Sciatic nerve movement in the deep gluteal space during hip rotations maneuvers

We hypothesize that the sciatic nerve in the subgluteal space has a specific behavior during internal and external coxofemoral rotation and during isometric contraction of the internal and external rotator muscles of the hip. In 58 healthy volunteers, sciatic nerve behavior was studied by ultrasound during passive internal and external hip rotation movements and during isometric contraction of internal and external rotators. Using MATLAB software, changes in nerve curvature at the beginning and end of each exercise were evaluated for longitudinal catches and axial movement for transverse catches. In the long axis, it was observed that during the passive internal rotation and during the isometric contraction of external rotators, the shape of the curve increased significantly while during the passive external rotation and the isometric contraction of the internal rotators the curvature flattened out. During passive movements in internal rotation, on the short axis, the nerve tended to move laterally and forward, while during external rotation the tendency of the nerve was to move toward a medial and backward position. During the isometric exercises, this displacement was less in the passive movements. Passive movements of hip rotation and isometric contraction of the muscles affect the sciatic nerve in the subgluteal space. Retrotrochanteric pain may be related to both the shear effect of the subgluteus muscles and the endoneural and mechanosensitive aggression to which the sciatic nerve is subjected

Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor

The apoptosis-inducing factor (AIF) is a mitochondrial-flavoprotein that, after cell death induction, is distributed to the nucleus to mediate chromatinolysis. In mitochondria, AIF is present in a monomer-dimer equilibrium that after reduction by NADH gets displaced toward the dimer. The crystal structure of the human AIF (hAIF):NAD(H)-bound dimer revealed one FAD and, unexpectedly, two NAD(H) molecules per protomer. A 1:2 hAIF:NAD(H) binding stoichiometry was additionally confirmed in solution by using surface plasmon resonance. The here newly discovered NAD(H)-binding site includes residues mutated in human disorders, and accommodation of the coenzyme in it requires restructuring of a hAIF portion within the 509-560 apoptogenic segment. Disruption of interactions at the dimerization surface by production of the hAIF E413A/R422A/R430A mutant resulted in a nondimerizable variant considerably less efficiently stabilizing charge-transfer complexes upon coenzyme reduction than WT hAIF. These data reveal that the coenzyme-mediated monomer-dimer transition of hAIF modulates the conformation of its C-terminal proapoptotic domain, as well as its mechanism as reductase. These observations suggest that both the mitochondrial and apoptotic functions of hAIF are interconnected and coenzyme controlled: a key information in the understanding of the physiological role of AIF in the cellular life and death cycle. © 2014 American Chemical Society.Peer Reviewe