Synonyms for neuropilin or Related words with neuropilin

plexin              ephrin              glypican              neuropilins              netrin              nectin              syndecan              sortilin              tgfrii              rhamm              alcam              angiopoietin              semaphorin              endosialin              cubilin              neogenin              frzb              upar              galectin              fzd              pleiotrophin              sorla              epha              ephb              nucleostemin              claudin              caveolin              norrin              ceacam              endoglin              neurofascin              ptprk              osmr              fshr              bmpr              mcam              tgfbrii              taci              cntfr              ngr              hhip              trii              pdgfd              epor              betaglycan              prominin              neurotactin              cripto              pdgfralpha              icoslg             



Examples of "neuropilin"
Neuropilin-1 is a therapeutic target protein in the treatment for leukemia and lymphoma, since It has been shown that there is increased expression in neuropilin-1 in leukemia and lymphoma cell lines. Also, antagonism of neuropilin-1 has been found to inhibit tumour cell migration and adhesion.
Neuropilin is a protein receptor active in neurons.
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.
Neuropilin 2 (NRP2) is a protein that in humans is encoded by the "NRP2" gene.
Neuropilin 1 has been shown to interact with Vascular endothelial growth factor A.
Vesencumab is an immunomodulator designed for the treatment of solid malignancies. It binds to neuropilin 1.
Neuropilin (NRP) and tolloid (TLL)-like 1 is a protein that in humans is encoded by the NETO1 gene.
Fms-like tyrosine kinase-1 (flt-1) was shown to be a VEGF receptor by Ferrara "et al." in 1992. The kinase insert domain receptor (KDR) was shown to be a VEGF receptor by Terman "et al." in 1992 as well. In 1998, neuropilin 1 and neuropilin 2 were shown to act as VEGF receptors.
Glycyl-tRNA synthetase has been shown to interact with EEF1D. Mutant forms of the protein associated with peripheral nerve disease have been shown to aberrantly bind to the transmembrane receptor protein neuropilin 1.
The structure of B1 domain (coagulation factor 5/8 type) of neuropilin-1 was determined through X-Ray Diffraction with a resolution of 2.90 Å. The secondary structure of this domain is 5% alpha helical and 46% beta sheet.
Plexin A4 binds to neuropilin 1 (Nrp1) and neuropilin 2 (Nrp2) and transduces signals from Sema3A, Sema6A, and Sema6B. These Nrp-plexin and semaphorin complexes initiate cascades that regulate diverse processes such as axon pruning and repulsion, dendritic attraction and branching, regulation of cell migration, vascular remodeling, and growth cone collapse. Both upregulation and downregulation of Plexin A4 has been observed following neural injury suggesting a dynamic role for Sema3A and Plexin A4 in neural maintenance and regeneration. Additionally, Sema3A and therefore its receptor, Plexin A4, have been implicated as possible components of fast-fatigable muscle fiber denervation in ALS.
Neurovascular development is the parallel emergence and patterning of the nervous system and the vascular system during embryogenesis and early life. Neurovascular congruency appears to be determined by shared molecular patterning mechanism involving axon guidance that involves axonal guidance molecules such as sema3A (semaphorin 3A) and (neuropilin).
Neuropilin 1 has been implicated in the vascularization and progression of cancers. NRP1 expression has been shown to be elevated in a number of human patient tumor samples, including brain, prostate, breast, colon, and lung cancers and NRP1 levels are positively correlated with metastasis.
A plexin is a protein which acts as a receptor for semaphorin. Plexin acts as a signal transduction molecule in the neuropilin-plexin receptor complex. Plexins also act as transduction factors for ITAM-DAP12-RANKL signalling pathway involved in osteoclastic differentiation.
Class 3 Semaphorins (SEMA3s) regulate angiogenesis by modulating endothelial cell adhesion, migration, proliferation, survival and the recruitment of pericytes. Furthermore, semaphorins can interfere with VEGF-mediated angiogenesis since both SEMA3s and VEGF-A compete for Neuropilin receptor binding at endothelial cells. The relative expression levels of SEMA3s and VEGF-A may therefore be important for angiogenesis.
This guidance cue for axons of neurons are signaled through receptor complexes containing Neuropilin-1 (NRP1) and a co-receptor. One of the first identified intracellular messenger required for the growth cone-collapse induced by Sema3A is the CRMP protein called CRMP2.
This gene encodes a member of the plexin-A family of semaphorin co-receptors. Semaphorins are a large family of secreted or membrane-bound proteins that mediate repulsive effects on axon pathfinding during nervous system development. A subset of semaphorins are recognized by plexin-A/neuropilin transmembrane receptor complexes, triggering a cellular signal transduction cascade that leads to axon repulsion. This plexin-A family member is thought to transduce signals from semaphorin-3A and -3C.
Angiogenesis is important in embryonic development but it is also a fundamental process of tumor growth. Deletion of the gene in Caecam1-/- mice results in a reduction of the abnormal vascularization seen in cancer and lowered nitric oxide production, suggesting a therapeutic possibility through targeting of this gene. The neuropilin co-receptor family mediates binding of VEGF in conjunction with the VEGFR1/VEGFR2 and Plexin signaling receptors, and therefore also plays a role in tumor vascular development.
The classification of angioblasts into arterial- or venous-identified cells is essential to form the proper branching morphology. Arterial segments of the early vasculature express ephrinB2 and DLL4 whereas venous segments express neuropilin-2 and EPHB4; this is believed to assist in guidance of flow from arterial-venous sections of the loop. However, mechanical cues provided by the heart’s first contractions are still necessary for complete remodelling.
During embryonic neurodevelopment, synapse elimination and axonal pruning are critical to ensure normal functioning of the central and peripheral nervous system. Studies have suggested that Sema3A/Neuropilin 2 (Npn2) interactions mediate synapse elimination and axonal pruning, as demonstrated by Sema3A/Npn2 loss-of-function studies in mice. The attractive cues mediated by Semaphorins are not well understood at the moment; however, protein kinase focal adhesion kinase (FAK) and MAP Kinase (MAPK) have been implicated in mediating downstream attractive signaling upon Semaphorin receptor stimulation.