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Isolation and characterization of the proteoglycans synthesized by adult human pulp fibroblasts in vitro
Author(s) -
BARTOLD P. M.,
MOULE A. J.,
LI H.,
RIGBY P.
Publication year - 1995
Publication title -
international endodontic journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.988
H-Index - 119
eISSN - 1365-2591
pISSN - 0143-2885
DOI - 10.1111/j.1365-2591.1995.tb00292.x
Subject(s) - biglycan , versican , decorin , proteoglycan , glycosaminoglycan , chondroitin , biochemistry , chemistry , in vitro , papain , chondroitin sulphate , syndecan 1 , dermatan sulfate , chondroitin sulfate , microbiology and biotechnology , enzyme , extracellular matrix , biology , cell
Summary 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 [ 35 S] 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.