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Gel Formation of Recombinant Fibrinogen Lacking αC Termini

  • Kenji KuboaEmail author
  • Yuka Masuda
  • Yoshiharu Toyama
  • Nobukazu Nameki
  • Nobuo Okumura
  • Masanori Ochiai
Part of the Progress in Colloid and Polymer Science book series (PROGCOLLOID, volume 136)

Abstract

In order to examine the role of αC domains, especially the terminal region of it, of fibrinogen Aα chain in the fibrin gel formation, we prepared a recombinant fibrinogen, Aα570 fibrinogen. Aα570 fibrinogen is the fibrinogen that is truncated at Aα570 and lacks 40 amino acids at the terminus of the αC domain. We examined the thrombin-catalyzed polymerization by transmission spectroscopy and confocal laser scanning microscopy (CLSM). We found that Aα570 fibrinogen exhibited a significantly delayed aggregation showing the importance of the terminal region of the αC domain in the polymerization process. Contrary to the fact that the addition of glucose to the mixture of fibrinogen and thrombin results in a substantial delay of the lateral aggregation of protofibrils for the native fibrinogen, delaying effect due to the addition of glucose disappeared thoroughly in the case of Aα570 fibrinogen. Turbidity measurements dependent upon the wavelength in the time course of gelation showed that mass per unit fiber length of Aα570 fibrinogen decreased significantly compared to the native fibrinogen, and the lateral aggregation of protofibrils was hindered significantly. Those results are consistent with the CLSM measurements that the bundles of protofibrils of Aα570 fibrinogen are thinner and denser with more branching than those of the native one. It was confirmed that C-terminal region of the αC domain plays an important role in the lateral aggregation and glucose interferes the interacting process between the αC domains.

Keywords

Fibrinogen Truncation αC domain Gelation Saccharides 

Notes

Acknowledgments

Authors, K. Kubota and N. Okumura, thank Prof. S. T. Lord for providing the plasmid vector that encodes the fibrinogen Aa chain. This work was partly supported by the Grant for Joint Research Program of the Institute of Low Temperature Science, Hokkaido Univ. and by the Ministry of Education, Japan.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2009

Authors and Affiliations

  • Kenji Kuboa
    • 1
    Email author
  • Yuka Masuda
    • 1
  • Yoshiharu Toyama
    • 1
  • Nobukazu Nameki
    • 1
  • Nobuo Okumura
    • 2
  • Masanori Ochiai
    • 3
  1. 1.Department of Chemistry and Chemical BiologyGraduate School of Engineering, Gunma UniversityGunmaJapan
  2. 2.Department of Bimedical Laboratory SciencesSchool of Medicine, Shinsyu UniversityNaganoJapan
  3. 3.Institute of Low Temperature ScienceHokkaido UniversityHokkaidoJapan

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