Conditions of formation of the heparin-fibronectin-collagen complex and the effect of plasmin

Biochim Biophys Acta. 1987 Sep 11;925(3):241-7. doi: 10.1016/0304-4165(87)90188-7.


The formation and composition of the insoluble heparin-fibronectin-collagen complex and its degradation by proteolysis was investigated. At fixed concentrations of the other molecular components of the complex, the maximal rate of complex formation, measured turbidimetrically, was reached at a concentration of 4 microM heparin and 0.9 microM collagen, while the rate of complex formation was linearly related to concentrations of fibronectin as high as 3 microM. Heparin was incorporated into the complex in a saturable manner, and was released in active anticoagulant form by plasmin but not by urokinase. The complex formation was inhibited by 5 mM calcium or 250 mM NaCl as well as by polybrene or spermin. It is suggested that fibronectin binds both heparin and collagen cooperatively to form an insoluble ternary complex of the extracellular matrix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding, Competitive
  • Calcium / pharmacology
  • Chemical Precipitation
  • Collagen*
  • Fibrinolysin / pharmacology*
  • Fibronectins*
  • Heparin*
  • Hexadimethrine Bromide / pharmacology
  • Humans
  • Hydrolysis
  • Kinetics
  • Protein Binding
  • Sodium Chloride / pharmacology
  • Solubility


  • Fibronectins
  • Sodium Chloride
  • Hexadimethrine Bromide
  • Heparin
  • Collagen
  • Fibrinolysin
  • Calcium