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Neuropilin 1
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<h2 id="function">Function</h2> <p>NRP1 is a membrane-bound <a href="/facts/Coreceptor/eJsUxd3F">coreceptor</a> to a <a href="/facts/Tyrosine_kinase_receptor/1oNWIdV8">tyrosine kinase receptor</a> for both <a href="/facts/Vascular_endothelial_growth_factor/kNDc0Xj0">vascular endothelial growth factor</a> (for example, <a href="/facts/VEGFA/Qpe3aBdD">VEGFA</a>) and <a href="/facts/Semaphorin/327okAXu">semaphorin</a> (for example, <a href="/facts/SEMA3A/qKnGD9uh">SEMA3A</a>) family members. NRP1 plays versatile roles in <a href="/facts/Angiogenesis/h0HF9IUd">angiogenesis</a>, <a href="/facts/Axon_guidance/c33o0dQx">axon guidance</a>, cell survival, <a href="/facts/Cell_migration/5ySAMquQ">migration</a>, and invasion.[supplied by OMIM]<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>Neuropilin 1 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/Vascular_endothelial_growth_factor_A/Qpe3aBdD">Vascular endothelial growth factor A</a>.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a><a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p> <h2 id="role-in-covid-19">Role in COVID-19</h2> <p>Research has shown that neuropilin 1 facilitates entry of <a href="/facts/Severe_acute_respiratory_syndrome_coronavirus_2/DxF8rDc1">SARS-CoV-2</a> into cells, making it a possible target for future antiviral drugs.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p> <h2 id="implication-in-cancer">Implication in cancer</h2> <p>Neuropilin 1 has been implicated in the <a href="/facts/Angiogenesis/h0HF9IUd">vascularization</a> 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 <a href="/facts/Metastasis/4dadbm6z">metastasis</a>.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a><a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a><a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> </p><p>In <a href="/facts/Prostate_cancer/Mx7XuDhm">prostate cancer</a> NRP1 has been demonstrated to be an <a href="/facts/Androgen/Rxey0HxX">androgen</a>-suppressed gene, upregulated during the adaptive response of prostate tumors to androgen-targeted therapies and a prognostic biomarker of clinical metastasis and lethal PCa.<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> In vitro and in vivo mouse studies have shown membrane bound NRP1 to be proangiogenic and that NRP1 promotes the vascularization of prostate tumors.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> </p><p>Elevated NRP1 expression is also correlated with the invasiveness of <a href="/facts/Non-small_cell_lung_cancer/9T47knRp">non-small cell lung cancer</a> both in vitro and in vivo.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> </p> <h3>Target for cancer therapies</h3> <p>As a <a href="/facts/Co-receptor/eJsUxd3F">co-receptor</a> for <a href="/facts/Vascular_endothelial_growth_factor/kNDc0Xj0">VEGF</a>, NRP1 is a potential target for cancer therapies. A synthetic peptide, EG3287, was generated in 2005 and has been shown to block NRP1 activity.<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> EG3287 has been shown to induce <a href="/facts/Apoptosis/8dVzSm4y">apoptosis</a> in tumor cells with elevated NRP1 expression.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> A patent for EG3287 was filed in 2002 and approved in 2003.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> As of 2015 there were no clinical trials ongoing or completed for EG3287 as a human cancer therapy. </p><p>Soluble NRP1 has the opposite effect of membrane bound NRP1 and has anti-VEGF activity. In vivo mouse studies have shown that injections of sNRP-1 inhibits progression of <a href="/facts/Acute_myeloid_leukemia/jvbXzg3J">acute myeloid leukemia</a> in mice.<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>Zachary I, Gliki G (February 2001). <a href="https://doi.org/10.1016%2FS0008-6363%2800%2900268-6">"Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family"</a>. <i>Cardiovascular Research</i>. 49 (3): 568–581. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0008-6363%2800%2900268-6">10.1016/S0008-6363(00)00268-6</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11166270">11166270</a>.</li> <li>He Z, Tessier-Lavigne M (August 1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980534-6">"Neuropilin is a receptor for the axonal chemorepellent Semaphorin III"</a>. <i>Cell</i>. 90 (4): 739–751. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980534-6">10.1016/S0092-8674(00)80534-6</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9288753">9288753</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:9720408">9720408</a>.</li> <li>Giger RJ, Urquhart ER, Gillespie SK, Levengood DV, Ginty DD, Kolodkin AL (November 1998). <a href="https://doi.org/10.1016%2FS0896-6273%2800%2980625-X">"Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity"</a>. <i>Neuron</i>. 21 (5): 1079–1092. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0896-6273%2800%2980625-X">10.1016/S0896-6273(00)80625-X</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9856463">9856463</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:18445456">18445456</a>.</li> <li>Chen H, He Z, Bagri A, Tessier-Lavigne M (December 1998). <a href="https://doi.org/10.1016%2FS0896-6273%2800%2980648-0">"Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins"</a>. <i>Neuron</i>. 21 (6): 1283–1290. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0896-6273%2800%2980648-0">10.1016/S0896-6273(00)80648-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9883722">9883722</a>.</li> <li>Takahashi T, Nakamura F, Jin Z, Kalb RG, Strittmatter SM (October 1998). "Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors". <i>Nature Neuroscience</i>. 1 (6): 487–493. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F2203">10.1038/2203</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10196546">10196546</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:38320889">38320889</a>.</li> <li>Rossignol M, Beggs AH, Pierce EA, Klagsbrun M (May 1999). "Human neuropilin-1 and neuropilin-2 map to 10p12 and 2q34, respectively". <i>Genomics</i>. 57 (3): 459–460. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fgeno.1999.5790">10.1006/geno.1999.5790</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10329017">10329017</a>.</li> <li>Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, et al. (July 1999). <a href="https://doi.org/10.1074%2Fjbc.274.30.21217">"Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1"</a>. <i>The Journal of Biological Chemistry</i>. 274 (30): 21217–21222. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.274.30.21217">10.1074/jbc.274.30.21217</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10409677">10409677</a>.</li> <li>Cai H, Reed RR (August 1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6782790">"Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1"</a>. <i>The Journal of Neuroscience</i>. 19 (15): 6519–6527. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1523%2FJNEUROSCI.19-15-06519.1999">10.1523/JNEUROSCI.19-15-06519.1999</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6782790">6782790</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10414980">10414980</a>.</li> <li>Takahashi T, Fournier A, Nakamura F, Wang LH, Murakami Y, Kalb RG, et al. (October 1999). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980062-8">"Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors"</a>. <i>Cell</i>. 99 (1): 59–69. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980062-8">10.1016/S0092-8674(00)80062-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10520994">10520994</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:18167425">18167425</a>.</li> <li>Tamagnone L, Artigiani S, Chen H, He Z, Ming GI, Song H, et al. (October 1999). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980063-X">"Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates"</a>. <i>Cell</i>. 99 (1): 71–80. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980063-X">10.1016/S0092-8674(00)80063-X</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10520995">10520995</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:17386412">17386412</a>.</li> <li>Gagnon ML, Bielenberg DR, Gechtman Z, Miao HQ, Takashima S, Soker S, et al. (March 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC15970">"Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 97 (6): 2573–2578. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2000PNAS...97.2573G">2000PNAS...97.2573G</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.040337597">10.1073/pnas.040337597</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC15970">15970</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10688880">10688880</a>.</li> <li>Gluzman-Poltorak Z, Cohen T, Herzog Y, Neufeld G (June 2000). <a href="https://doi.org/10.1074%2Fjbc.M909259199">"Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected]"</a>. <i>The Journal of Biological Chemistry</i>. 275 (24): 18040–18045. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M909259199">10.1074/jbc.M909259199</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10748121">10748121</a>.</li> <li>Fuh G, Garcia KC, de Vos AM (September 2000). <a href="https://doi.org/10.1074%2Fjbc.M003955200">"The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1"</a>. <i>The Journal of Biological Chemistry</i>. 275 (35): 26690–26695. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M003955200">10.1074/jbc.M003955200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10842181">10842181</a>.</li> <li>Rossignol M, Gagnon ML, Klagsbrun M (December 2000). "Genomic organization of human neuropilin-1 and neuropilin-2 genes: identification and distribution of splice variants and soluble isoforms". <i>Genomics</i>. 70 (2): 211–222. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fgeno.2000.6381">10.1006/geno.2000.6381</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11112349">11112349</a>.</li> <li>Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (September 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1083732">"Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing"</a>. <i>EMBO Reports</i>. 1 (3): 287–292. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fembo-reports%2Fkvd058">10.1093/embo-reports/kvd058</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1083732">1083732</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11256614">11256614</a>.</li> <li>Whitaker GB, Limberg BJ, Rosenbaum JS (July 2001). <a href="https://doi.org/10.1074%2Fjbc.M102315200">"Vascular endothelial growth factor receptor-2 and neuropilin-1 form a receptor complex that is responsible for the differential signaling potency of VEGF(165) and VEGF(121)"</a>. <i>The Journal of Biological Chemistry</i>. 276 (27): 25520–25531. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M102315200">10.1074/jbc.M102315200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11333271">11333271</a>.</li> <li>Walter JW, North PE, Waner M, Mizeracki A, Blei F, Walker JW, et al. (March 2002). "Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma". <i>Genes, Chromosomes & Cancer</i>. 33 (3): 295–303. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fgcc.10028">10.1002/gcc.10028</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11807987">11807987</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:33428561">33428561</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M (March 1998). "Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor". Cell. 92 (6): 735–745. doi:10.1016/S0092-8674(00)81402-6. PMID 9529250. S2CID 547080. <a href="https://doi.org/10.1016%2FS0092-8674%2800%2981402-6" target="_blank">https://doi.org/10.1016%2FS0092-8674%2800%2981402-6</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Chen H, Chédotal A, He Z, Goodman CS, Tessier-Lavigne M (September 1997). "Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III". Neuron. 19 (3): 547–559. doi:10.1016/S0896-6273(00)80371-2. PMID 9331348. S2CID 17985062. <a href="https://doi.org/10.1016%2FS0896-6273%2800%2980371-2" target="_blank">https://doi.org/10.1016%2FS0896-6273%2800%2980371-2</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: NRP1 neuropilin 1". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>"Entrez Gene: NRP1 neuropilin 1". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8829</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M (March 1998). "Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor". Cell. 92 (6): 735–745. doi:10.1016/S0092-8674(00)81402-6. PMID 9529250. S2CID 547080. <a href="https://doi.org/10.1016%2FS0092-8674%2800%2981402-6" target="_blank">https://doi.org/10.1016%2FS0092-8674%2800%2981402-6</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Mamluk R, Gechtman Z, Kutcher ME, Gasiunas N, Gallagher J, Klagsbrun M (July 2002). "Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain". The Journal of Biological Chemistry. 277 (27): 24818–24825. doi:10.1074/jbc.M200730200. PMID 11986311. <a href="https://doi.org/10.1074%2Fjbc.M200730200" target="_blank">https://doi.org/10.1074%2Fjbc.M200730200</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Cantuti-Castelvetri L, Ojha R, Pedro LD, Djannatian M, Franz J, Kuivanen S, et al. (November 2020). "Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity". Science. 370 (6518): 856–860. Bibcode:2020Sci...370..856C. doi:10.1126/science.abd2985. PMC 7857391. PMID 33082293. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7857391" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7857391</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>"Neuropilin-1 drives SARS-CoV-2 infectivity, finds breakthrough study". MedicalXpress. <a href="https://medicalxpress.com/news/2020-10-neuropilin-sars-cov-infectivity-breakthrough.html" target="_blank">https://medicalxpress.com/news/2020-10-neuropilin-sars-cov-infectivity-breakthrough.html</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Tse BW, Volpert M, Ratther E, Stylianou N, Nouri M, McGowan K, et al. (June 2017). "Neuropilin-1 is upregulated in the adaptive response of prostate tumors to androgen-targeted therapies and is prognostic of metastatic progression and patient mortality". Oncogene. 36 (24): 3417–3427. doi:10.1038/onc.2016.482. PMC 5485179. PMID 28092670. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485179" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485179</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Fakhari M, Pullirsch D, Abraham D, Paya K, Hofbauer R, Holzfeind P, et al. (January 2002). 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