Your browser doesn't support javascript.
loading
Fibrinogen alpha C chain 5.9 kDa fragment (FIC5.9), a biomarker for various pathological conditions, is produced in post-blood collection by fibrinolysis and coagulation factors.
Kikuchi, Wataru; Nishimura, Motoi; Kuga, Takahisa; Tsuchida, Sachio; Saito, Tatsuya; Satoh, Mamoru; Noda, Kenta; Kodera, Yoshio; Tomonaga, Takeshi; Nomura, Fumio.
Afiliação
  • Kikuchi W; Department of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan ; R&D Department, Nittobo Medical Co., Ltd., Koriyama, Japan.
  • Nishimura M; Department of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan.
  • Kuga T; Department of Biochemistry and Molecular Biology, Kyoto Pharmaceutical University, Kyoto, Japan.
  • Tsuchida S; Department of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan.
  • Saito T; Department of Physics, School of Science, Kitasato University, Sagamihara, Kanagawa Japan.
  • Satoh M; Department of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan.
  • Noda K; R&D Department, Nittobo Medical Co., Ltd., Koriyama, Japan.
  • Kodera Y; Department of Physics, School of Science, Kitasato University, Sagamihara, Kanagawa Japan.
  • Tomonaga T; Laboratory of Proteome Research, National Institute of Biomedical Innovation, Osaka, Japan.
  • Nomura F; Division of Clinical Mass Spectrometry and Clinical Genetics, Chiba University Hospital, Chiba, Japan.
Clin Proteomics ; 13: 27, 2016.
Article em En | MEDLINE | ID: mdl-27761105
ABSTRACT

BACKGROUND:

Fibrinogen alpha C chain 5.9 kDa fragment (FIC5.9) is a new serum biomarker for chronic hepatitis that was discovered by proteomics analysis. Previous studies have shown that FIC5.9 is derived from the C-terminal region of fibrinogen alpha chain and the serum levels of FIC5.9 decrease in chronic hepatitis. It also have been reported that FIC5.9 cannot be detected in the blood stream of the systemic circulation and it is released from fibrinogen during blood clotting in collecting tube. However, the mechanism of FIC5.9 releasing from fibrinogen is unclear.

METHODS:

We formulated a hypothesis that FIC5.9 is released by enzymes that are activated by post-blood collection and may be coagulation and fibrinolysis factors. In this study, we analyzed the mechanisms of FIC5.9 releasing from fibrinogen in healthy blood.

RESULTS:

Our analysis showed that thrombin acts as an initiator for FIC5.9 releasing, and that mainly plasmin cleaves N-terminal end of FIC5.9 and neutrophil elastase cleave C-terminal end of FIC5.9.

CONCLUSION:

FIC5.9 reflects minute changes in coagulation and fibrinolysis factors and may be associated with pathological conditions.
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Clin Proteomics Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Japão

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Clin Proteomics Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Japão