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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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A novel variant fibrinogen, deletion of Bbeta111Ser in coiled-coil region, affecting fibrin lateral aggregation

Nobuo Okumura1, Fumiko Terasawa, Masako Hirota-Kawadobora

  • 1Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University, Japan. nobuoku@gipac.shinshu-u.ac.jp

Clinica Chimica Acta; International Journal of Clinical Chemistry
|October 19, 2005
PubMed

Insights

A novel fibrinogen variant, Kyoto IV (BbetaDelta111Ser), was identified in an infant with low functional fibrinogen. This variant shows altered polymerization, impacting fibrin clot formation under varying salt conditions.

Area of Science:

  • Hematology
  • Molecular Biology
  • Biochemistry

Background:

  • An infant presented with low functional fibrinogen concentration (<0.50 g/l), suggesting dysfibrinogenemia or hypofibrinogenemia.
  • Fibrinogen is a critical protein for blood clot formation.

Observation:

  • Identified a novel heterozygous fibrinogen variant, Kyoto IV, resulting from a 3-bp deletion in the Bbeta-chain gene, specifically deleting Serine at position 111 (BbetaDelta111Ser) within the coiled-coil region.
  • Observed discrepancies in functional fibrinogen determinations across different reagents and analyzers, attributed to variations in NaCl concentration.

Findings:

  • Kyoto IV fibrinogen demonstrated augmented polymerization under normal physiological conditions compared to normal fibrinogen.
  • Under 0.21 mol/l NaCl conditions, Kyoto IV fibrinogen exhibited significantly impaired polymerization compared to normal controls, indicating altered salt sensitivity.
  • The Bbeta111Ser residue in the coiled-coil region plays a crucial role in fibrin lateral aggregation.

Implications:

  • The BbetaDelta111Ser variant contributes to altered fibrin polymerization dynamics.
  • Understanding the role of the coiled-coil region in fibrinogen is vital for diagnosing and managing dysfibrinogenemia.
  • This finding advances knowledge of fibrinogen structure-function relationships and their impact on hemostasis.
Abstract

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