Calibration of the mechanical boundary conditions for a patient-specific thoracic aorta model including the heart motion effect

Objective: we propose a procedure for calibrating 4 parameters governing the mechanical boundary conditions (BCs) of a thoracic aorta (TA) model derived from one patient with ascending aortic aneurysm. The BCs reproduce the visco-elastic structural support provided by the soft tissue and the spine and allow for the inclusion of the heart motion effect. Methods: we first segment the TA from magnetic resonance imaging (MRI) angiography and derive the heart motion by tracking the aortic annulus from cine-MRI. A rigid-wall fluid-dynamic simulation is performed to derive the time-varying wall pressure field. We build the finite element model considering patient-specific material properties and imposing the derived pressure field and the motion at the annulus boundary. The calibration, which involves the zero-pressure state computation, is based on purely structural simulations. After obtaining the vessel boundaries from the cine-MRI sequences, an iterative procedure is performed to minimize the distance between them and the corresponding boundaries derived from the deformed structural model. A strongly-coupled fluid-structure interaction (FSI) analysis is finally performed with the tuned parameters and compared to the purely structural simulation. Results and conclusion: the calibration with structural simulations allows to reduce maximum and mean distances between image-derived and simulation-derived boundaries from 8.64 mm to 6.37 mm and from 2.24 mm to 1.83 mm, respectively. The maximum root mean square error between the deformed structural and FSI surface meshes is 0.19 mm. This procedure may prove crucial for increasing the model fidelity in replicating the real aortic root kinematics

Evaluation of structural change and local strain distribution in polymers comparatively imaged by FFSA and OCT techniques

Mechanical material testing combined with optical coherence tomography (OCT) allows for the first time the immediate detection of inner structural changes along with a qualitative observation of the local strain distribution in surface near bulk regions of semitransparent and translucent specimens. In addition to a 3D full field strain analysis (FFSA) system based on digital image correlation (DIC), a customized spectral domain OCT system operating at 1550 nm was applied for investigation. Exemplified by tensile testing of elastomer particle filled polypropylene specimens, local dissimilarity evaluation of the OCT images was performed. The results show the high potential of OCT to provide complementary information to DIC-based FFSA, like to identify processes influencing the remaining life of advanced commodity plastics such as the start and progress of yielding, identification of the yielding point, localization of the necking front and the development of small scale voids as in the case of matrix crazing

Prognostic interest of energy loss index in patients with low gradient severe aortic stenosis and preserved ejection fraction

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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsible for HSP expression, is one of the targets of HSP27. In stressed cells, HSP27 enters the nucleus and, in the form of large oligomers, binds to HSF1 and induces its modification by SUMO-2/3 on lysine 298. HSP27-induced HSF1 modification by SUMO-2/3 takes place downstream of the transcription factor phosphorylation on S303 and S307 and does not affect its DNA-binding ability. In contrast, this modification blocks HSF1 transactivation capacity. These data show that HSP27 exerts a feedback inhibition of HSF1 transactivation and enlighten the strictly regulated interplay between HSPs and HSF1. As we also show that HSP27 binds to the SUMO-E2-conjugating enzyme, Ubc9, our study raises the possibility that HSP27 may act as a SUMO-E3 ligase specific for SUMO-2/3