Adhesion, growth, and matrix production by fibroblasts on laminin substrates.

John Couchman, Magnus Höök, David A. Rees, Rupert Timpl

The Journal of Cell Biology · 1983 · 199 citations · 28 references

DOIFull text

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Concepts

TL;DR

Human embryonic skin fibroblasts attach and spread on laminin substrates without protein synthesis, using fibronectin‑depleted serum and anti‑fibronectin antibodies. Attachment and spreading on laminin are comparable to fibronectin, are blocked by anti‑laminin antibodies, involve distinct receptors, and support subsequent growth and extracellular matrix production.

Abstract

Human embryonic skin fibroblasts have been shown to attach and spread on laminin substrates in the absence of protein synthesis and presence of fibronectin-depleted serum and anti-fibronectin antibodies. Rates of attachment and the type of spreading are virtually identical on fibronectin and laminin-coated substrates with the development of microfilament bundles and focal adhesions. Antibodies to laminin, but not fibronectin, will prevent or reverse fibroblast adhesion to laminin, whereas antibodies to fibronectin but not laminin will give similar results on fibronectin-coated substrates. These and other results indicate that fibroblasts possess distinct receptors for laminin and fibronectin which on contact with suitable substrates promote adhesion through interaction with common intermediates. This type of adhesion is compatible with subsequent growth and extracellular matrix production.

References

28