Abnormal Formation of Fibrin Network from X-ray Irradiated Fibrinogen: Two-color Fluorescence Analysis of the Dynamic Process and the Incorporation of Fibrinolytic Components into Fibrin by Confocal Laser-Scanning Microscopy

• Koh Chang-Sung

  1Department of Medicine, Shinshu University School of Medicine

• Takahashi Kei

  Department of Physiology, Shimane Medical College

• Sakurai Shumpei

  Hematology and Oncology Section, The Medical School, Northwestern University, School of Medicine

• Kwaan Hau C.

  Hematology and Oncology Section, The Medical School, Northwestern University, School of Medicine

抄録

Analysis of the process of fibrin polymerization was spectrophotometrically examined by the absorbance at 350 nm. The time-depemdent process showed a sigmoidal curve consisting of a lag- (5 min), exponential- (5 to 30 min) and plateauphase (over than 30). The time-delay was found in the polymerization of X-ray irradiated fibrinogen. It was X-ray dose-dependent, and the adition of normal fibrinogen to the irradiated one abolished the time-delay. X-ray irradiated fibrinogen showed no changes in the components, A α, B β, and γ chains, on reduced SDS-polyacrylamide gels. However, confocal laser-scanning microscopic visualization of the fibrin networks from X-ray irradiated FITC-labeled fibrinogen demonstrated that the networks consisting of nodes and fibers were poorly organized: Fibers were half in length, and diameters of nodes and the thickness of fibers were reduced by 30 to 40% compared to the normal ones. When normal networks were analyzed by the digital-imaging method, the networks in lag- and exponential-phase (early-phase) contained nodes and shorter fibers than those in plateau (late-phase). Fibrinolytic components such as RITC-labeled plasminogen and RITC-labeled N-terminal fragment of urokinase-type plasminogen were found to be homogeneously localized at both nodes and fibers, and their densities were gradually higher in nodes than in fibers. These results suggest that the growth of networks is apparently mediated by nodes, and X-ray irradiation allows molecular lesions to form at one of the terminal domains of fibrinogen, facilitating a dysfunction of the assembly of fibrin monomers by end-to-end elongation.

収録刊行物

• bioimages

  bioimages 5 (2), 49-58, 1997

  日本バイオイメージング学会

キーワード

• confocal laser scanning microscopy
• fibrin network
• X-ray
• irradiation
• abnormal fibrinogen
• fibrinolytic components
• molecular assembly

詳細情報

• CRID: 1391693801397672320
• NII論文ID: 10002038111
• NII書誌ID: AA11084187
• DOI: 10.11169/bioimages.5.49
• ISSN: 09192719
• 本文言語コード: en
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可