Pulmonary arteries segmentation from CT images using PA-Net with attention module and contour loss.

Background: Pulmonary embolism is a kind of cardiovascular disease that threatens human life and health. Since pulmonary embolism exists in the pulmonary artery, improving the segmentation accuracy of pulmonary artery is the key to the diagnosis of pulmonary embolism. Traditional medical image segmentation methods have limited effectiveness in pulmonary artery segmentation.

The SGK3-triggered ubiquitin-proteasome degradation of podocalyxin (PC) and ezrin in podocytes was associated with the stability of the PC/ezrin complex.

Podocyte damage is commonly accompanied by destabilization of the podocalyxin (PC)/ezrin complex. Serum- and glucocorticoid-inducible kinase 3 (SGK3) plays a role in the maintenance of podocyte function, but the details of this role are poorly understood. Herein we demonstrated that SGK3 and its downstream target protein neural precursor cell expressed developmentally downregulated protein 4 subtype 2 (Nedd4-2) triggered PC and ezrin interaction.

Lack of serum- and glucocorticoid-inducible kinase 3 leads to podocyte dysfunction.

Serum- and glucocorticoid-inducible kinase 3 (SGK3) is a downstream mediator of PI3K, which is essential for maintaining the functional integrity of podocytes. However, little is known about the role of SGK3 in podocyte function. Herein, we demonstrated that SGK3 contributes to the maintenance of podocyte integrity.

Glycogen Synthase Kinase-3 Modulates Hyperosmotic-Induced Urea Transporter A1 Relocation in the Inner Medullary Collecting Duct Cells.

Aim: Glycogen synthase kinase 3 (GSK3) regulates urine concentration by mediating the vasopressin-induced aquaporin 2 expression and water permeability, although it is unknown whether GSK3 also mediates the accumulation of the urea transporter A1 (UT-A1). The aim of this study is to investigate the effect of GSK3 on UT-A1 distribution.

Methods: Mouse inner medullary collecting duct 3 cells were transfected with UT-A1-GFP construct.