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Protein kinase C modulation of fibronectin matrix assembly

C E Somers1, D F Mosher

  • 1Department of Medicine, University of Wisconsin, Madison 53706.

The Journal of Biological Chemistry
|October 25, 1993
PubMed

Insights

Protein kinase C (PKC) regulates fibronectin (Fn) matrix assembly in fibroblasts. Inhibiting PKC reduces Fn binding, while activating it increases binding, suggesting PKC-mediated phosphorylation is key.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Extracellular Matrix Research

Background:

  • Fibroblasts utilize cell surface sites for fibronectin (Fn) assembly into the extracellular matrix.
  • Understanding the regulation of Fn matrix assembly is crucial for tissue repair and development.

Purpose of the Study:

  • To investigate the role of protein kinase C (PKC) in modulating fibronectin matrix assembly by fibroblasts.
  • To identify the specific kinase involved in regulating Fn binding to fibroblast cell surfaces.

Main Methods:

  • Treatment of fibroblasts with various kinase inhibitors (ML-7, H7, HA1004, calphostin C, staurosporine) and PKC activators (phorbol esters).
  • Quantification of 125I-labeled plasma Fn and Fn fragment binding to treated fibroblasts.
  • Dose-response analysis of inhibitor effects to identify the target kinase.

Main Results:

  • Kinase inhibitors rapidly and reversibly decreased the binding of labeled Fn and its fragments to fibroblasts.
  • Dose-response data strongly implicated protein kinase C (PKC) as the targeted kinase.
  • Activation of PKC led to increased Fn binding, confirming its modulatory role.

Conclusions:

  • Fibronectin matrix assembly is modulated by PKC-mediated phosphorylation.
  • PKC plays a significant role in regulating the interaction of fibronectin with fibroblast cell surface sites.
  • Targeting PKC may offer a strategy to influence extracellular matrix formation.

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