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Objective: To investigate the regulatory effect of zyxin on the distribution of platelet cytoskeleton.
Methods: Platelets were isolated from zyxin-knockout (Zyx) and wild type (WT) mice respectively and corresponding platelet cytoskeleton components were separated. The expressions of β-actin, α-actinin, filamin A and myosin ⅡA in cytoskeleton components were detected by Western blot. Actin polymerization was induced by the actin polymerization inducer Jasplakinolide (Jas) in WT and Zyx platelets. Also, the expressions of the cytoskeleton proteins in cytoskeleton components were detected by Western blot. WT and Zyx platelets were allowed to spread on fibrinogen-coated surface. Platelet F-actin was labeled with Alexa Fluor 488-conjugated phalloidin and the fluorescent intensity was compared between WT and Zyx platelets.
Results: After zyxin gene was knockout, the expressions of cytoskeleton proteins β-actin, α-actinin, filamin A, and myosin Ⅱ A in resting and Jas-induced platelets were significantly increased. In the platelet spreading on fibrinogen surface, F-actin was increased in Zyx platelets as compared with that in WT platelets.
Conclusion: Zyxin significantly regulates the distribution of platelet cytoskeleton, which plays an important role in maintaining platelet cytoskeleton homeostasis.
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http://dx.doi.org/10.19746/j.cnki.issn.1009-2137.2021.03.035 | DOI Listing |
Cell Chem Biol
August 2025
Division of Neuroscience and Cellular Structure, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address:
Endolysosomes are dynamic organelles that undergo movement along the cytoskeleton, fusion, fission, and tubulation during their lifetime. These processes are regulated by complex molecular machineries, including the structurally related hetero-octameric complexes BLOC-1 and BORC. BLOC-1 associates with early endosomes to mediate the biogenesis of lysosome-related organelles (LROs), such as melanosomes and platelet dense bodies.
View Article and Find Full Text PDFAntioxidants (Basel)
August 2025
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstr. 15, 48149 Münster, Germany.
Almost every cell of a multicellular organism is in contact with the extracellular matrix (ECM), which provides the shape and mechanic stability of tissue, organs and the entire body. At the molecular level, cells contact the ECM via integrins. Integrins are transmembrane cell adhesion molecules that connect the ECM to the cytoskeleton, which they bind with their extracellular and intracellular domains.
View Article and Find Full Text PDFFront Cell Dev Biol
August 2025
Unité de Biologie Moléculaire, Cellulaire et du Développement (MCD, UMR 5077), Centre de Biologie Intégrative (CBI, FR 3743), Université de Toulouse, CNRS, UPS, Toulouse, France.
Invadosomes are a family of subcellular actin-based structures essential for cell-extracellular matrix (ECM) interaction and remodeling. In non-invasive cells, they are referred to as podosomes, which enable adhesion, migration, and ECM remodeling via secretion of metalloproteinases or mechano-traction. In invasive tumoral cells, these structures are called invadopodia due to their function.
View Article and Find Full Text PDFCell Tissue Res
August 2025
Department of Biochemistry and Molecular Biology, Cumming School of Medicine, and Faculty of Veterinary Medicine, University of Calgary, Calgary, AB, Canada.
Mechanisms governing somatic cell interactions in the testis are not well defined. The platelet-derived growth factor (PDGF) pathway mediates epithelial-mesenchymal interactions and is involved in testicular morphogenesis in rodents. However, its roles in the testis of higher mammals remain largely unknown.
View Article and Find Full Text PDFJ Clin Invest
August 2025
Department of Cardiovascular Sciences, School of Medical Sciences, College of Medicine and Health, University of Birmingham, Birmingham, United Kingdom.
SLFN14-related thrombocytopenia is a rare bleeding disorder caused by SLFN14 mutations altering hemostasis in patients with platelet dysfunction. Schlafen (SLFN) proteins are highly conserved in mammals where SLFN14 is specifically expressed in megakaryocyte (MK) and erythroblast lineages. The role of SLFN14 in megakaryopoiesis and platelet function has not been elucidated.
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