Synonyms for neuropilins or Related words with neuropilins

plexin              ephrinb              semaphorins              netrins              netrin              neuropilin              plexins              glypicans              ephrins              fgfrs              ephs              wnts              neuregulins              sfrps              ectodomains              neogenin              betaglycan              syncam              neurofascin              tgfrii              syndecan              frizzleds              pdgfrs              syndecans              semaphorin              rgmb              ephrina              caspr              trks              glypican              heteromerization              nectin              rhamm              ephrin              bmpr              multimerin              ephb              agrin              desmocollins              emilin              synaptotagmins              norrin              attractin              tgfri              tetraspan              cubilin              endodomain              erbbs              taci              trii             



Examples of "neuropilins"
Neuropilins work as co-receptors as they have a very small cytoplasmic domain and thus rely upon other molecules (normally plexins) to transduce their signals across a cell membrane. Neuropilins generally work as dimers and different combinations have different affinities for molecules. For example, NRP-1 homodimers have high affinity for Sema3A, whilst NRP-2 homodimers have high affinity for Sema3F. Another ligand for neuropilins is VEGF, a growth factor involved in the regulation of angiogenesis.
In addition to binding to VEGFRs, VEGF binds to receptor complexes consisting of both neuropilins and VEGFRs. This receptor complex has increased VEGF signalling activity in endothelial cells (blood vessels). Neuropilins (NRP) are pleitrophic receptors and therefore other molecules may interfere with the signalling of the NRP/VEGFR receptor complexes. For example, Class 3 semaphorins compete with VEGF for NRP binding and could therefore regulate VEGF-mediated angiogensis.
In addition to binding to VEGFRs, TACO VEGF binds to receptor complexes consisting of both neuropilins and VEGFRs. This receptor complex has increased VEGF signalling activity in endothelial cells (blood vessels). Neuropilins (NRP) are pleitrophic receptors and therefore other molecules may interfere with the signalling of the NRP/VEGFR receptor complexes. For example, Class 3 semaphorins compete with VEGF for NRP binding and could therefore regulate VEGF-mediated angiogenesis.
Neuropilin-1 is a protein that in humans is encoded by the "NRP1" gene. In humans, the neuropilin 1 gene is located at 10p11.22. This is one of two human neuropilins.
There are two forms of Neuropilins, NRP-1 and NRP-2. They are transmembrane glycoproteins, and predominantly co-receptors for another class of proteins known as semaphorins. Of the semaphorins, NRP-1 and NRP-2 are specifically receptors for class-3 semaphorins, which, among many things, are responsible for axon guidance during the development of the nervous system in vertebrates.
Inside the embryo, the dorsal aorta forms and eventually connect the heart to the capillary plexus of the yolk sac. This forms a closed-loop system of rigid endothelial tubing. It is known that even this early in the process of vasculogenesis, before the onset of blood flow, sections of the tube system may express ephrins or neuropilins, genetic markers of arterial or venous identities, respectively. These identities are still somewhat flexible, but the initial characterization is important to the embryonic remodelling process.
Semaphorins are a class of secreted and membrane proteins that were originally identified as axonal growth cone guidance molecules. They primarily act as short-range inhibitory signals and signal through multimeric receptor complexes. Semaphorins are usually cues to deflect axons from inappropriate regions, especially important in neural system development. The major class of proteins that act as their receptors are called plexins, with neuropilins as their co-receptors in many cases. The main receptors for semaphorins are plexins, which have established roles in regulating Rho-family GTPases. Recent work shows that plexins can also influence R-Ras, which, in turn, can regulate integrins. Such regulation is probably a common feature of semaphorin signalling and contributes substantially to our understanding of semaphorin biology.
Some of the various chemotactic cues that have been explored in the mechanisms of pioneer axons include netrin, ephrin, semaphorin, Slit-Robo, and Notch. Receptors for these molecules have also been studied. Netrins primarily function as attractions of pioneer axons towards the midline. They can act from a distance as much as a few millimeters, as well as act in short range. Netrins can also act as a repellant. Unique among chemoattractants is that the function of netrin has been conserved among a variety of species across 600 million years. Like netrin, ephrin can function as both an attractant and repellant. Ephrins primarily play a role in setting a gradient along the anterior-poster axis for the guidance of developing retinal axons. Semaphorins, which were first identified on specific axons in the grasshopper CNS, function primarily as short-range inhibitory cues that steer pioneer axons away from less ideal regions. Receptor complexes for semaphorins include neuropilins and plexins
In Sema3A signaling cascade, CRMP plays a role as intracellular messenger mediating repulsive signal. Sema3A initiates clustering of the receptor Neuropilin 1 and Plexin A1. While some of the other class of Semaphorins directly bind to Plexin receptors, Sema3A does not bind to Plexin directly. Instead, it interacts with Neuropilins as ligand-binding co-receptor for Plexin and releases Plexin-based signaling. The signal transduction pathway downstream of activated Plexin receptor is mediated by CRMPs. In response to Sema3A signaling cascade, CRMPs which exist as a heterotetramer in the cytosol bind to the cytosolic domain of PlexA and its conformation changes. Further, CRMPs are phosphorylated by Cdk5, GSK3β, and Fes, a tyrosine protein kinase. Especially, phosphorylation of CRMP-1 and CRMP-2 are essential for Sema3A-regulated axonal guidance. In the presence of CRMP-2, the signal can induce alterations of Rac-dependent pathway, which modulates the actin filament assembly in the growth cone. In the absence of Sema3A, the interaction between CRMP tetramer and PlexA is blocked. Phospholipase D2 (PLD-2) which is localized in the growth cone and is involved in actin cytoskeleton rearrangement, can be inhibited by CRMP-2 and its inhibition results in actin depolymerization and possibly affects axonal growth cone collapse. In the presence of CRMP-2, the signal can induce alterations of Rac-dependent pathway, which modulates the actin filament assembly in the growth cone.
Axon branches retract in a distal to proximal manner. The axonal contents that are retracted are thought to be recycled to other parts of the axon. The biological mechanism with which axonal pruning occurs still remains unclear for the mammalian central nervous system. However, pruning has been associated with guidance molecules in mice. Guidance molecules serve to control axon pathfinding through repulsion, and also initiate pruning of exuberant synaptic connections. Semaphorin ligands and the receptors neuropilins and plexins are used to induce retraction of the axons to initiate hippocampo-septal and infrapyramidal bundle (IPB) pruning. Stereotyped pruning of the hippocampal projections have been found to be significantly impaired in mice that have a Plexin-A3 defect. Specifically, axons that are connected to a transient target will retract once the Plexin-A3 receptors are activated by class 3 semaphorin ligands. In IPB, the expression of mRNA for Sema3F is present in the hippocampus prenatally, lost postnatally and returns in the stratum oriens. Coincidentally, onset IPB pruning occurs around the same time. In the case of the hippocampal-septal projections, expression of mRNA for Sema3A was followed by the initiation of pruning after 3 days. This suggests that pruning is triggered once the ligand reaches threshold protein levels within a few days after detectable mRNA expression. Pruning of axons along the visual corticospinal tract (CST) is defective in neuropilin-2 mutants and plexin-A3 and plexin-A4 double mutant mice. Sema3F is also expressed in the dorsal spinal cord during the pruning process. There is no motor CST pruning defect observed in these mutants.