Publications by authors named "S Sastre"

Human CblC catalyzes the indispensable processing of dietary vitamin B by the removal of its β-axial ligand and an either one- or two-electron reduction of its cobalt center to yield cob(II)alamin and cob(I)alamin, respectively. Human CblC possesses five cysteine residues of an unknown function. We hypothesized that Cys149, conserved in mammals, tunes the CblC reactivity.

View Article and Find Full Text PDF

The oxidation of Met to methionine sulfoxide (MetSO) by oxidants such as hydrogen peroxide, hypochlorite, or peroxynitrite has profound effects on protein function. This modification can be reversed by methionine sulfoxide reductases (msr). In the context of pathogen infection, the reduction of oxidized proteins gains significance due to microbial oxidative damage generated by the immune system.

View Article and Find Full Text PDF

Severe cases of acute respiratory distress syndrome (ARDS) may require prolonged (>28 d) extracorporeal membrane oxygenation (ECMO). In nonresolving disease, recovery is uncertain, and lung transplant may be proposed. This study aims to identify the variables influencing survival and to describe the functional status of these patients at 6 months.

View Article and Find Full Text PDF
Article Synopsis
  • Bacterial toxins, specifically enterotoxigenic toxins like LT, can affect heart function by binding to receptors on heart cells (cardiomyocytes), which may lead to conditions like cardiomyopathy and sudden cardiac death (SIDS).
  • LT disrupts calcium homeostasis in heart cells, impacting their electrical activity and leading to significant alterations in heart performance, such as increased heart rate variability and changes in action potentials.
  • The findings suggest that the B subunit of the LT toxin plays an active role in heart dysfunction and points to a possible link between enterotoxigenic bacteria and instances of sudden cardiac death, emphasizing a need for further understanding of this connection.
View Article and Find Full Text PDF

Inwardly rectifying potassium (Kir) channels play a key role in maintaining the resting membrane potential and supporting potassium homeostasis. There are many variants of Kir channels, which are usually tetramers in which the main subunit has two trans-membrane helices attached to two N- and C-terminal cytoplasmic tails with a pore-forming loop in between that contains the selectivity filter. These channels have domains that are strongly modulated by molecules present in nutrients found in different diets, such as phosphoinositols, polyamines and Mg.

View Article and Find Full Text PDF