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ArticleClinical proteomics2016

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.

Wataru Kikuchi, Motoi Nishimura, Takahisa Kuga, Sachio Tsuchida, Tatsuya Saito, Mamoru Satoh, Kenta Noda, Yoshio Kodera, Takeshi Tomonaga, Fumio Nomura

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Article in Clinical proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Serum peptides as candidate biomarkers for relapsing polychondritis.Journal of mass spectrometry and advances in the clinical lab · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 6 institutions in 1 country.

Wataru KikuchiDepartment of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan ; R&D Department, Nittobo Medical Co., Ltd., Koriyama, Japan.
Motoi NishimuraDepartment of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan.
Takahisa KugaDepartment of Biochemistry and Molecular Biology, Kyoto Pharmaceutical University, Kyoto, Japan.
Sachio TsuchidaDepartment of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan.
Tatsuya SaitoDepartment of Physics, School of Science, Kitasato University, Sagamihara, Kanagawa Japan.
Mamoru SatohDepartment of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan.
Kenta NodaR&D Department, Nittobo Medical Co., Ltd., Koriyama, Japan.
Yoshio KoderaDepartment of Physics, School of Science, Kitasato University, Sagamihara, Kanagawa Japan.
Takeshi TomonagaLaboratory of Proteome Research, National Institute of Biomedical Innovation, Osaka, Japan.
Fumio NomuraDivision of Clinical Mass Spectrometry and Clinical Genetics, Chiba University Hospital, Chiba, Japan.
Chiba University · JPKitasato University · JPChiba University Hospital · JPKyoto Pharmaceutical University · JPNational Institute of Biomedical Innovation, Health and Nutrition · JPNitto Boseki (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFibrinogen 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.

methodsWe 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.

resultsOur 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.

conclusionFIC5.9 reflects minute changes in coagulation and fibrinolysis factors and may be associated with pathological conditions.

Indexed as

BiomarkerCoagulationFibrinogenFibrinogen alpha C chain 5.9 kDa fragment (FIC5.9)HepatitisPlasminThrombin

Identifiers

PMID27761105
PMCPMC5055723
OpenAlexW2529279770

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.