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

Béla Papp, Tünde Kovács, István Léránt, Zsolt Nagy, Raymund Machovich

Research output: Article

7 Citations (Scopus)

Abstract

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 μM heparin and 0.9μM collagen, while the rate of complex formation was linearly related to concentrations of fibronectin as high a 3 μM. Heparin was incorporated into the complex in a saturable manner, and was release 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.

Original languageEnglish
Pages (from-to)241-247
Number of pages7
JournalBBA - General Subjects
Volume925
Issue number3
DOIs
Publication statusPublished - szept. 11 1987

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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