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https://www.selleckchem.com/products/ory-1001-rg-6016.html Cardiac muscle thin filaments are composed of actin, tropomyosin, and troponin that change conformation in response to Ca2+ binding, triggering muscle contraction. Human cardiac troponin C (cTnC) is the Ca2+-sensing component of the thin filament. It contains structural sites (III/IV) that bind both Ca2+ and Mg2+, and a regulatory site (II) that has been thought to bind only Ca2+. Binding of Ca2+ at this site initiates a series of conformational changes that culminate in force production. However, the mechanisms that underpin the regulation of binding at site II remain unclear. Here, we have quantified the interaction between site II and Ca2+/Mg2+ through Isothermal Titration Calorimetry and Thermodynamic Integration simulations. Direct and competitive binding titration with wild type N-terminal cTnC (N-cTnC) and full-length cTnC indicate that physiologically relevant concentrations of both Ca2+/ Mg2+ interacted with the same locus. Moreover, the D67A/D73A N-cTnC construct in which two coordinating residues within site II were removed was found to have significantly reduced affinity for both cations. In addition, 1 mM Mg2+ caused a 1.4-fold lower affinity for Ca2+. These experiments strongly suggest that cytosolic free Mg2+ occupies a significant population of the available site II. Interaction of Mg2+ with site II of cTnC likely has important functional consequences for the heart both at baseline as well as in diseased states which decrease or increase the availability of Mg2+ such as secondary hyperparathyroidism or ischemia, respectively.The LDL receptor-related protein 1 (LRP1) is a multi-functional transmembrane protein with endocytosis and signal transduction functions. Previous studies have shown that hepatic LRP1 deficiency exacerbates diet-induced steatohepatitis and insulin resistance via mechanisms related to increased lysosome and mitochondria permeability and dysfunction. The current study exami
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