Heparin modulates the organization of hydrated collagen gels and inhibits gel contraction by fibroblasts

C. Guidry, F. Grinnell

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

We studied the effects of extracellular matrix components on fibroblast contraction of hydrated collagen gels. After 4-h incubations, heparin-containing collagen gels contracted only 10% compared with 50% contraction of control gels. Contraction was not affected by hyaluronic acid, dermatan sulfate, or fibronectin, implying that the activity of heparin was specific. The possibility that heparin inhibited attachment of the cells to the gels was ruled out. Also, addition of heparin to the incubation medium had no effect on contraction. Microscopic examination showed that control collagen gels were composed of a uniform network of interlocking fibrils of similar sizes. Heparin-containing gels, on the other hand, were highly variable with some collagen bundles containing 5-6 collagen fibrils and other regions containing amorphous material. Unlike the control gels, the fibrils of heparin-containing gels were not continuously interconnected. Based on the results, we propose that fibroblasts attach normally to the collagen fibrils of heparin-containing gels and attempt to contract the gels, but the mechanical forces exerted by fibroblasts on individual collagen fibrils cannot be propagated throughout the gels.

Original languageEnglish (US)
Pages (from-to)1097-1103
Number of pages7
JournalJournal of Cell Biology
Volume104
Issue number4
StatePublished - 1987

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Heparin
Collagen
Fibroblasts
Gels
Dermatan Sulfate
Hyaluronic Acid
Fibronectins
Extracellular Matrix

ASJC Scopus subject areas

  • Cell Biology

Cite this

Heparin modulates the organization of hydrated collagen gels and inhibits gel contraction by fibroblasts. / Guidry, C.; Grinnell, F.

In: Journal of Cell Biology, Vol. 104, No. 4, 1987, p. 1097-1103.

Research output: Contribution to journalArticle

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