Evidence map›Paper›PMID 34333754›Full record

ArticleInternational journal of hematology2021

A novel variant fibrinogen, AαE11del, demonstrating the importance of AαE11 residue in thrombin binding.

Takahiro Kaido, Masahiro Yoda, Tomu Kamijo, Shinpei Arai, Kazuyoshi Yamauchi, Nobuo Okumura

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Article in International journal of hematology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Takahiro KaidoDepartment of Medical Sciences, Graduate School of Medicine, Science and Technology, Shinshu University, Matsumoto, Japan.
Masahiro YodaDepartment of Clinical Laboratory Investigation, Graduate School of Medicine, Shinshu University, Matsumoto, Japan.
Tomu KamijoDepartment of Medical Sciences, Graduate School of Medicine, Science and Technology, Shinshu University, Matsumoto, Japan.
Shinpei AraiDepartment of Clinical Laboratory Investigation, Graduate School of Medicine, Shinshu University, Matsumoto, Japan.
Kazuyoshi YamauchiDepartment of Clinical Laboratory Investigation, Graduate School of Medicine, Shinshu University, Matsumoto, Japan.
Nobuo OkumuraDepartment of Clinical Laboratory Investigation, Graduate School of Medicine, Shinshu University, Matsumoto, Japan. nobuoku@shinshu-u.ac.jp.
Shinshu University · JPShinshu University Hospital · JP

Funding

anders jahres fond til vitenskapens fremme JP20K07799
6 · The paper itself

Abstract

introductionWe identified a novel heterozygous AαE11del variant in a patient with congenital dysfibrinogenemia. This mutation is located in fibrinopeptide A (FpA). We analyzed the effect of AαE11del on the catalyzation of thrombin and batroxobin and simulated the stability of the complex structure between the FpA fragment (AαG6-V20) peptide and thrombin. MATERIALS AND

methodsWe performed fibrin polymerization and examined the kinetics of FpA release catalyzed by thrombin and batroxobin using purified plasma fibrinogen. To clarify the association between the AαE11 residue and thrombin, we calculated binding free energy using molecular dynamics simulation trajectories.

resultsIncreasing the thrombin concentration improved release of FpA from the patient's fibrinogen to approximately 90%, compared to the previous 50% of that of normal fibrinogen. Fibrin polymerization of variant fibrinogen also improved. In addition, greater impairment of variant FpA release from the patient's fibrinogen was observed with thrombin than with batroxobin. Moreover, the calculated binding free energy showed that the FpA fragment-thrombin complex became unstable due to the missing AαE11 residue.

conclusionsOur findings indicate that the AαE11 residue is involved in FpA release in thrombin catalyzation more than in batroxobin catalyzation, and that the AαE11 residue stabilizes FpA fragment-thrombin complex formation.

Indexed as

Sequence DeletionAfibrinogenemiaBatroxobinBlood CoagulationBlood Coagulation TestsDNA Mutational AnalysisFibrinFibrinopeptide AHeterozygoteHumansKineticsMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingProtein ConformationProtein MultimerizationBatroxobinFibrinFibrinopeptide AThrombinBinding free energyDysfibrinogenemiaFibrinogenFibrinopeptide AThrombin

Identifiers

PMID34333754
OpenAlexW3189865338

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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.