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Sökning: WFRF:(Koch Karl Wilhelm)

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1.
  • Dell'Orco, Daniele, et al. (författare)
  • Calcium binding, structural stability and guanylate cyclase activation in GCAP1 variants associated with human cone dystrophy
  • 2010
  • Ingår i: Cellular and Molecular Life Sciences. - : Springer Science and Business Media LLC. - 1420-9071 .- 1420-682X. ; 67:6, s. 973-984
  • Tidskriftsartikel (refereegranskat)abstract
    • Guanylate cyclase activating protein 1 (GCAP1) is a neuronal Ca2+ sensor (NCS) that regulates the activation of rod outer segment guanylate cyclases (ROS-GCs) in photoreceptors. In this study, we investigated the Ca2+-induced effects on the conformation and the thermal stability of four GCAP1 variants associated with hereditary human cone dystrophies. Ca2+ binding stabilized the conformation of all the GCAP1 variants independent of myristoylation. The myristoylated wild-type GCAP1 was found to have the highest Ca2+ affinity and thermal stability, whereas all the mutants showed decreased Ca2+ affinity and significantly lower thermal stability in both apo and Ca2+-loaded forms. No apparent cooperativity of Ca2+ binding was detected for any variant. Finally, the nonmyristoylated mutants were still capable of activating ROS-GC1, but the measured cyclase activity was shifted toward high, nonphysiological Ca2+ concentrations. Thus, we conclude that distorted Ca2+-sensor properties could lead to cone dysfunction.
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2.
  • Dell'Orco, Daniele, et al. (författare)
  • Dynamics of Conformational Ca2+-Switches in Signaling Networks Detected by a Planar Plasmonic Device
  • 2012
  • Ingår i: Analytical Chemistry. - : American Chemical Society (ACS). - 1520-6882 .- 0003-2700. ; 84:6, s. 2982-2989
  • Tidskriftsartikel (refereegranskat)abstract
    • Ca2+-sensor proteins regulate a variety of intracellular processes by adopting specific conformations in response to finely tuned changes in Ca2+-concentration. Here we present a surface plasmon resonance (SPR)-based approach, which allows for simultaneous detection of conformational dynamics of four Ca2+-sensor proteins (calmodulin, recoverin, GCAP1, and GCAP2) operating in the vertebrate phototransduction cascade, over variations in Ca2+ concentration in the 0.1-0.6 mu M range. By working at conditions that quantitatively mimic those found in the cell, we show that the method is able to detect subtle differences in the dynamics of each Ca2+-sensor, which appear to be influenced by the presence of free Mg2+ at physiological concentration and by posttranslational modifications such as myristoylation. Comparison between the macroscopic Ca2+-binding constants, directly measured by competition with a chromophoric chelator, and the concerted binding-conformational switch detected by SPR at equilibrium reveals the relative contribution of the conformational change process to the SPR signal. This process appears to be influenced by the presence of other cations that perturb Ca2+-binding and the conformational transition by competing with Ca2+, or by pure electrostatic screening. In conclusion, the approach described here allows a comparative analysis of protein conformational changes occurring under physiologically relevant molecular crowding conditions in ultrathin biosensor layers.
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