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Related Experiment Video

Updated: May 9, 2026

Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets

Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets

Published on: November 29, 2024

Platelets are a previously unrecognised source of MIF.

T Strüßmann¹, S Tillmann, T Wirtz

¹Prof. Dr. rer. nat. Jürgen Bernhagen, Institute of Biochemistry and Molecular Cell Biology, RWTH Aachen University, Pauwelsstrasse 30, D-52074 Aachen, Germany, Tel.: +49 241 80 88 840/31/41, Fax: +49 241 80 82 427, E-mail: jbernhagen@ukaachen.de, Web: www.ukaachen.de/sites/lfg/bcmzb.

Thrombosis and Haemostasis

|July 13, 2013

Summary

Platelets secrete macrophage migration inhibitory factor (MIF), a key inflammatory cytokine. This finding reveals platelets as a novel source of MIF, crucial for inflammatory cell recruitment in conditions like atherogenesis.

Keywords:

Atherosclerosis chemokines cytokines inflammatory mediators macrophage

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Microfluidics in Assessing Platelet Function

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Isolation and Characterization of Neutrophil-derived Microparticles for Functional Studies

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Published on: March 2, 2018

Area of Science:

Immunology
Cell Biology
Cardiovascular Research

Background:

Macrophage migration inhibitory factor (MIF) is an inflammatory cytokine involved in atherogenesis.
Platelets are implicated in atherogenesis and release chemokines.
The role of platelets in MIF production and secretion was previously uninvestigated.

Purpose of the Study:

To determine if platelets express and secrete MIF.
To investigate the subcellular localization and mRNA presence of MIF in platelets.
To assess the functional role of platelet-derived MIF in inflammatory cell recruitment.

Main Methods:

Western blot and ELISA were used to detect and quantify MIF protein in human and mouse platelets.
Confocal microscopy examined MIF localization within platelets.
Quantitative PCR (qPCR) assessed MIF mRNA levels.
Transwell assays evaluated monocyte chemotaxis using platelet supernatants, with and without MIF-neutralizing antibodies.

Main Results:

MIF protein was detected and quantified in human and mouse platelets.
MIF localized to granular structures within platelets but did not co-localize with known platelet cytokines.
Platelets contain low levels of MIF mRNA.
Thrombin and collagen stimulated MIF release, while ADP and oxidized LDL did not.
Platelet supernatants significantly enhanced monocyte chemotaxis, an effect blocked by MIF-neutralizing antibodies.

Conclusions:

Platelets are a previously unrecognized source of secreted MIF, particularly upon activation by thrombin and collagen.
Platelet-derived MIF contributes significantly to the chemotactic capacity of activated platelets.
MIF plays a role in atherogenic cell recruitment, highlighting a novel mechanism in inflammatory processes.