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Septins Contribute to Platelet Shape and Functionality

O. Kim1, E. Mordakhanova2, O. Vagin3, R. Litvinov1,2, J. Weisel1

1University of Pennsylvania, Department of Cell and Developmental Biology, Philadelphia, United States, 2Kazan Federal University, Institute of Fundamental Medicine and Biology, Kazan, Russian Federation, 3University of California, Los Angeles, United States

Abstract Number: PB1648

Meeting: ISTH 2020 Congress

Theme: Platelets and Megakaryocytes » Platelet Function and Interactions

Background: Platelets are blood cells that play an important role in hemostasis and thrombosis. Activated platelets change shape due to reorganization of cytoskeleton. Septins, a family of GTP-binding cytoskeletal proteins, are implicated in cytokinesis and mitosis of nucleated cells, but their role in platelets is largely unknown.

Aims: To study the septins in resting and activated platelets and their contribution to platelet morphology and functions.

Methods: Confocal microscopy, flow cytometry, biomechanical and biochemical assays were used to examine structural and functional changes in human platelets. Septins 2 and 9 were immunostained in resting and activated platelets, either spread on a fibrinogen-coated surface or contracting within a 3D plasma clot. Clot contraction was assessed by tracking the clot size.

Results: In resting platelets, septin 2 concentrated at the cell periphery, colocalizing with the microtubule marginal ring, while septin 9 was distributed as small patches over the cell volume, often with a peripheral localization. In thrombin-activated platelets, septins were also observed in filopodia. Activation with thrombin resulted in a 2-fold increase of septin intensity. Inhibition of septin dynamics with forchlorfenuron (FCF) caused dose-dependent perturbations, including a substantial decrease of platelet roundness and surface curvature. In FCF-pretreated platelets activated with TRAP, expression of activated integrin αIIbβ3 was significantly suppressed. FCF impeded clot contraction with a 6-fold increase of the lag-time and up to a 3-fold decrease of the extent of contraction. Alterations in septin structure caused by FCF abrogated platelet spreading by 50% and accelerated thrombin-induced platelet fragmentation.

Conclusions: Septins are important for stabilizing platelet shape and supporting platelet integrity; septins are involved in platelet biomechanical functions, such as contractility and adhesion.

Funding: Work supported by the Program of Competitive Growth at KFU and grants 18-415-160004, 19-015-00075, 20-015-00257 from the Russian Foundation for Basic Research, and 17SDG33680177 from AHA.

To cite this abstract in AMA style:

Kim O, Mordakhanova E, Vagin O, Litvinov R, Weisel J. Septins Contribute to Platelet Shape and Functionality [abstract]. Res Pract Thromb Haemost. 2020; 4 (Suppl 1). https://abstracts.isth.org/abstract/septins-contribute-to-platelet-shape-and-functionality/. Accessed January 26, 2021.
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