyaluronidase in the presence of human serum. Anal. Biochem. 118, 76-84 (1981)
    • (1981) Anal. Biochem. , vol.118 , pp. 76-84
    • Gacesa, P.1    Savitsky, M.J.2    Dodgson, K.S.3    Olavesen, A.H.4
  • 33
    • 0016705234 scopus 로고
    • Effect of ionic strength and pH on the properties of purified bovine testicular hyaluronidase
    • Gorham, S.D., Olavesen, A.H., Dodgson, K.S.: Effect of ionic strength and pH on the properties of purified bovine testicular hyaluronidase. Connect. Tissue Res. 3, 17-25 (1975)
    • (1975) Connect. Tissue Res. , vol.3 , pp. 17-25
    • Gorham, S.D.1    Olavesen, A.H.2    Dodgson, K.S.3
  • 34
    • 0025784914 scopus 로고
    • The separation of chondroitin sulfate disaccharides and hyaluronan oligosaccharides by capillary zone electrophoresis
    • Carney, S.L., Osborne, D.J.: The separation of chondroitin sulfate disaccharides and hyaluronan oligosaccharides by capillary zone electrophoresis. Anal. Biochem. 195, 132-140 (1991)
    • (1991) Anal. Biochem. , vol.195 , pp. 132-140
    • Carney, S.L.1    Osborne, D.J.2
  • 37
    • 0028938648 scopus 로고
    • Enzymic reconstruction of glycosaminoglycan oligosaccharide chains using the transglycosylation reaction of bovine testicular hyaluronidase
    • Saitoh, H., Takagaki, K., Majima, M., Nakamura, T., Matsuki, A., Kasai, M., Narita, H., Endo, M.: Enzymic reconstruction of glycosaminoglycan oligosaccharide chains using the transglycosylation reaction of bovine testicular hyaluronidase. J. Biol. Chem. 270, 3741-3747 (1995)
    • (1995) J. Biol. Chem. , vol.270 , pp. 3741-3747
    • Saitoh, H.1    Takagaki, K.2    Majima, M.3    Nakamura, T.4    Matsuki, A.5    Kasai, M.6    Narita, H.7    Endo, M.8
  • 38
    • 0035449896 scopus 로고    scopus 로고
    • Alkalinization of acrosome measured by GFP as a pH indicator and its relation to sperm capacitation
    • Nakanishi, T., Ikawa, M., Yamada, S., Toshimori, K., Okabe, M.: Alkalinization of acrosome measured by GFP as a pH indicator and its relation to sperm capacitation. Dev. Biol. 237, 222-231 (2001)
    • (2001) Dev. Biol. , vol.237 , pp. 222-231
    • Nakanishi, T.1    Ikawa, M.2    Yamada, S.3    Toshimori, K.4    Okabe, M.5
  • 39
    • 3042697038 scopus 로고    scopus 로고
    • Hyaluronan: From extracellular glue to pericellular cue
    • Toole, B.P.: Hyaluronan: from extracellular glue to pericellular cue. Nat. Rev. Cancer 4, 528-539 (2004)
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 528-539
    • Toole, B.P.1


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