Polyphosphate, Zn
blood coagulation factors
polyphosphates
prekallikrein
thrombosis
zinc
Journal
Journal of thrombosis and haemostasis : JTH
ISSN: 1538-7836
Titre abrégé: J Thromb Haemost
Pays: England
ID NLM: 101170508
Informations de publication
Date de publication:
12 2019
12 2019
Historique:
received:
23
05
2019
accepted:
09
08
2019
pubmed:
20
8
2019
medline:
9
9
2020
entrez:
18
8
2019
Statut:
ppublish
Résumé
Inorganic polyphosphate modulates the contact pathway of blood clotting, which is implicated in thrombosis and inflammation. Polyphosphate polymer lengths are highly variable, with shorter polymers (approximately 60-100 phosphates) secreted from human platelets, and longer polymers (up to thousands of phosphates) in microbes. We previously reported that optimal triggering of clotting via the contact pathway requires very long polyphosphates, although the impact of shorter polyphosphate polymers on individual proteolytic reactions of the contact pathway was not interrogated. We conducted in vitro measurements of enzyme kinetics to investigate the ability of varying polyphosphate sizes, together with high molecular weight kininogen and Zn The individual contact pathway reactions were differentially dependent on polyphosphate length. Very long-chain polyphosphate was required to support factor XII autoactivation, whereas platelet-size polyphosphate significantly accelerated the activation of factor XII by kallikrein, and the activation of prekallikrein by factor XIIa. Intriguingly, polyphosphate did not support prekallikrein autoactivation. We also report that high molecular weight kininogen was required only when kallikrein was the enzyme (ie, FXII activation by kallikrein), whereas Zn Platelet polyphosphate and Zn
Sections du résumé
BACKGROUND
Inorganic polyphosphate modulates the contact pathway of blood clotting, which is implicated in thrombosis and inflammation. Polyphosphate polymer lengths are highly variable, with shorter polymers (approximately 60-100 phosphates) secreted from human platelets, and longer polymers (up to thousands of phosphates) in microbes. We previously reported that optimal triggering of clotting via the contact pathway requires very long polyphosphates, although the impact of shorter polyphosphate polymers on individual proteolytic reactions of the contact pathway was not interrogated.
OBJECTIVES AND METHODS
We conducted in vitro measurements of enzyme kinetics to investigate the ability of varying polyphosphate sizes, together with high molecular weight kininogen and Zn
RESULTS
The individual contact pathway reactions were differentially dependent on polyphosphate length. Very long-chain polyphosphate was required to support factor XII autoactivation, whereas platelet-size polyphosphate significantly accelerated the activation of factor XII by kallikrein, and the activation of prekallikrein by factor XIIa. Intriguingly, polyphosphate did not support prekallikrein autoactivation. We also report that high molecular weight kininogen was required only when kallikrein was the enzyme (ie, FXII activation by kallikrein), whereas Zn
CONCLUSIONS
Platelet polyphosphate and Zn
Identifiants
pubmed: 31420909
doi: 10.1111/jth.14612
pmc: PMC6893101
mid: NIHMS1056790
pii: S1538-7836(22)03092-6
doi:
Substances chimiques
Kininogen, High-Molecular-Weight
0
Polyphosphates
0
Factor Xa
EC 3.4.21.6
Zinc
J41CSQ7QDS
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2131-2140Subventions
Organisme : NHLBI NIH HHS
ID : UM1 HL120877
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL058837
Pays : United States
Organisme : NHLBI NIH HHS
ID : R35 HL140025
Pays : United States
Organisme : NHLBI NIH HHS
ID : R35 HL135823
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL081326
Pays : United States
Informations de copyright
© 2019 International Society on Thrombosis and Haemostasis.
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