High impact information on Plvap

• PV-1 is a novel endothelial protein shown by immunocytochemical tests to be specifically associated with the stomatal diaphragms of caveolae in lung endothelium [1].
• In these cells, PV-1 exhibits only partial perinuclear colocalization with Cav-1 and F-actin [2].
• Endothelial cells transfected with a rat PV-1 construct show a punctate membrane distribution of PV-1, perinuclear accumulation, and an association with the nuclear envelope [2].
• PV1 is an endothelium-specific integral membrane glycoprotein that is associated with both the stomatal diaphragms of caveolae, TECs, and VVOs as well as the diaphragms of endothelial fenestrae [3].
• Our data bring further support to the paradigm by which PV1 dimers would form the fibrils of the diaphragms with a function in the microvascular permeability [3].

Biological context of Plvap

• These findings indicate that the mitogenic effect of PACAP mediated via activation of the GTP-binding protein coupled PACAP/VIP-1 (PV1) receptor is linked to the MAP kinase cascade, increased expression of the proto-oncogenes c-fos and c-jun and activation of the heterodimeric transcription factor AP-1 [4].

Anatomical context of Plvap

• Plasmalemma vesicle protein-1 (PV-1) is a caveolae-associated protein that is enriched in lung endothelial cells [2].
• Developmental regulation of PV-1 in rat lung: association with the nuclear envelope and limited colocalization with Cav-1 [2].

References