Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods.


Journal

Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414

Informations de publication

Date de publication:
08 04 2021
Historique:
received: 02 03 2021
revised: 31 03 2021
accepted: 06 04 2021
entrez: 30 4 2021
pubmed: 1 5 2021
medline: 18 9 2021
Statut: epublish

Résumé

Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Mutations at the heparin-binding region lead to functional defect, type II heparin-binding site (IIHBS) AT deficiency. The aim of this study was to investigate and compare the molecular background of AT Budapest 3 (p.Leu131Phe, ATBp3), AT Basel (p.Pro73Leu), and AT Padua (p.Arg79His) mutations. Advanced in silico methods and heparin-binding studies of recombinant AT proteins using surface plasmon resonance method were used. Crossed immunoelectrophoresis and Differential Scanning Fluorimetry (NanoDSF) were performed in plasma samples. Heparin affinity of AT Padua was the lowest (KD = 1.08 × 10

Identifiants

pubmed: 33917853
pii: biom11040544
doi: 10.3390/biom11040544
pmc: PMC8068293
pii:
doi:

Substances chimiques

Recombinant Proteins 0
antithrombin III Basel 0
antithrombin III Padua 0
Antithrombin III 9000-94-6
Heparin 9005-49-6

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : European Union under European Regional Development Fund
ID : GINOP-2.3.2-15-2016-00039
Organisme : National Research, Development and Innovation Office, Hungarian Ministry of Innovation and Technology
ID : OTKA K116228
Organisme : European Union under European Regional Development Fund
ID : GINOP-2.3.2–15-2016–00044
Organisme : European Union under European Regional Development Fund
ID : GINOP-2.3.3–15-2016–00020

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Auteurs

Réka Gindele (R)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Krisztina Pénzes-Daku (K)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Gábor Balogh (G)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Judit Kállai (J)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Réka Bogáti (R)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Bálint Bécsi (B)

Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Ferenc Erdődi (F)

Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Éva Katona (É)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

Zsuzsanna Bereczky (Z)

Division of Clinical Laboratory Science, Department of Laboratory Medicine, Faculty of Medicine, University of Debrecen, 4032 Debrecen, Hungary.

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