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1 ± 1.3 mm² [P<.001]; -2.1 ± 1.0 mm² [P<.01]; -2.1 ± 1.4 mm² [P=.03], respectively) and in ostial distal MV and ostial SB after Axxess (-2.1 ± 0.8 mm² [P<.001]; -1.6 ± 0.7 mm² [P<.01], respectively), while in proximal Axxess segment, the MLA remained stable (-0.1 ± 0.0; P=.93) and significantly larger than modified-T, mainly due to a smaller neointimal area (1.8 ± 0.7 mm² vs 3.2 ± 0.6 mm²; P<.001). Acute BVS strut discontinuities were observed in 53%, and late intraluminal dismantling was seen in 38% of patients. At 3 years, 1 MACE and no scaffold thromboses were observed.

In this serial imaging bifurcation study, BVS luminal dimensions were significantly smaller at 30 months, with acute strut discontinuities and late Intraluminal dismantling frequently observed.
In this serial imaging bifurcation study, BVS luminal dimensions were significantly smaller at 30 months, with acute strut discontinuities and late Intraluminal dismantling frequently observed.
Pulmonary vein stenosis (PVS) is aggressive, with high morbidity and mortality. Surgical and catheter interventions yield modest success, at best. Refinements in catheter interventions could potentially improve outcomes in this patient population. The goal of this study was to determine the utility of intravascular ultrasound (IVUS) for patients with congenital heart disease and PVS.

Single-center, retrospective review of patients with congenital heart disease and PVS undergoing diagnostic or interventional catheterizations from March 2015 to February 2020. IVUS of the pulmonary veins was performed using an Eagle Eye Platinum IVUS catheter (Volcano Corporation).

Five patients underwent 6 procedures (2 diagnostic, 4 interventional). Median age was 1.5 years (range, 0.7-47.5 years) and weight was 8.8 kg (range, 7.3-61 kg). For the interventional procedures, mean pulmonary vein gradient was 8.7 mm Hg with reduction to 1.1 mm Hg (P<.001). Four patients had congenital PVS and 1 patient was post repair of Scimitar syndrome with an obstructed pulmonary venous baffle. Use of IVUS allowed confirmation of stent expansion and apposition, interval vessel growth after initial stenting, and detection of long-segment hypoplasia, unlikely to respond to intervention. There were no thrombotic complications related to IVUS use.

IVUS of the pulmonary veins is safe and easy to perform, and provides detailed imaging of PVS to help guide therapy. For those requiring intervention, adequate stent apposition to the pulmonary vein walls, as well as limiting vessel overdilation, may minimize future in-stent stenosis and need for reintervention in this challenging disease.
IVUS of the pulmonary veins is safe and easy to perform, and provides detailed imaging of PVS to help guide therapy. For those requiring intervention, adequate stent apposition to the pulmonary vein walls, as well as limiting vessel overdilation, may minimize future in-stent stenosis and need for reintervention in this challenging disease.The complex between lipoprotein lipase (LPL) and its endothelial receptor (GPIHBP1) is responsible for the lipolytic processing of triglyceride-rich lipoproteins (TRLs) along the capillary lumen, a physiologic process that releases lipid nutrients for vital organs such as heart and skeletal muscle. LPL activity is regulated in a tissue-specific manner by endogenous inhibitors (angiopoietin-like [ANGPTL] proteins 3, 4, and 8), but the molecular mechanisms are incompletely understood. ANGPTL4 catalyzes the inactivation of LPL monomers by triggering the irreversible unfolding of LPL's α/β-hydrolase domain. Here, we show that this unfolding is initiated by the binding of ANGPTL4 to sequences near LPL's catalytic site, including β2, β3-α3, and the lid. Using pulse-labeling hydrogen‒deuterium exchange mass spectrometry, we found that ANGPTL4 binding initiates conformational changes that are nucleated on β3-α3 and progress to β5 and β4-α4, ultimately leading to the irreversible unfolding of regions that form LPL's catalytic pocket. LPL unfolding is context dependent and varies with the thermal stability of LPL's α/β-hydrolase domain (T m of 34.8 °C). GPIHBP1 binding dramatically increases LPL stability (T m of 57.6 °C), while ANGPTL4 lowers the onset of LPL unfolding by ∼20 °C, both for LPL and LPL•GPIHBP1 complexes. These observations explain why the binding of GPIHBP1 to LPL retards the kinetics of ANGPTL4-mediated LPL inactivation at 37 °C but does not fully suppress inactivation. The allosteric mechanism by which ANGPTL4 catalyzes the irreversible unfolding and inactivation of LPL is an unprecedented pathway for regulating intravascular lipid metabolism.Genomic imprinting occurs before fertilization, impacts every cell of the developing child, and may be sensitive to environmental perturbations. The noncoding RNA, nc886 (also called VTRNA2-1) is the only known example of the ∼100 human genes imprinted by DNA methylation, that shows polymorphic imprinting in the population. The nc886 gene is part of an ∼1.6-kb differentially methylated region (DMR) that is methylated in the oocyte and silenced on the maternal allele in about 75% of humans worldwide. Here, we show that the presence or absence of imprinting at the nc886 DMR in an individual is consistent across different tissues, confirming that the imprint is established before cellular differentiation and is maintained into adulthood. We investigated the relationships between the frequency of imprinting in newborns and maternal age, alcohol consumption and cigarette smoking before conception in more than 1,100 mother/child pairs from South Africa. Oxaliplatin DNA inhibitor The probability of imprinting in newborns was increased in older mothers and decreased in mothers who drank alcohol before conception. On the other hand, cigarette smoking had no apparent relationship with the frequency of imprinting. These data show an epigenetic change during oocyte maturation which is potentially subject to environmental influence. Much focus has been placed on avoiding alcohol consumption during pregnancy, but our data suggest that drinking before conception may affect the epigenome of the newborn.
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