Apparent cooperativity of Ca2+ binding associated with crystallization of Ca2+-binding protein from sarcoplasmic reticulum☆
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Role of junctin protein interactions in cellular dynamics of calsequestrin polymer upon calcium perturbation
2012, Journal of Biological ChemistryCitation Excerpt :The bidirectional reactions of CSQ polymerization and depolymerization may thus be critical in Ca2+ homeostasis. Previous studies have proposed that positive cooperative binding of Ca2+ by CSQ is concomitant with a shift in equilibrium from the soluble to the crystalline forms of CSQ (27), which folds into a more compact structure (28–30). Thus, CSQ polymerization appears beneficial for Ca2+ deposit.
Potential adverse interaction of human cardiac calsequestrin
2010, European Journal of PharmacologyCitation Excerpt :However, considering the similar isothermal titration calorimetry response of daunorubicin either with or without Ca2+ (Fig. 4D) and negative ∆S (Table 1), the anthracycline-binding pocket or consequence of such binding might be different from those of other compounds. Various evidence showed that the high-capacity and low-affinity Ca2+ binding by CASQ has been linked to its dynamic polymer behavior, which has been also linked to its localization and/or trafficking (Cho et al., 2007; Franzini-Armstrong et al., 1987; Gatti et al., 2001; Hayakawa et al., 1994; Kim et al., 2007; MacLennan and Reithmeier, 1998; Maurer et al., 1985; Paolini et al., 2007; Park et al., 2004; Park et al., 2003; Royer and Ríos, 2009; Saito et al., 1984; Tanaka et al., 1986; Tijskens et al., 2003; Wang et al., 1998). Increasing Ca2+ occupancy fills the electronegative pockets formed in the inter-subunit interfaces of CASQ oligomer, cross-bridging and eventually forming a long linear polymer.
Dysregulated sarcoplasmic reticulum calcium release: Potential pharmacological target in cardiac disease
2008, Pharmacology and TherapeuticsCitation Excerpt :Due to the proximity of CASQ matrices to RyR2, CASQ2 polymers are thought to provide the stores of releasable Ca2+ which activate myocyte contraction. In this regard, condensed CASQ represents the high Ca2+ binding capacity form of the protein and possesses at least twice the Ca2+ binding capacity of monomeric CASQ in both skeletal and cardiac muscle (Tanaka et al., 1986; Park et al., 2004). CASQ condensation reportedly involves head-to-tail oligomerization that occurs through front-to-front and back-to-back dimerization contacts involving the N- and C-terminal regions of the protein, respectively (Wang et al., 1998; Park et al., 2004).
Characterization of Human Cardiac Calsequestrin and its Deleterious Mutants
2007, Journal of Molecular BiologyDrastic reduction in the luminal Ca<sup>2+</sup>-binding proteins calsequestrin and sarcalumenin in dystrophin-deficient cardiac muscle
2004, Biochimica et Biophysica Acta - Molecular Basis of DiseaseUse of continuous-elution gel electrophoresis as a preparative tool for blot overlay analysis
2003, Analytical BiochemistryCitation Excerpt :The diagrammatic representations in Figs. 5b and c summarize the conclusion that one can draw from the differential overlay pattern using the two different probes. Calsequestrin seems to interact with all four central elements of triadic signal transduction: (i) it forms self-aggregates that exhibit cooperative kinetics with respect to ion binding [26], (ii) it is stabilized by interactions with junctin [27], and (iii) it communicates with Ca2+-release units indirectly via triadin [25] and directly by coupling to the ryanodine receptor [28]. This shows that membrane-associated proteins can be isolated by preparative gel electrophoresis without loosing their biological binding affinities and that they can be successfully employed as peroxidase-conjugated probes in differential overlay blot analyses.
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This work was supported in part by grants from the National Institutes of Health (AM 14632) and the Muscular Dystrophy Association, a Biomedical Research Support Grant from the National Institutes of Health administered by Vanderbilt University (to S.F.), Grants-in-Aid for Special Project Research (60123007) from the Ministry of Education, Science and Culture, Japan (to T.O.), grants from the Nato Foundation and the Uehara Memorial Foundation (to M.T.), and by a fellowship from the American Heart Association, Tennessee Affiliate (to A.M.).
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Present address: Department of Microbiology, Swiss Federal Institut of Technology, CH-8092 Zurich, Switzerland.