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Related Experiment Video

Updated: Feb 13, 2026

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay

Published on: September 9, 2012

Enzymatically oxidized phospholipids restore thrombin generation in coagulation factor deficiencies.

David A Slatter¹, Charles L Percy¹, Keith Allen-Redpath¹

¹Systems Immunity Research Institute and Division of Infection and Immunity, Cardiff University, Cardiff, United Kingdom.

|March 23, 2018

Summary

Enzymatically oxidized phospholipids (eoxPL), specifically hydroxyeicosatetraenoic acid-phospholipids (HETE-PLs), restore hemostasis by enhancing coagulation factor function. These findings suggest HETE-PLs as a potential therapy for bleeding disorders.

Keywords:

Coagulation Hematology

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Area of Science:

Biochemistry
Immunology
Hematology

Background:

Hemostasis relies on coagulation factors and phospholipid surfaces for clot formation.
Pathological bleeding often involves hemostatic defects.
Enzymatically oxidized phospholipids (eoxPL) are produced by innate immune cells.

Purpose of the Study:

To investigate the role of innate immune cell-derived eoxPL, specifically HETE-PLs, in restoring hemostasis.
To explore the molecular mechanisms by which HETE-PLs enhance coagulation.
To assess the potential therapeutic utility of HETE-PLs in bleeding disorders.

Main Methods:

In vitro studies using isolated coagulation factor/cofactor complexes.
Assessment of HETE-PLs in human and murine bleeding models (hemophilia A).
Analysis of HETE-PL levels in patients post-cardiopulmonary bypass (CPB).
Surface plasmon resonance to confirm protein binding.
Measurement of membrane biophysical properties (curvature, thickness, charge, homogeneity).

Main Results:

HETE-PLs restored hemostasis in murine hemophilia A and enhanced coagulation in factor-deficient human plasma.
HETE-PL levels were decreased in platelets from patients after CPB.
HETE-PLs (HETE-PEs and HETE-PCs) enhanced extrinsic tenase, intrinsic tenase, and prothrombinase complexes.
Positional isomer specificity was observed, with 9-, 15-, and 12-HETE-PLs being more effective.
HETE-PEs bound to FII and FX, increased membrane curvature and thickness, potentially enhancing factor accessibility.

Conclusions:

Innate immune-derived eoxPL (HETE-PLs) enhance calcium-dependent coagulation factor function.
HETE-PLs demonstrate potential as a therapeutic agent for pathological bleeding and hemostatic defects.
Decreased HETE-PLs post-CPB may contribute to bleeding complications in surgical patients.