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Your search keyword '"Marcelo D. Costabel"' showing total 3 results
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3 results on '"Marcelo D. Costabel"'

1. Magnesium enhances aurintricarboxylic acid’s inhibitory action on the plasma membrane Ca2+-ATPase

Author

Cecilia A. Souto-Guevara, Diego Obiol, Camila L. Bruno, Mariela S. Ferreira-Gomes, Juan Pablo F. C. Rossi, Marcelo D. Costabel, and Irene C. Mangialavori

Subjects
PMCA, Plasma membrane Ca2+-ATPase, ATA, Inhibition mechanism, ATA-magnesium complex, ATA-binding site, Medicine, Science
Abstract

Abstract Our research aimed to elucidate the mechanism by which aurintricarboxylic acid (ATA) inhibits plasma membrane Ca2+-ATPase (PMCA), a crucial enzyme responsible for calcium transport. Given the pivotal role of PMCA in cellular calcium homeostasis, understanding how it is inhibited by ATA holds significant implications for potentially regulating physiopathological cellular processes in which this pump is involved. Our experimental findings revealed that ATA employs multiple modes of action to inhibit PMCA activity, which are influenced by ATP but also by the presence of calcium and magnesium ions. Specifically, magnesium appears to enhance this inhibitory effect. Our experimental and in-silico results suggest that, unlike those reported in other proteins, ATA complexed with magnesium (ATA·Mg) is the molecule that inhibits PMCA. In summary, our study presents a novel perspective and establishes a solid foundation for future research efforts aimed at the development of new pharmacological molecules both for PMCA and other proteins.

Published
2024
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3. Similar structures but different mechanisms: Prediction of FABPs-membrane interaction by electrostatic calculation

Author

Fernando, Zamarreño, Fernando E, Herrera, Betina, Córsico, and Marcelo D, Costabel

Subjects
Models, Molecular, Cell Membrane, Lipid Bilayers, Osmolar Concentration, Static Electricity, Phosphatidylserines, Fatty Acid-Binding Proteins, Protein Structure, Tertiary, Rats, Mice, Species Specificity, Phosphatidylcholines, Animals, Humans, Thermodynamics, Cattle, Chickens, Protein Binding
Abstract

The role of fatty acid binding proteins as intracellular fatty acid transporters may require their direct interaction with membranes. In this way different mechanisms have been previously characterized through experimental studies suggesting different models for FABPs-membrane association, although the process in which the molecule adsorbs to the membrane remains to be elucidated. To estimate the importance of the electrostatic energy in the FABP-membrane interaction, we computationally modeled the interaction of different FABPs with both anionic and neutral membranes. Free Electrostatic Energy of Binding (dE), was computed using Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS (Adaptive Poisson Boltzmann Solver). Based on the computational analysis, it is found that recruitment to membranes is facilitated by non-specific electrostatic interactions. Also energetic analysis can quantitatively differentiate among the mechanisms of membrane association proposed and determinate the most energetically favorable configuration for the membrane-associated states of different FABPs. This type of calculations could provide a starting point for further computational or experimental analysis.

Published
2011

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