Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers

Leonid Medved', Tatiana Ugarova, Yuri Veklich, Nina Lukinova, John Weisel

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Structures formed during the early stages of clot formation have been produced in a controlled manner by polymerization of soluble fibrin monomers prepared from dissolved normal clots that had been formed upon addition of thrombin to fibrinogen. In agreement with other studies using different approaches, electron microscopy of negatively contrasted or rotary-shadowed specimens of these preparations reveal two-stranded protofibrils, as well as shorter oligomers and fibrin monomers. Individual fibrin molecules are similar in appearance to fibrinogen, suggesting that no large-scale changes in conformation occur on removal of the fibrinopeptides. Moreover, these micrographs show details of the protofibril structure not previously seen. The visualization of clear cross-over points of the filaments making up the protofibril indicate that these structures are twisted. Diffraction patterns of electron micrographs of both protofibrils and fibers and computer modeling of protofibrils also suggest that these structures are twisted but not precisely ordered.

Original languageEnglish (US)
Pages (from-to)503-509
Number of pages7
JournalJournal of molecular biology
Volume216
Issue number3
DOIs
StatePublished - Dec 5 1990
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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