Current trends in image-guided chest interventions.

Interventional radiology (IR) is a rapidly expanding medical subspecialty and refers to a range of image-guided procedural techniques. The image guidance allows real-time visualization and precision placement of a needle, catheter, wire and device to deep body structures through small incisions. Advantages include reduced risks, faster recovery and shorter hospital stays, lower costs and less patient discomfort. The range of chest interventional procedures keeps on expanding due to improved imaging facilities, better percutaneous assess devices and advancing ablation and embolization techniques. These advances permit procedures to be undertaken safely, simultaneously and effectively, hence escalating the role of IR in the treatment of chest disorders. This review article aims to cover the latest developments in some image-guided techniques of the chest, including thermal ablation therapy of lung malignancy, targeted therapy of pulmonary embolism, angioplasty and stenting of mediastinal venous/superior vena cava occlusion, pulmonary arteriovenous malformation treatment and bronchial artery embolization for haemoptysis.

PB1 and UBA domains of p62 are essential for aggresome-like induced structure formation.

ALIS are large, transient, cytosolic aggregates that serve as storage compartments for ubiquitin-tagged defective ribosomal products. We determined the importance of the protein p62 in the formation of ALIS and demonstrated that two domains of p62-PB1 and UBA-are essential for ALIS assembly. Those two major binding domains of p62, also known as sequestosome 1, were shown to play a critical role in the formation of autophagosomes or cytoplasmic aggregates. Specifically, the PB1 domain is essential for self-oligomerization, and the UBA domain allows p62 to bind to polyubiquitin chains or ubiquitinated proteins. After stimulation of RAW 264.7 macrophages with lipopolysaccharide, we observed a significant decrease in the number of cells with ALIS. Importantly, cells overexpressing either a PB1 mutant or UBA-deleted p62 construct also exhibited a substantially diminished number of cells containing ALIS. Since both p62 and ubiquitin are found in ALIS, we evaluated the dynamics of YFP-tagged p62 in ALIS. In contrast to the findings of a previous study that evaluated GFP-tagged ubiquitin motility in ALIS, we determined that YFP-tagged p62 has very limited mobility. Lastly, we determined that GST-tagged full-length p62 binds to Lys-63-linked polyubiquitin chains but not to Lys-48-linked chains. Overall, our findings provide insight on the essential role that p62, particularly its PB1 and UBA domains, has in the formation of ALIS.