The established triple co-culture blood-–brain barrier (BBB) model could be used for predicting drugs’ BBB permeability, and co-culture with neurons and astrocytes enhanced brain endothelial cells’ integrity by secreting GDNF, which upregulated claudin-5 and VE-cadherin expression.

Super-resolution imaging uncovers sparse occludin vs. clustered ZO1/claudin-5 architecture, and claudin-5 arrangement compacting during blood-brain-barrier tight-junction (TJ) maturation in which TJs become first restrictive to large and later to small molecules.

Activation of Wnt/β-catenin signaling in endothelial progenitors derived from human pluripotent stem cells partially induces the specialized blood–brain barrier phenotype while the same treatment in matured endothelial cells is less efficacious.

Organ and vessel-type-specific differences in endothelial cell barrier composition and properties uncover the distinct importance of the major tight junction protein Claudin5 in restricting agonist-induced leakage.

Paracellular, trans-tight junction channels, which communicate between two extracellular compartments without crossing the plasma membrane, are a new class of ion channel with unitary behaviors similar to traditional transmembrane channels.

Endothelial tightening by augmenting low level Wnt/β-catenin activity in vessels of the mouse subfornical organ, influences neuronal activation in water-deprived mice, linking endothelial barrier properties to neuro-vascular coupling.

Eprhin B1 in the cardiomyocyte regulates the maturation of the adult surface crest architecture and of the diastolic function during a late postnatal stage in rodents.

Mouse genetic approaches show that multiple Wnt endothelial sources orchestrate the spatiotemporal distribution of hepatocyte functions during liver maturation and respecify metabolic zonation during liver repair.

Mammary progenitors identified by a new marker, ICAM-1, undergo epithelial-mesenchymal transition and luminal-to-basal switch in response to paracrine Met activation.

The DMA-1/LRR-TM cell surface receptor signals through partially redundant pathways to cell-autonomously pattern dendrites, including by directly forming a complex with both the TIAM-1/GEF and ACT-4/Actin.