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Red Blood Cell and Platelet Mechanics
Published in Michel R. Labrosse, Cardiovascular Mechanics, 2018
The platelet cytoskeleton consists of three major components: a spectrin-based skeleton adherent to the plasma membrane, microtubule coils (marginal band) along the perimeter, and the cytoplasmic actin network. Actin is the most abundant protein, with 2 × 106 molecules per platelet. Approximately 800,000 actin monomers assemble to form 2000–4000 actin filaments (Hartwig and DeSisto 1991). The crosslinker protein filamin A was shown to be important for controlling the distribution of the GPIb-V-IX receptor on the platelet surface and attaching it to the actin cytoskeleton (Nakamura et al. 2006). On activation, platelets rearrange their cytoskeleton with the help of cytoskeletal-regulatory proteins (such as gelsolin, cofilin, profilin, Arp2/3, Wiskott–Aldrich Syndrome protein (WASP), and CapZ), change their discoid form to spherical shape, and tether the integrin αIIbβ3 to the underlying, newly assembled actin filaments. Finally, cytoplasmic myosin binds to actin polymers and applies contractile forces (Cove and Crawford 1975). In general, the platelet has turned out be a good model to study mechanobiological questions, since platelets are anucleated cells, have a high actin content, and highly express mechanical-relevant receptors, such as integrins (αIIbβ3: 80,000 copies), on a small surface (Ciciliano et al. 2014).
Effects of homocysteine and memantine on oxidative stress related TRP cation channels in in-vitro model of Alzheimer’s disease
Published in Journal of Receptors and Signal Transduction, 2021
İshak Suat Övey, Mustafa Nazıroğlu
Stock solution of the AP-18, N-(p-amylcinnamoyl) Anthranilic acid (ACA), CapZ, CAPSN and CIN were prepared in DMSO and they were diluted into appropriate concentrations. TRPA1 was gated by adding extracellular CIN (0.1 mM), and the channel was inhibited extracellular administration of AP-18 (0.02 mM) into extracellular buffer. TRPM2 was gated by adding extracellular CumPx (0.1 mM), and it was extracellularly inhibited by ACA (0.025 mM). TRPV1 was gated by adding extracellular CAPSN (0.1 mM), and it was extracellularly inhibited by CapZ (0.1 mM).