Abstract
Amelogenin, the major protein component of tooth enamel, is shown to be a cell adhesion protein. Since it had been shown that an amelogenin-containing preparation, Emdogain, possessed cell-adhesive activity, we tested the hypothesis that amelogenin was responsible for cell-adhesive activity. Recombinant amelogenin was found to promote adhesion at less than 15 micro g/60-mm plate and requires divalent cations for activity. While we found that amelogenin does not bind to collagen or heparin under physiological conditions, it was demonstrated previously that amelogenin does bind to hydroxyapatite. The cell-adhesive activity of amelogenin may play a role in development and may provide a partial explanation for the therapeutic effects of Emdogain in periodontal regeneration.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amelogenin
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Biocompatible Materials / chemistry
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Calcium / pharmacology
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Cell Adhesion / drug effects
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Cell Adhesion Molecules / metabolism
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Cell Adhesion Molecules / pharmacology
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Cell Adhesion Molecules / physiology*
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Cell Culture Techniques
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Collagen Type I / metabolism
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Dental Enamel Proteins / metabolism
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Dental Enamel Proteins / pharmacology
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Dental Enamel Proteins / physiology*
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Durapatite / chemistry
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Extracellular Matrix Proteins / metabolism
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Heparin / metabolism
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Humans
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Magnesium / pharmacology
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Osteosarcoma / metabolism
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Osteosarcoma / pathology
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Periodontal Ligament / cytology
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Periodontal Ligament / metabolism
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Recombinant Proteins
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Surface Properties
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Tumor Cells, Cultured
Substances
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Amelogenin
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Biocompatible Materials
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Cell Adhesion Molecules
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Collagen Type I
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Dental Enamel Proteins
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Extracellular Matrix Proteins
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Recombinant Proteins
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enamel matrix proteins
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Heparin
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Durapatite
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Magnesium
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Calcium