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Article ; Online: Combining human platelet proteomes and transcriptomes: possibilities and challenges.

Huang, Jingnan / Heemskerk, Johan W M / Swieringa, Frauke

2023 Volume 34, Issue 1, Page(s) 2224454

Abstract: The anucleate human platelets contain a broad pattern of mRNAs and other RNA transcripts. The high quantitative similarity of mRNAs in megakaryocytes and platelets from different sources points to a common origin, and suggests a random redistribution of ... ...

Abstract	The anucleate human platelets contain a broad pattern of mRNAs and other RNA transcripts. The high quantitative similarity of mRNAs in megakaryocytes and platelets from different sources points to a common origin, and suggests a random redistribution of mRNA species upon proplatelet formation. A comparison of the classified platelet transcriptome (17.6k transcripts) with the identified platelet proteome (5.2k proteins) indicates an under-representation of:
MeSH term(s)	Humans ; Proteome ; Blood Platelets ; Transcriptome ; Megakaryocytes ; Databases, Factual ; RNA, Messenger
Chemical Substances	Proteome ; RNA, Messenger
Language	English
Publishing date	2023-04-14
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1034283-7
ISSN	1369-1635 ; 0953-7104
ISSN (online)	1369-1635
ISSN	0953-7104
DOI	10.1080/09537104.2023.2224454
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Article ; Online: High fibrinogen γ' levels in patient plasma increase clot formation at arterial and venous shear.

Macrae, Fraser L / Swieringa, Frauke / Heemskerk, Johan W M / Ariëns, Robert A S

Blood advances

2021 Volume 5, Issue 17, Page(s) 3468–3477

Abstract: Fibrinogen γ' accounts for 3% to 40% of plasma fibrinogen. Earlier studies indicated that fibrinogen γ' forms altered fibrin clots under static conditions, whereas clinically, altered plasma γ' levels are associated with arterial and venous thrombosis. ... ...

Abstract	Fibrinogen γ' accounts for 3% to 40% of plasma fibrinogen. Earlier studies indicated that fibrinogen γ' forms altered fibrin clots under static conditions, whereas clinically, altered plasma γ' levels are associated with arterial and venous thrombosis. However, the effects of static vs flow conditions on the role of γ' throughout the pathophysiological range is unknown. This study explores the effects of γ' levels on clot formation and structure in static and flow conditions. Coagulation of plasma samples with low (n = 41; 3%), normal (n = 45; 10%), or high (n = 33; 30%) γ' levels were compared with that of purified fibrinogen mixtures with increasing ratios of γ' (3%, 10%, 30%). Clots were analyzed by confocal microscopy, permeation, turbidity, and lysis techniques. In a novel 2-step flow-perfusion model, fibrinogen-deficient plasma repleted with increasing ratios of γ' (3%, 10%, 30%) or plasmas with low (n = 5, 3%) or high (n = 5, 30%) γ' were flowed over preformed platelet aggregates at arterial (500 s-1) and venous (150 s-1) shear rates. Increasing γ' percentages within the pathophysiological range (3%-30%) did not result in any change in clot-formation rates; however, it led to significantly higher clot density, thinner fibers, and slower lysis in static conditions. Under flow at arterial shear, high γ' (30%) led to faster (+44.1%-75.3%) and increased (+104%-123%) fibrin deposition, with clots exhibiting a larger volume (+253%-655%) and height (+130%-146%). These trends were magnified at venous shear. Overall, our findings demonstrate the significant impact of pathophysiological fibrinogen γ' levels on clot structure and provide new flow-dependent mechanisms to explain how γ' increases thrombosis risk.
MeSH term(s)	Blood Coagulation Tests ; Fibrin ; Fibrinogen ; Fibrinogens, Abnormal ; Humans
Chemical Substances	Fibrinogens, Abnormal ; fibrinogen gamma' ; Fibrin (9001-31-4) ; Fibrinogen (9001-32-5)
Language	English
Publishing date	2021-08-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2915908-8
ISSN	2473-9537 ; 2473-9529
ISSN (online)	2473-9537
ISSN	2473-9529
DOI	10.1182/bloodadvances.2020003346
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Article ; Online: Reversible Platelet Integrin αIIbβ3 Activation and Thrombus Instability.

Zou, Jinmi / Swieringa, Frauke / de Laat, Bas / de Groot, Philip G / Roest, Mark / Heemskerk, Johan W M

International journal of molecular sciences

2022 Volume 23, Issue 20

Abstract: Integrin αIIbβ3 activation is essential for platelet aggregation and, accordingly, for hemostasis and arterial thrombosis. The αIIbβ3 integrin is highly expressed on platelets and requires an activation step for binding to fibrinogen, fibrin or von ... ...

Abstract	Integrin αIIbβ3 activation is essential for platelet aggregation and, accordingly, for hemostasis and arterial thrombosis. The αIIbβ3 integrin is highly expressed on platelets and requires an activation step for binding to fibrinogen, fibrin or von Willebrand factor (VWF). A current model assumes that the process of integrin activation relies on actomyosin force-dependent molecular changes from a bent-closed and extended-closed to an extended-open conformation. In this paper we review the pathways that point to a functional reversibility of platelet αIIbβ3 activation and transient aggregation. Furthermore, we refer to mouse models indicating that genetic defects that lead to reversible platelet aggregation can also cause instable thrombus formation. We discuss the platelet agonists and signaling pathways that lead to a transient binding of ligands to integrin αIIbβ3. Our analysis points to the (autocrine) ADP P2Y
MeSH term(s)	Mice ; Animals ; Platelet Glycoprotein GPIIb-IIIa Complex/metabolism ; von Willebrand Factor/metabolism ; Platelet Aggregation Inhibitors/pharmacology ; Platelet Aggregation Inhibitors/therapeutic use ; Platelet Aggregation Inhibitors/metabolism ; Actomyosin/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; Platelet Activation ; Platelet Aggregation ; Blood Platelets/metabolism ; Thrombosis/metabolism ; Fibrinogen/metabolism ; Protein Kinase C/metabolism ; Adenosine Diphosphate/metabolism ; Fibrin/metabolism ; Phosphatidylinositols/metabolism
Chemical Substances	Platelet Glycoprotein GPIIb-IIIa Complex ; von Willebrand Factor ; Platelet Aggregation Inhibitors ; Actomyosin (9013-26-7) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Fibrinogen (9001-32-5) ; Protein Kinase C (EC 2.7.11.13) ; Adenosine Diphosphate (61D2G4IYVH) ; Fibrin (9001-31-4) ; Phosphatidylinositols
Language	English
Publishing date	2022-10-19
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms232012512
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Article ; Online: Reversing direct factor Xa or thrombin inhibitors: Factor V addition to prothrombin complex concentrate is beneficial in vitro.

Brinkman, Herm Jan M / Swieringa, Frauke / Zuurveld, Marleen / Veninga, Alicia / Brouns, Sanne L N / Heemskerk, Johan W M / Meijers, Joost C M

Research and practice in thrombosis and haemostasis

2022 Volume 6, Issue 3, Page(s) e12699

Abstract: Background: Prothrombin complex concentrate (PCC) is a human plasma-derived mixture of partially purified vitamin K-dependent coagulation factors (VKCF). Current therapeutic indication is treatment and perioperative prophylaxis of bleeding in acquired ... ...

Abstract	Background: Prothrombin complex concentrate (PCC) is a human plasma-derived mixture of partially purified vitamin K-dependent coagulation factors (VKCF). Current therapeutic indication is treatment and perioperative prophylaxis of bleeding in acquired VKCF deficiency. Off-label uses include treatment of direct factor Xa- or thrombin inhibitor-associated bleeds, treatment of trauma-induced coagulopathy, and hemorrhagic complications in patients with liver disease. Objective: Considering PCC as a general prohemostatic drug, we argued that its clinical efficacy can benefit from supplementation with coagulation factors that are absent in the current PCC formulation. In this study, we focused on factor V. Methods: We mimicked a coagulopathy in vitro by spiking whole blood or derived plasma with the direct oral anticoagulants (DOAC) rivaroxaban or dabigatran. We studied DOAC reversal by PCC and factor V concentrate (FVC) using a thrombin generation assay, thromboelastography, fibrin generation clot lysis test, and microfluidic thrombus formation under flow. Results: In DOAC-treated plasma, PCC increased the amount of thrombin generated. The addition of FVC alone or in combination with PCC caused a partial correction of the thrombin generation lag time and clotting time. In DOAC-treated whole blood, the combination of PCC and FVC synergistically improved clotting time under static conditions, whereas complete correction of fibrin formation was observed under flow. Clot strength and clot resistance toward tissue plasminogen activator-induced lysis were both increased with PCC and further enhanced by additional FVC. Conclusion: Our in vitro study demonstrates a beneficial effect of the combined use of PCC and FVC in DOAC reversal.
Language	English
Publishing date	2022-04-25
Publishing country	United States
Document type	Journal Article
ISSN	2475-0379
ISSN (online)	2475-0379
DOI	10.1002/rth2.12699
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Article ; Online: Multi-omics approaches to study platelet mechanisms.

Solari, Fiorella A / Krahn, Daniel / Swieringa, Frauke / Verhelst, Steven / Rassaf, Tienush / Tasdogan, Alpaslan / Zahedi, Rene P / Lorenz, Kristina / Renné, Thomas / Heemskerk, Johan W M / Sickmann, Albert

Current opinion in chemical biology

2023 Volume 73, Page(s) 102253

Abstract: Platelets are small anucleate cell fragments (2-4 μm in diameter) in the blood, which play an essential role in thrombosis and hemostasis. Genetic or acquired platelet dysfunctions are linked to bleeding, increased risk of thromboembolic events and ... ...

Abstract	Platelets are small anucleate cell fragments (2-4 μm in diameter) in the blood, which play an essential role in thrombosis and hemostasis. Genetic or acquired platelet dysfunctions are linked to bleeding, increased risk of thromboembolic events and cardiovascular diseases. Advanced proteomic approaches may pave the way to a better understanding of the roles of platelets in hemostasis, and pathophysiological processes such as inflammation, metastatic spread and thrombosis. Further insights into the molecular biology of platelets are crucial to aid drug development and identify diagnostic markers of platelet activation. Platelet activation is known to be an extremely rapid process and involves multiple post-translational mechanisms at sub second time scale, including proteolysis and phosphorylation. Multi-omics technologies and biochemical approaches can be exploited to precisely probe and define these posttranslational pathways. Notably, the absence of a nucleus in platelets significantly reduces the number of present proteins, simplifying mass spectrometry-based proteomics and metabolomics approaches.
MeSH term(s)	Humans ; Blood Platelets/metabolism ; Blood Platelets/pathology ; Proteomics ; Multiomics ; Platelet Activation ; Thrombosis/metabolism ; Thrombosis/pathology
Language	English
Publishing date	2023-01-21
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1439176-4
ISSN	1879-0402 ; 1367-5931
ISSN (online)	1879-0402
ISSN	1367-5931
DOI	10.1016/j.cbpa.2022.102253
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Zs.A 4986: Show issues

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Article ; Online: Use of microfluidics to assess the platelet-based control of coagulation.

Nagy, Magdolna / Heemskerk, Johan W M / Swieringa, Frauke

Platelets

2017 Volume 28, Issue 5, Page(s) 441–448

Abstract: This paper provides an overview of the various types of microfluidic devices that are employed to study the complex processes of platelet activation and blood coagulation in whole blood under flow conditions. We elaborate on how these devices are used to ...

Abstract	This paper provides an overview of the various types of microfluidic devices that are employed to study the complex processes of platelet activation and blood coagulation in whole blood under flow conditions. We elaborate on how these devices are used to detect impaired platelet-dependent fibrin formation in blood from mice or patients with specific bleeding disorders. We provide a practical guide on how to assess formation of a platelet-fibrin thrombus under flow, using equipment that is present in most laboratories. In addition, we describe current insights on how blood flow and shear rate alter the location of platelet populations, von Willebrand factor, coagulation factors, and fibrin in a growing thrombus. Finally, we discuss possibilities and limitations for the clinical use of microfluidic devices to evaluate a hemostatic or prothrombotic tendency in patient blood samples.
Language	English
Publishing date	2017-07
Publishing country	England
Document type	Journal Article
ZDB-ID	1034283-7
ISSN	1369-1635 ; 0953-7104
ISSN (online)	1369-1635
ISSN	0953-7104
DOI	10.1080/09537104.2017.1293809
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Article ; Online: Toward Zero Variance in Proteomics Sample Preparation: Positive-Pressure FASP in 96-Well Format (PF96) Enables Highly Reproducible, Time- and Cost-Efficient Analysis of Sample Cohorts.

Loroch, Stefan / Kopczynski, Dominik / Schneider, Adriana C / Schumbrutzki, Cornelia / Feldmann, Ingo / Panagiotidis, Eleftherios / Reinders, Yvonne / Sakson, Roman / Solari, Fiorella A / Vening, Alicia / Swieringa, Frauke / Heemskerk, Johan W M / Grandoch, Maria / Dandekar, Thomas / Sickmann, Albert

Journal of proteome research

2022 Volume 21, Issue 4, Page(s) 1181–1188

Abstract: As novel liquid chromatography-mass spectrometry (LC-MS) technologies for proteomics offer a substantial increase in LC-MS runs per day, robust and reproducible sample preparation emerges as a new bottleneck for throughput. We introduce a novel strategy ... ...

Abstract	As novel liquid chromatography-mass spectrometry (LC-MS) technologies for proteomics offer a substantial increase in LC-MS runs per day, robust and reproducible sample preparation emerges as a new bottleneck for throughput. We introduce a novel strategy for positive-pressure 96-well filter-aided sample preparation (PF96) on a commercial positive-pressure solid-phase extraction device. PF96 allows for a five-fold increase in throughput in conjunction with extraordinary reproducibility with Pearson product-moment correlations on the protein level of
MeSH term(s)	Animals ; Chromatography, Liquid/methods ; Humans ; Mass Spectrometry/methods ; Mice ; Peptides/analysis ; Proteomics/methods ; Reproducibility of Results
Chemical Substances	Peptides
Language	English
Publishing date	2022-03-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.1c00706
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Article ; Online: Integrating platelet and coagulation activation in fibrin clot formation.

Swieringa, Frauke / Spronk, Henri M H / Heemskerk, Johan W M / van der Meijden, Paola E J

Research and practice in thrombosis and haemostasis

2018 Volume 2, Issue 3, Page(s) 450–460

Abstract: Platelets interact with the coagulation system in a multitude of ways, not only during the phases of thrombus formation, but also in specific areas within a formed thrombus. This review discusses current concepts of platelet control of thrombin ... ...

Abstract	Platelets interact with the coagulation system in a multitude of ways, not only during the phases of thrombus formation, but also in specific areas within a formed thrombus. This review discusses current concepts of platelet control of thrombin generation, fibrin formation and structure, and anticoagulation. Indicated are how combined signalling via the platelet receptors for collagen (glycoprotein VI) and thrombin induces the secretion of (anti)coagulation factors, as well as surface exposure of phosphatidylserine, thereby catalysing thrombin generation. This procoagulant platelet response is also facilitated by the adhesive complexes glycoprotein Ib-V-IX and integrin α
Language	English
Publishing date	2018-05-20
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2475-0379
ISSN (online)	2475-0379
DOI	10.1002/rth2.12107
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Article ; Online: Platelet proteomics: from discovery to diagnosis.

Looße, Christina / Swieringa, Frauke / Heemskerk, Johan W M / Sickmann, Albert / Lorenz, Christin

Expert review of proteomics

2018 Volume 15, Issue 6, Page(s) 467–476

Abstract: Introduction: Platelets are the smallest cells within the circulating blood with key roles in physiological hemostasis and pathological thrombosis regulated by the onset of activating/inhibiting processes via receptor responses and signaling cascades. ... ...

Abstract	Introduction: Platelets are the smallest cells within the circulating blood with key roles in physiological hemostasis and pathological thrombosis regulated by the onset of activating/inhibiting processes via receptor responses and signaling cascades. Areas covered: Proteomics as well as genomic approaches have been fundamental in identifying and quantifying potential targets for future diagnostic strategies in the prevention of bleeding and thrombosis, and uncovering the complexity of platelet functions in health and disease. In this article, we provide a critical overview on current functional tests used in diagnostics and the future perspectives for platelet proteomics in clinical applications. Expert commentary: Proteomics represents a valuable tool for the identification of patients with diverse platelet associated defects. In-depth validation of identified biomarkers, e.g. receptors, signaling proteins, post-translational modifications, in large cohorts is decisive for translation into routine clinical diagnostics.
MeSH term(s)	Biomarkers/blood ; Blood Platelets/metabolism ; Genomics ; Humans ; Mass Spectrometry ; Protein Processing, Post-Translational/genetics ; Proteome/genetics ; Proteomics/trends ; Signal Transduction/genetics ; Thrombosis/blood ; Thrombosis/genetics
Chemical Substances	Biomarkers ; Proteome
Language	English
Publishing date	2018-06-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2299100-1
ISSN	1744-8387 ; 1478-9450
ISSN (online)	1744-8387
ISSN	1478-9450
DOI	10.1080/14789450.2018.1480111
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Article ; Online: Platelets and coagulation in thrombus formation: aberrations in the Scott syndrome.

van Geffen, Johanna P / Swieringa, Frauke / Heemskerk, Johan W M

Thrombosis research

2016 Volume 141 Suppl 2, Page(s) S12–6

Abstract: Platelets play key roles in thrombosis and hemostasis by forming aggregates and providing a procoagulant surface, at which thrombin is generated and fibrin fibers are formed. Here we present an overview of the different mechanisms how platelets ... ...

Abstract	Platelets play key roles in thrombosis and hemostasis by forming aggregates and providing a procoagulant surface, at which thrombin is generated and fibrin fibers are formed. Here we present an overview of the different mechanisms how platelets orchestrate coagulation processes in thrombus formation in thrombosis and hemostasis. Parts of these are via Ca(2+)-dependent activation responses, leading to phosphatidylserine exposure; swelling to form balloons with increased binding of coagulation factors; and calpain-mediated integrin αIIbβ3 cleavage and inactivation. Other mechanisms are secretion of (anti) coagulation factors, and αIIbβ3-mediated thrombus retraction, and clot retraction. In a thrombus, coagulation factors are found at both platelets and fibrin fibers. Many of the procoagulant platelet activities are altered in the Scott syndrome.
MeSH term(s)	Animals ; Blood Coagulation ; Blood Coagulation Disorders/blood ; Blood Coagulation Disorders/metabolism ; Blood Coagulation Disorders/pathology ; Blood Platelets/metabolism ; Blood Platelets/pathology ; Hemostasis ; Humans ; Platelet Activation ; Thrombin/metabolism ; Thrombosis/blood ; Thrombosis/metabolism ; Thrombosis/pathology
Chemical Substances	Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2016-05
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	121852-9
ISSN	1879-2472 ; 0049-3848
ISSN (online)	1879-2472
ISSN	0049-3848
DOI	10.1016/S0049-3848(16)30355-3
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