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Isolation and characterization of the proteoglycans synthesized by adult human pulp fibroblasts in vitro.

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  • Additional Information
    • Author-Supplied Keywords:
      fibroblast
      glycosaminoglycan
      proteoglycan
      pulp
    • Abstract:
      The proteoglycans synthesized by fibroblasts derived from healthy human adult dental pulps have been isolated and characterized on the basis of their glycosaminoglycan content, molecular size and charge. The proteoglycans were identified by their labelling with [35S] sulphate and susceptibility to digestion by papain. The sulphated glycosaminoglycans associated with the proteoglycans were identified following specific enzymatic and chemical degradations as chondroitin sulphate, dermatan sulphate and heparan sulphate. Dermatan sulphate and chondroitin sulphate were identified as the major glycosaminoglycans secreted into the medium, whereas chrondroitin sulphate and heparan sulphate were the principal glycosaminoglycans associated with the cell layers. The proteoglycans could be fractionated on the basis of their charge and size into a number of heterogeneous pools. The principal proteoglycans isolated were small and contained either chondroitin sulphate or dermatan sulphate and most likely correspond to decorin and biglycan. Other molecules with features similar to versican and syndecan were also identified. [ABSTRACT FROM AUTHOR]
    • Abstract:
      Copyright of International Endodontic Journal is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
    • Author Affiliations:
      1Department of Dentistry, The University of Queensland, Brisbane, Australia.
    • ISSN:
      0143-2885
    • Accession Number:
      10.1111/j.1365-2591.1995.tb00292.x
    • Accession Number:
      12880198