Integrity of the pericellular fibronectin matrix of fibroblasts is independent of sulfated glycosaminoglycans.

K. Hedman, T. Vartio, S. Johansson, L. Kjellén, M. Höök, A. Linker, E. M. Salonen, A. Vaheri

    Research output: Contribution to journalArticlepeer-review

    7 Scopus citations

    Abstract

    The pericellular matrix fibers of cultured human fibroblasts contain fibronectin, other glycoproteins, and heparan and chondroitin sulfate proteoglycans. In the present study, cell-free pericellular matrices were isolated from metabolically labeled fibroblast cultures. The isolated matrices were digested with heparinase from Flavobacterium heparinum, and then analyzed for sulfated glycosaminoglycans (GAGs). Nitrous acid degradation was used to distinguish the N-sulfated GAGs (heparan sulfate) from chondroitin sulfate. Fibronectin and the other major matrix polypeptides were studied using gel electrophoresis, enzyme immunoassay and immunofluorescence. Upon heparinase digestion, greater than 95% of sulfated GAGs were degraded in the matrix without detectable release of fibronectin or other matrix polypeptides or alteration of the fibrillar matrix structure. We conclude that in fibroblast cultures the integrity of the fibrillar matrix is independent of sulfated GAGs. Together with earlier observations, this suggests that filamentous polymerization of fibronectin forms the backbone of early connective tissue matrix.

    Original languageEnglish (US)
    Pages (from-to)581-584
    Number of pages4
    JournalThe EMBO journal
    Volume3
    Issue number3
    DOIs
    StatePublished - Mar 1984

    ASJC Scopus subject areas

    • General Neuroscience
    • Molecular Biology
    • General Biochemistry, Genetics and Molecular Biology
    • General Immunology and Microbiology

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