Neuropilin regulation of angiogenesis, arteriogenesis, and vascular permeability.
Bottom Line: Understanding the mechanisms of NRP1 signaling is, therefore, of profound importance for the design of therapies aiming to control vascular functions.Previous work has shown that vascular NRP1 can variably serve as a receptor for two secreted glycoproteins, the VEGF-A and SEMA3A, but it also has a poorly understood role as an adhesion receptor.Here, we review current knowledge of NRP1 function during blood vessel growth and homeostasis, with special emphasis on the vascular roles of its multiple ligands and signaling partners.
Affiliation: UCL Institute of Ophthalmology, University College London, London, UK.Show MeSH
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Mentions: NRP1 is a single-pass transmembrane glycoprotein of 130 kDa  that was originally discovered in the developing frog nervous system as an axonal adhesion protein  and subsequently in mammals as a receptor for secreted axon guidance cues of the class 3 semaphorin family such as SEMA3A [38,49]. In addition to binding semaphorins, NRP1 also binds VEGF165, an isoform of the vascular endothelial growth factor VEGF-A that arises through alternative splicing [32,75]. These multiple NRP1 interactions are facilitated by a large extracellular domain of 860 amino acids that is organized into five domains, termed a1, a2, b1, b2, and c (Figure1A) [26,71]. Whereas the a and b domains bind ligands, the c domain promotes oligomerization.
Affiliation: UCL Institute of Ophthalmology, University College London, London, UK.