VCAM-1

<h2 id="structure">Structure</h2>
<p>VCAM-1 is a member of the <a href="/facts/Immunoglobulin_superfamily/Wveu4BIL">immunoglobulin superfamily</a>, the superfamily of proteins including <a href="/facts/Antibody/MX8pdTdP">antibodies</a> and <a href="/facts/T_cell_receptor/zDqyWyG4">T-cell receptors</a>. The VCAM-1 gene contains six or seven <a href="/facts/Immunoglobulin/MX8pdTdP">immunoglobulin</a> domains, and is expressed on both large and small <a href="/facts/Blood_vessel/FG3GjPNW">blood vessels</a> only after the <a href="/facts/Endothelial/L4ENFVnw">endothelial</a> cells are stimulated by <a href="/facts/Cytokine/SdWpWABH">cytokines</a>. It is <a href="/facts/Alternative_splicing/nNRwPVNK">alternatively spliced</a> into two known <a href="/facts/RNA/HxPeNfNj">RNA</a> <a href="/facts/Transcription_(genetics)/bDgp9HDN">transcripts</a> that encode different isoforms in humans.<a class="footnote-ref" id="fnref:2" href="#fn:2"><sup>2</sup></a> The gene product is a cell surface <a href="/facts/Sialoglycoprotein/TQgglVkP">sialoglycoprotein</a>, a type I membrane protein that is a member of the <a href="/facts/Immunoglobulin_superfamily/Wveu4BIL">Ig superfamily</a>.
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<h2 id="function">Function</h2>
<p>The VCAM-1 protein mediates the adhesion of <a href="/facts/Lymphocyte/pS2pv2Ma">lymphocytes</a>, <a href="/facts/Monocyte/FW4NNMKM">monocytes</a>, <a href="/facts/Eosinophil/yhIKA8bE">eosinophils</a>, and <a href="/facts/Basophil/FRN1ugHk">basophils</a> to vascular <a href="/facts/Endothelium/L4ENFVnw">endothelium</a>. It also functions in leukocyte-endothelial cell <a href="/facts/Signal_transduction/1bs0Me6w">signal transduction</a>, and it may play a role in the development of <a href="/facts/Atherosclerosis/WIS8QQ6v">atherosclerosis</a> and <a href="/facts/Rheumatoid_arthritis/qFK4Xwv7">rheumatoid arthritis</a>.
</p><p>Upregulation of VCAM-1 in endothelial cells by cytokines occurs as a result of increased <a href="/facts/Gene_transcription/bDgp9HDN">gene transcription</a> (e.g., in response to <a href="/facts/Tumor_necrosis_factor-alpha/7NWNIaCb">tumor necrosis factor-alpha</a> (TNF-α) and <a href="/facts/Interleukin-1/dSToCWMd">interleukin-1</a> (IL-1)) and through stabilization of <a href="/facts/Messenger_RNA/oUL6qxQn">messenger RNA</a> (mRNA) (e.g., <a href="/facts/Interleukin-4/FacDJ3TY">Interleukin-4</a> (IL-4)). The promoter region of the <i>VCAM1</i> gene contains functional tandem <a href="/facts/NF-%25CE%25BAB/qcpt5vuQ">NF-κB</a> (nuclear factor-kappa B) sites. The sustained expression of VCAM-1 lasts over 24 hours.
</p><p>Primarily, the VCAM-1 protein is an endothelial <a href="/facts/Ligand/6etB3qeW">ligand</a> for <a href="/facts/VLA-4/Fv6PRoBB">VLA-4</a> (Very Late Antigen-4 or integrin α4β1) of the β1 subfamily of <a href="/facts/Integrin/DNYUGbBp">integrins</a>. VCAM-1 expression has also been observed in other cell types (e.g., <a href="/facts/Smooth_muscle_cells/mpcpTsHp">smooth muscle cells</a>). It has also been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/Ezrin/AGRXyzLQ">EZR</a><a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> and <a href="/facts/Moesin/dBaWyKMm">Moesin</a>.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a>
</p><p>VCAM-1 is also upregulated if vWF (Von Willebrand Factor) is given in knock-out (KO) ADMATS13 mice but not on mice without KO.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a>
</p><p>CD106 also exists on the surface of some subpopulations of <a href="/facts/Mesenchymal_stem_cell/W0jeK2a3">mesenchymal stem cells</a> (MSC).<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a>
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<h2 id="pharmacology">Pharmacology</h2>
<p>Certain <a href="/facts/Melanoma/qdT7E97Y">melanoma</a> cells can use VCAM-1 to adhere to the endothelium,<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> VCAM-1 may participate in monocyte recruitment to atherosclerotic sites, and it is highly overexpressed in the inflamed brain.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> As a result, VCAM-1 is a potential <a href="/facts/Drug/FFFUI9n4">drug</a> target.
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<h2 id="further-reading">Further reading</h2>

<ul><li>Yonekawa K, Harlan JM (2005). <a href="https://doi.org/10.1189%2Fjlb.0804460">"Targeting leukocyte integrins in human diseases"</a>. <i>J. Leukoc. Biol</i>. 77 (2): 129–40. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1189%2Fjlb.0804460">10.1189/jlb.0804460</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15548573">15548573</a>.</li>
<li>Wu TC (2007). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3179385">"The role of vascular cell adhesion molecule-1 in tumor immune evasion"</a>. <i>Cancer Res</i>. 67 (13): 6003–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1158%2F0008-5472.CAN-07-1543">10.1158/0008-5472.CAN-07-1543</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3179385">3179385</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/17616653">17616653</a>.</li></ul>

<h2 id="external-links">External links</h2>
<ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=VCAM-1">VCAM-1</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li>
<li>Overview of all the structural information available in the <a href="/facts/Protein_Data_Bank/oUhq4ABD">PDB</a> for <a href="/facts/UniProt/lfDDHjAl">UniProt</a>: <i><a href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P19320">P19320</a></i> (Vascular cell adhesion protein 1) at the <a href="/facts/PDBe-KB/p1WX7lPH">PDBe-KB</a>.</li></ul>

<h2 id="references">References</h2>

<ol>
<li id="fn:1"><p>Cybulsky M, Fries JW, Williams AJ, Sultan P, Eddy RL, Byers MG, Shows TB, Gimbrone MA Jr, Collins T (1991). "The human VCAM1 gene is assigned to chromosome 1p31-p32". Cytogenet. Cell Genet. 58 (3–4): 1850–1867. doi:10.1159/000133735. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li>
<li id="fn:2"><p>"Entrez Gene: VCAM1 vascular cell adhesion molecule 1". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7412" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7412</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li>
<li id="fn:3"><p>Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, Furthmayr H, Sanchez-Madrid F (Jun 2002). "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes". J. Cell Biol. 157 (7): 1233–45. doi:10.1083/jcb.200112126. PMC 2173557. PMID 12082081. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173557" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173557</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li>
<li id="fn:4"><p>Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, Furthmayr H, Sanchez-Madrid F (Jun 2002). "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes". J. Cell Biol. 157 (7): 1233–45. doi:10.1083/jcb.200112126. PMC 2173557. PMID 12082081. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173557" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173557</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li>
<li id="fn:5"><p>Le Besnerais M, Favre J, Denis CV, Mulder P, Martinet J, Nicol L, et al. (2016). "Assessment of endothelial damage and cardiac injury in a mouse model mimicking thrombotic thrombocytopenic purpura". J Thromb Haemost. 14 (10): 1917–1930. doi:10.1111/jth.13439. PMID 27501520. <a href="https://doi.org/10.1111%2Fjth.13439" target="_blank">https://doi.org/10.1111%2Fjth.13439</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li>
<li id="fn:6"><p>Yang ZX, Han ZB, Ji YR, Wang YW, Liang L, Chi Y, et al. (2013). "CD106 identifies a subpopulation of mesenchymal stem cells with unique immunomodulatory properties". PLOS One. 8 (3): e59354. Bibcode:2013PLoSO...859354Y. doi:10.1371/journal.pone.0059354. PMC 3595282. PMID 23555021. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3595282" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3595282</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li>
<li id="fn:7"><p>Eibl RH, Benoit M (2004). "Molecular resolution of cell adhesion forces". IEE Proceedings - Nanobiotechnology. 151 (3): 128–32. doi:10.1049/ip-nbt:20040707 (inactive 7 December 2024). PMID 16475855.{{cite journal}}:  CS1 maint: DOI inactive as of December 2024 (link) <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li>
<li id="fn:8"><p>Marcos-Contreras OA (2020). "Selective targeting of nanomedicine to inflamed cerebral vasculature to enhance the blood–brain barrier". Proceedings of the National Academy of Sciences of the United States of America. 117 (7): 3405–3414. doi:10.1073/pnas.1912012117. PMC 7035611. PMID 32005712. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7035611" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7035611</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li>
</ol>

VCAM-1 open-in-new

VCAM-1