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Related Experiment Videos

Tb(III)-ion-binding-induced conformational changes in platelet factor XIII.

K E Achyuthan1, A Mary, C S Greenberg

  • 1Department of Medicine, Duke University Medical Center, Durham, NC 27710.

The Biochemical Journal
|January 15, 1989
PubMed
Summary

Calcium ions are essential for activating Factor XIII zymogen. Terbium ions can mimic calcium during activation but inhibit the enzyme

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Enzymology

Background:

  • Calcium ions (Ca(II)) are critical for the proteolytic activation of Factor XIII zymogen to its active form, Factor XIIIa.
  • Understanding the role of divalent cations in Factor XIII activation and function is crucial for comprehending hemostasis and thrombosis.

Purpose of the Study:

  • To investigate the effect of terbium ions (Tb(III)) and other lanthanide ions (Ln(III)) on the proteolytic activation and transglutaminase activity of Factor XIII.
  • To elucidate the binding interactions and functional consequences of Tb(III) on Factor XIII.

Main Methods:

  • Proteolytic activation of Factor XIII using thrombin or trypsin in the presence of various concentrations of Ca(II), EDTA, Tb(III), and other Ln(III) ions.
  • Assays for transglutaminase activity, molecular mass determination (SDS-PAGE), and protein binding studies (affinity chromatography, fluorescence spectroscopy).

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Main Results:

  • Tb(III) ions at 40 microM supported proteolytic activation of Factor XIII, yielding Factor XIIIa with comparable activity and molecular mass to Ca(II)-formed Factor XIIIa.
  • Lower Tb(III) concentrations (1-5 microM) led to Factor XIII fragmentation and loss of activity, while higher concentrations (>40 microM) rendered Factor XIII resistant to proteolysis.
  • Tb(III) inhibited Factor XIIIa transglutaminase activity non-competitively and interfered with Factor XIII binding to fibrinogen, indicating conformational changes induced by Tb(III) binding.

Conclusions:

  • Terbium ions can substitute for calcium ions in the proteolytic activation of Factor XIII, but exhibit complex dose-dependent effects on enzyme activity and stability.
  • Lanthanide ions, particularly Tb(III), interact with Factor XIII, inducing conformational changes that modulate its structure, proteolytic susceptibility, and interaction with substrates like fibrinogen.