Plasmalemma vesicle-associated protein (PLVAP)

Plasmalemma vesicle-associated protein (PLVAP) is a type II integral membrane glycoprotein expressed specifically in endothelial cells, where it forms the stomatal and fenestral diaphragms that are critical for regulating the permeability of blood vessels. Structurally, PLVAP forms disulfide-bonded homodimers and comprises a short intracellular tail, a transmembrane domain, and a long glycosylated extracellular domain with coiled-coil regions. Functionally, PLVAP is essential for endothelial barrier integrity, controlling the selective exchange of solutes and the migration of leukocytes; its upregulation is associated with increased angiogenesis and permeability in a variety of pathological settings including cancer, diabetic retinopathy, traumatic injuries, and renal disease. PLVAP serves as both a therapeutic target—its inhibition reduces pathological vascular leakage and inflammation—and a biomarker for vascular damage and angiogenic activity. Loss-of-function mutations or therapeutic blockade can cause life-threatening vascular leak syndromes, highlighting its crucial physiological role in vascular homeostasis.

Other names

Plasmalemmal vesicle-associated proteinPV-1plasmalemma vesicle-associated protein-1

Blocking or modulating PLVAP can inhibit endothelial permeability and leukocyte transmigration. Inhibition may suppress pathological angiogenesis and inflammatory leukocyte trafficking.