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Journal of Dental Research
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Separation and Properties of Rabbit Buccal Mucosal Wound Hyaluronidase

C.N. Bertolami

Department of Oral and Maxillofacial Surgery, Massachusetts General Hospital, Fruit Street, Boston, Massachusetts 02114

R.H. Day

Harvard School of Dental Medicine, Boston, Massachusetts

D.G. Ellis

Shriners Burns Institute

This study establishes the existence of a mammalian buccal mucosal wound hyaluronidase (hyaluronate 4-glycohydrolase; EC 3.2.1.35) having properties distinct from those of the endogenous lysosomal hyaluronidase of normal (uninjured) buccal mucosa. A time-dependent change in hyaluronidase activity was measured, with the highest specific activity occurring on post-wound day 4 (7.7 ± 1.3 unitslmg protein), followed by consecutive decreases until activity was no longer discernible by day 21. Mucosal wound hyaluronidase closely resembled a previously described integumentary wound endoglycosidase in terms of a high pH optimum (5.0-6.0), distinct (but non-exclusive) substrate preference for hyaluronic acid, and ability to generate saturated depolymerization products by an endoglycosidic hydrolysis.

REFERENCES

  • Alexander, S.A. and Donoff, R.B. (1979): Identification and Localization of Wound Hyaluronidase, J Surg Res 27:163-167.[CrossRef][Medline] [Order article via Infotrieve]
  • Balazs, A. and Holmgren, H.J. (1950): The Basic Dye-uptake and the Presence of a Growth-inhibiting Substance in the Healing Tissue of Skin Wounds, Exp Cell Res 1:206-216.
  • Barnhart, B.J.; Cox, S.H.; and Kraemer, P.M. (1979): Detachment Variants of Chinese Hamster Cells: Hyaluronic Acid as a Modulator of Cell Detachment, Exp Cell Res 119:327-332.[CrossRef][Medline] [Order article via Infotrieve]
  • Bertolami, C.N. and Donoff, R.B. (1982): Identification, Characterization, and Partial Purification of Mammalian Skin Wound Hyaluronidase, J Invest Derm 79:417-421.[CrossRef][Medline] [Order article via Infotrieve]
  • Bertolami, C.N. and Ellis, D.G. (1985): Identification and Characterization of Rabbit Buccal Mucosal Hyaluronidase, J Dent Res 64:913-918.[Abstract/Free Full Text]
  • Bollet, A.J.; Bonner, W.M.; and Nance, J.L. (1963): The Presence of Hyaluronidase in Various Mammalian Tissues, J Biol Chem 238:3522-3527.[Free Full Text]
  • Chevrier, A.; Girard, N.; Delpech, B.; and Gilbert, D. (1982): Inhibition of Active E Rosette Forming T Lymphocytes by Hyaluronic Acid. Evidence for a Receptor for Hyaluronic Acid on a Lymphocyte Subpopulation, Biomedicine 36:100-103.
  • Donoff, R.B.; Swann, D.A.; and Schweidt, S.H. (1984): Glycosaminoglycans of Normal and Hypertrophic Human Scar, Exp Molec Pathol 40:13-20.[CrossRef][Medline] [Order article via Infotrieve]
  • Fairbanks, G.; Steck, T.L.; and Wallach, D.F.H. (1971): Electrophoretic Analysis of the Major Polypeptides of the Human Erythrocyte Membrane, Biochem 10:2606-2617.[CrossRef][Medline] [Order article via Infotrieve]
  • Feinberg, R.N. and Beebe, D.C. (1983): Hyaluronate in Vasculogenesis, Science 220:1177-1179.[Abstract/Free Full Text]
  • Fenger, M. (1982): Purification of Human Serum Hyaluronidase Using Chromatofocusing, J Chromatog 240:173-179.[Medline] [Order article via Infotrieve]
  • Fiszer-Szafarz, B. (1984): Hyaluronidase Polymorphism Detected by Polyacrylamide Gel Electrophoresis. Application to Hyaluronidases from Bacteria, Slime Molds, Bee and Snake Venoms, Bovine Testis, Rat Liver Lysosomes, and Human Serum, Anal Biochem 143:76-81.
  • Fiszer-Szafarz, B. and Nadal, C. (1977): Lysosomal Enzyme Activities in the Regenerating Rat Liver, Cancer Res 34:354-357.
  • Forrester, J.V. and Balazs, E.A. (1980): Inhibition of Phagocytosis by High Molecular Weight Hyaluronate, Immunology 40:435-446.[Medline] [Order article via Infotrieve]
  • Goggins, J.F.; Lazarus, G.S.; and Fullmer, H.M. (1968): Hyaluronidase Activity of Alveolar Macrophages, J Histochem Cytochem 16:688-692.[Medline] [Order article via Infotrieve]
  • Gold, E.W. (1982): Purification and Properties of Hyaluronidase from Human Liver, Biochem J 205:69-74.[Medline] [Order article via Infotrieve]
  • Hakanson, L.; Hallgren, R.; and Venge, P. (1980): Regulation of Granulocyte Formation by Hyaluronic Acid, J Clin Invest 66:298-305.[Medline] [Order article via Infotrieve]
  • Hopps, R.M. and Prout, R.E.S. (1972): Identification of Tissue and Bacterial Hyaluronidase in Human Saliva, J Periodont Res 7:236-241.[CrossRef][Medline] [Order article via Infotrieve]
  • Iub Commission On Biochemistry Nomenclature ( 1979): Enzyme Nomenclature, Recommendations (1978) of the Nomenclature Committee of the International Union of Biochemistry, New York: Academic Press.
  • Iupac-Iub Commission On Biochemical Nomenclature (1977): Nomenclature of Multiple Forms of Enzymes; Recommendations, 1976, J Biol Chem 252:5939-5941.[Free Full Text]
  • Levvy, G.A. and Marsh, C.A. (1959): Preparation and Properties of BETA-Glucuronidase, Adv Carbohyd Chem 14:381-428.
  • Lowry, O.; Rosebrough, N.J.; Farr, A.L.; and Randall, R.J. (1951): Protein Measurement with the Folin Phenol Reagent, J Biol Chem 193:265-275.[Free Full Text]
  • Orkin, R.W. and Toole, B.P. (1978): Hyaluronidase Activity and Hyaluronate Content of the Developing Chick Embryo Heart, Dev Biol 66:308-320.[CrossRef][Medline] [Order article via Infotrieve]
  • Partridge, S.M. (1948): Filter-paper Partition Chromatography of Sugars, Biochem 42:238-253.[CrossRef]
  • Polansky, J.R.; Toole, B.P.; and Gross, J. (1974): Brain Hyaluronidase: Changes in Activity During Chick Development, Science 183:862-864.[Abstract/Free Full Text]
  • Reissig, J.L.; Strominger, J.L.; and Leloir, L.F. (1955): A Modified Colorimetric Method for the Estimation of N-acetylamino Sugars, J Biol Chem 217:959-966.[Free Full Text]
  • Sahu, S.C. (1981): Hyaluronidase Activity in Alveolar Secretions of Human Lung, Biochem Med 25:56-61.[CrossRef][Medline] [Order article via Infotrieve]
  • Savage, K. and Swann, D.A. (1985): A Comparison of Glycosaminoglycan Synthesis by Human Fibroblasts from Normal Skin, Normal Scar, and Hypertrophic Scar, J Invest Derm 84:521-526.
  • Soru, E. and Ionescu-Stoian, F. (1965): The Purification of Testicular Hyaluronidase by Chromatography on a Mixed Column, J Chromatog 17:538-541.[CrossRef][Medline] [Order article via Infotrieve]
  • Swann, D.A.; Garg, H.G.; Jung, W.; and Hermann, H. (1985): Studies on Human Scar Tissue Proteoglycans, J Invest Derm 84:527-531.[Medline] [Order article via Infotrieve]
  • Turley, E.A. (1982): Purification of a Hyaluronate-binding Protein Fraction that Modifies Cell Social Behavior, Biochem Biophys Res Commun 108:1016-1024.[CrossRef][Medline] [Order article via Infotrieve]
  • Yamada, M.; Hasegawa, E.; and Kanamori, M. (1977): Purification of Hyaluronidase from Human Placenta, J Biochem 81:485-494.[Abstract/Free Full Text]
  • Yang, C.H. and Srivastava, P.N. (1974): Separation and Properties of Hyaluronidase from Rat Sperm Acrosomes, J Reprod Fert 37:17-25.[Abstract/Free Full Text]
  • Yang, C.H. and Srivastava, P.N. (1975): Purification of Bull Sperm Hyaluronidase by Concanavalin-A Affinity Chromatography, Biochem Biophys Acta 391:382-387.[Medline] [Order article via Infotrieve]
  • Zaneveld, L.J.D.; Polakoski, K.L.; and Schumacher, G.F.B. (1973): Properties of Acrosomal Hyaluronidase from Bull Spermatozoa: Evidence for its Similarity to Testicular Hyaluronidase, J Biol Chem 248:564-570.[Abstract/Free Full Text]

Journal of Dental Research, Vol. 65, No. 6, 939-944 (1986)
DOI: 10.1177/00220345860650061701
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This Article
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Right arrow Articles by Ellis, D.G.
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What's this?