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<title>Cell adhesion molecule</title>

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<span id="openzim-page-title" class="mw-page-title-main"><span class="mw-page-title-main">Cell adhesion molecule</span></span>

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</style><div role="note" class="hatnote navigation-not-searchable">This article is about cell adhesion molecules. For the role of CAMs in the formation and stabilization of neural synapses, see <a href="Synaptic_stabilization" title="Synaptic stabilization">Synaptic stabilization</a>.</div>

<p><b>Cell adhesion molecules</b> (<b>CAMs</b>) are a subset of cell surface proteins<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> that are involved in the <a href="Molecular_binding" title="Molecular binding">binding</a> of cells with other cells or with the <a href="Extracellular_matrix" title="Extracellular matrix">extracellular matrix</a> (ECM), in a process called <a href="Cell_adhesion" title="Cell adhesion">cell adhesion</a>.<sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> In essence, CAMs help cells stick to each other and to their surroundings. CAMs are crucial components in maintaining tissue structure and function. In fully developed animals, these molecules play an integral role in generating force and movement and consequently ensuring that organs are able to execute their functions normally.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> In addition to serving as "molecular glue", CAMs play important roles in the cellular mechanisms of growth, contact inhibition, and apoptosis. Aberrant expression of CAMs may result in a wide range of pathologies, ranging from frostbite to cancer.<sup id="cite_ref-pmid8199653_4-0" class="reference"><a href="#cite_note-pmid8199653-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>

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<div class="mw-heading mw-heading2"><h2 id="Structure">Structure</h2></div>

<p>CAMs are typically single-pass <a href="Transmembrane_receptor" class="mw-redirect" title="Transmembrane receptor">transmembrane receptors</a> <sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> and are composed of three conserved domains: an intracellular domain that interacts with the <a href="Cytoskeleton" title="Cytoskeleton">cytoskeleton</a>, a transmembrane domain, and an extracellular domain. CAMs can interact in two different ways:<sup id="cite_ref-pmid9242926_6-0" class="reference"><a href="#cite_note-pmid9242926-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> <b>homophilic</b> binding to the same type of CAM on another cell, and <b>heterophilic</b> binding to a different type of CAM.

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<div class="mw-heading mw-heading2"><h2 id="Families_of_CAMs">Families of CAMs</h2></div>

<p>There are four major superfamilies or groups of CAMs: the <a href="Immunoglobulin" class="mw-redirect" title="Immunoglobulin">immunoglobulin</a> super family of cell adhesion molecules (<a href="IgCAM" class="mw-redirect" title="IgCAM">IgCAMs</a>), <a href="Cadherin" title="Cadherin">Cadherins</a>, <a href="Integrin" title="Integrin">Integrins</a>, and the Superfamily of <a href="Pattern_recognition_receptor#C-type_lectin_receptors_(CLR)" title="Pattern recognition receptor">C-type of lectin-like domains proteins</a> (<b>CTLDs</b>). <a href="Proteoglycans" class="mw-redirect" title="Proteoglycans">Proteoglycans</a> are also considered to be a class of CAMs.

</p><p>One classification system involves the distinction between calcium-independent CAMs and calcium-dependent CAMs.<sup id="cite_ref-pmid6165990_7-0" class="reference"><a href="#cite_note-pmid6165990-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> The Ig-superfamily CAMs do not depend on Ca<sup>2+</sup> while integrins, cadherins and selectins depend on Ca<sup>2+</sup>. In addition, integrins participate in cell–matrix interactions, while other CAM families participate in cell–cell interactions.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup>

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<div class="mw-heading mw-heading3"><h3 id="Calcium-independent">Calcium-independent</h3></div>

<div role="note" class="hatnote navigation-not-searchable">Main article: <a href="IgSF_CAM" title="IgSF CAM">IgSF CAM</a></div>

<p><a href="Immunoglobulin_superfamily" title="Immunoglobulin superfamily">Immunoglobulin superfamily</a> CAMs (IgSF CAMs) is regarded as the most diverse superfamily of CAMs. This family is characterized by their extracellular domains containing Ig-like domains. The Ig domains are then followed by <a href="Fibronectin_type_III_domain" title="Fibronectin type III domain">Fibronectin type III domain</a> repeats and IgSFs are anchored to the membrane by a GPI moiety. This family is involved in both homophilic or heterophilic binding and has the ability to bind integrins or different IgSF CAMs.

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<div class="mw-heading mw-heading3"><h3 id="Calcium-dependent">Calcium-dependent</h3></div>

<div class="mw-heading mw-heading4"><h4 id="Integrins">Integrins</h4></div>

<div role="note" class="hatnote navigation-not-searchable">Main article: <a href="Integrin" title="Integrin">Integrin</a></div>

<p><a href="Integrin" title="Integrin">Integrins</a>, one of the major classes of receptors within the ECM,<sup id="cite_ref-Brown1995_9-0" class="reference"><a href="#cite_note-Brown1995-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> mediate cell–ECM interactions with <a href="Collagen" title="Collagen">collagen</a>, <a href="Fibrinogen" title="Fibrinogen">fibrinogen</a>, <a href="Fibronectin" title="Fibronectin">fibronectin</a>, and <a href="Vitronectin" title="Vitronectin">vitronectin</a>.<sup id="cite_ref-Humphries2006_10-0" class="reference"><a href="#cite_note-Humphries2006-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> Integrins provide essential links between the <a href="Extracellular_environment" class="mw-redirect" title="Extracellular environment">extracellular environment</a> and the intracellular signalling pathways, which can play roles in cell behaviours such as <a href="Apoptosis" title="Apoptosis">apoptosis</a>, <a href="Cellular_differentiation" title="Cellular differentiation">differentiation</a>, <a href="Cell_fate_determination" title="Cell fate determination">survival</a>, and <a href="Transcription_(genetics)" class="mw-redirect" title="Transcription (genetics)">transcription</a>.<sup id="cite_ref-Schnapp2006_11-0" class="reference"><a href="#cite_note-Schnapp2006-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup>

</p><p>Integrins are <a href="Heterodimer" class="mw-redirect" title="Heterodimer">heterodimeric</a>, as they consist of an alpha and beta subunit.<sup id="cite_ref-Garcia2005_12-0" class="reference"><a href="#cite_note-Garcia2005-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> There are currently 18 alpha subunits and 8 beta subunits, which combine to make up 24 different integrin combinations.<sup id="cite_ref-Humphries2006_10-1" class="reference"><a href="#cite_note-Humphries2006-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> Within each of the alpha and beta subunits there is a large extracellular domain, a transmembrane domain and a short cytoplasmic domain.<sup id="cite_ref-Vinater1994_13-0" class="reference"><a href="#cite_note-Vinater1994-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> The extracellular domain is where the <a href="Ligand" title="Ligand">ligand</a> binds through the use of divalent <a href="Cation" class="mw-redirect" title="Cation">cations</a>. The integrins contain multiple divalent cation binding sites in the extracellular domain <sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup>). The integrin cation binding sites can be occupied by Ca2+ or by Mn2+ ions. Cations are necessary but not sufficient for integrins to convert from the inactive bent conformation into the active extended conformation. Both the presence of cations bound to the multiple cation binding sites is required, along with the direct physical association with ECM ligands for integrins to attain the extended structure and concomitant activation.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> Thus, rise in extracellular Ca2+ ions may serve to prime the integrin heterodimer. The release of intracellular Ca2+ have been shown to be important for integrin inside-out activation.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> However, extracellular Ca2+ binding may exert different effects depending on the type of integrin and the cation concentration.<sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup>

Integrins regulate their activity within the body by changing conformation. Most exist at rest in a low <a href="Dissociation_constant#Protein-ligand_binding" title="Dissociation constant">affinity</a> state, which can be altered to high affinity through an external agonist which causes a conformational change within the integrin, increasing their affinity.<sup id="cite_ref-Schnapp2006_11-1" class="reference"><a href="#cite_note-Schnapp2006-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup>

</p><p>An example of this is the aggregation of <a href="Platelets" class="mw-redirect" title="Platelets">platelets</a>;<sup id="cite_ref-Schnapp2006_11-2" class="reference"><a href="#cite_note-Schnapp2006-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Agonists such as <a href="Thrombin" title="Thrombin">thrombin</a> or <a href="Collagen" title="Collagen">collagen</a> trigger the integrin into its high affinity state, which causes increased <a href="Fibrinogen" title="Fibrinogen">fibrinogen</a> binding, causing platelet aggregation.

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<div class="mw-heading mw-heading4"><h4 id="Cadherins">Cadherins</h4></div>

<div role="note" class="hatnote navigation-not-searchable">Main article: <a href="Cadherin" title="Cadherin">Cadherin</a></div>

<p>The <b><a href="Cadherin" title="Cadherin">cadherins</a></b> are homophilic <span class="chemf nowrap"><a href="Calcium_in_biology" title="Calcium in biology">Ca<span class="nowrap"><span style="display:inline-block;margin-bottom:-0.3em;vertical-align:0.8em;line-height:1em;font-size:80%;text-align:left"><sup style="font-size:inherit;line-height:inherit;vertical-align:baseline">2+</sup><br><sub style="font-size:inherit;line-height:inherit;vertical-align:baseline"></sub></span></span></a></span>-dependent <a href="Glycoproteins" class="mw-redirect" title="Glycoproteins">glycoproteins</a>.<sup id="cite_ref-Buxton1992_18-0" class="reference"><a href="#cite_note-Buxton1992-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> The classic cadherins (<a href="CDH1_(gene)" class="mw-redirect" title="CDH1 (gene)">E-</a>, <a href="CDH2" class="mw-redirect" title="CDH2">N-</a> and <a href="CDH3_(gene)" title="CDH3 (gene)">P-</a>) are concentrated at the <a href="Adherens_junction" title="Adherens junction">intermediate cell junctions</a>, which link to the <a href="Actin" title="Actin">actin</a> filament network through specific linking proteins called <a href="Catenin" title="Catenin">catenins</a>.<sup id="cite_ref-Buxton1992_18-1" class="reference"><a href="#cite_note-Buxton1992-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup>

</p><p>Cadherins are notable in embryonic development. For example, cadherins are crucial in <a href="Gastrulation" title="Gastrulation">gastrulation</a> for the formation of the <a href="Mesoderm" title="Mesoderm">mesoderm</a>, <a href="Endoderm" title="Endoderm">endoderm</a>, and <a href="Ectoderm" title="Ectoderm">ectoderm</a>. Cadherins also contribute significantly to the development of the nervous system. The distinct temporal and spatial localization of cadherins implicates these molecules as major players in the process of <a href="Synaptic_stabilization" title="Synaptic stabilization">synaptic stabilization</a>. Each cadherin exhibits a unique pattern of tissue distribution that is carefully controlled by calcium. The diverse family of cadherins include epithelial (E-cadherins), placental (P-cadherins), neural (N-cadherins), retinal (<a href="CDH4" title="CDH4">R-cadherins</a>), brain (B-cadherins and T-cadherins), and muscle (M-cadherins).<sup id="cite_ref-Buxton1992_18-2" class="reference"><a href="#cite_note-Buxton1992-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> Many cell types express combinations of cadherin types.

</p><p>The <a href="Extracellular" class="mw-redirect" title="Extracellular">extracellular</a> domain has major repeats called extracellular cadherin domains (ECD). Sequences involved in <span class="chemf nowrap">Ca<span class="nowrap"><span style="display:inline-block;margin-bottom:-0.3em;vertical-align:0.8em;line-height:1em;font-size:80%;text-align:left"><sup style="font-size:inherit;line-height:inherit;vertical-align:baseline">2+</sup><br><sub style="font-size:inherit;line-height:inherit;vertical-align:baseline"></sub></span></span></span> binding between the ECDs are necessary for <a href="Cell_adhesion" title="Cell adhesion">cell adhesion</a>. The cytoplasmic domain has specific regions where catenin proteins bind.<sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup>

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<div class="mw-heading mw-heading4"><h4 id="Selectins">Selectins</h4></div>

<div role="note" class="hatnote navigation-not-searchable">Main article: <a href="Selectin" title="Selectin">Selectin</a></div>

<p>The <b><a href="Selectin" title="Selectin">selectins</a></b> are a family of heterophilic CAMs that are dependent on <a href="Fucosylation" title="Fucosylation">fucosylated</a> carbohydrates, e.g., <a href="Mucin" title="Mucin">mucins</a> for binding. The three family members are <a href="E-selectin" title="E-selectin">E-selectin</a> (<a href="Endothelium" title="Endothelium">endothelial</a>), <a href="L-selectin" title="L-selectin">L-selectin</a> (<a href="Leukocyte" class="mw-redirect" title="Leukocyte">leukocyte</a>), and <a href="P-selectin" title="P-selectin">P-selectin</a> (<a href="Platelet" title="Platelet">platelet</a>). The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (<a href="PSGL-1" class="mw-redirect" title="PSGL-1">PSGL-1</a>), which is a mucin-type glycoprotein expressed on all white blood cells. Selectins have been implicated in several roles but they are especially important in the immune system by helping white blood cell homing and trafficking.<sup id="cite_ref-pmid14964308_20-0" class="reference"><a href="#cite_note-pmid14964308-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup>

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<div class="mw-heading mw-heading2"><h2 id="Biological_function_of_CAMs">Biological function of CAMs</h2></div>

<p>The variety in CAMs leads to diverse functionality of these proteins in the biological setting. One of the CAMS that are particularly important in the lymphocyte homing is <a href="Addressin" title="Addressin">addressin</a>.<sup id="cite_ref-21" class="reference"><a href="#cite_note-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> Lymphocyte homing is a key process occurring in a strong immune system. It controls the process of circulating lymphocytes adhering to particular regions and organs of the body.<sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> The process is highly regulated by cell adhesion molecules, particularly, the addressin also known as MADCAM1. This antigen is known for its role in tissue-specific adhesion of lymphocytes to high endothelium venules.<sup id="cite_ref-pmid19860663_23-0" class="reference"><a href="#cite_note-pmid19860663-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> Through these interactions they play a crucial role in orchestrating circulating lymphocytes.

</p><p>CAM function in cancer metastasis, inflammation, and thrombosis makes it a viable therapeutic target that is currently being considered. For example, they block the metastatic cancer cells' ability to extravasate and home to secondary sites. This has been successfully demonstrated in metastatic melanoma that hones to the lungs. In mice, when antibodies directed against CAMs in the lung endothelium were used as treatment there was a significant reduction in the number of metastatic sites.<sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup>

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<div class="side-box-text plainlist">Wikimedia Commons has media related to <span style="font-weight: bold; font-style: italic;"><a href="https://commons.wikimedia.org/wiki/Category:Cell_adhesion_molecules" class="extiw external" title="commons:Category:Cell adhesion molecules">Cell adhesion molecules</a></span>.</div></div>

</div>

<ul><li><a href="Cell_membrane" title="Cell membrane">Cell membrane</a></li>

<li><a href="Cell_migration" title="Cell migration">Cell migration</a></li>

<li><a href="Immunological_synapse" title="Immunological synapse">Immunological synapse</a></li>

<li><a href="Trogocytosis" title="Trogocytosis">Trogocytosis</a></li></ul>

<div class="mw-heading mw-heading2"><h2 id="References">References</h2></div>

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<li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Cell+Adhesion+Molecules">Cell+Adhesion+Molecules</a> at the U.S. National Library of Medicine <a href="Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</span>

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<li id="cite_note-21"><span class="mw-cite-backlink"><b><a href="#cite_ref-21">^</a></b></span> <span class="reference-text"><cite id="CITEREFBergGoldsteinJimlaNakache1989" class="citation journal cs1">Berg, Ellen Lakey; Goldstein, Leslie A.; Jimla, Mark A.; Nakache, Maurice; Picker, Louis J.; Streeter, Philip R.; Wu, Nora W.; Zhou, David; Butcher, Eugene C. (1 April 1989). "Homing Receptors and Vascular Addressins: Cell Adhesion Molecules that Direct Lymphocyte Traffic". <i>Immunological Reviews</i>. <b>108</b> (1): <span class="nowrap">5–</span>18. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1600-065X.1989.tb00010.x">10.1111/j.1600-065X.1989.tb00010.x</a>. <a href="ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/1600-065X">1600-065X</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/2670744">2670744</a>. <a href="S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:37831094">37831094</a>.</cite></span>

</li>

<li id="cite_note-22"><span class="mw-cite-backlink"><b><a href="#cite_ref-22">^</a></b></span> <span class="reference-text"><cite id="CITEREFPicker1994" class="citation journal cs1">Picker, Louis (1 June 1994). "Control of lymphocyte homing". <i>Current Opinion in Immunology</i>. <b>6</b> (3): <span class="nowrap">394–</span>406. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2F0952-7915%2894%2990118-X">10.1016/0952-7915(94)90118-X</a>. <a href="ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/0952-7915">0952-7915</a>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/7917107">7917107</a>.</cite></span>

</li>

<li id="cite_note-pmid19860663-23"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid19860663_23-0">^</a></b></span> <span class="reference-text"><cite id="CITEREFGorfuRivera-NievesLey2009" class="citation journal cs1">Gorfu G, Rivera-Nieves J, Ley K (September 2009). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770881">"Role of beta7 integrins in intestinal lymphocyte homing and retention"</a>. <i>Curr. Mol. Med</i>. <b>9</b> (7): <span class="nowrap">836–</span>50. <a href="Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F156652409789105525">10.2174/156652409789105525</a>. <a href="ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/1566-5240">1566-5240</a>. <a href="PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770881">2770881</a></span>. <a href="PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19860663">19860663</a>.</cite></span>

</li>

<li id="cite_note-24"><span class="mw-cite-backlink"><b><a href="#cite_ref-24">^</a></b></span> <span class="reference-text"><cite id="CITEREFAndreoliBrownFambroughHoffman2013" class="citation book cs1">Andreoli, Thomas E.; Brown, A. M.; Fambrough, D. M.; Hoffman, Joseph F.; Schultz, Stanley G.; Welsh, Michael J. (2013). <a rel="nofollow" class="external text" href="https://books.google.com/books?id=GvTjBwAAQBAJ&pg=PA34"><i>Molecular Biology of Membrane Transport Disorders</i></a>. Springer Science & Business Media. <a href="ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <bdi>978-1-4613-1143-0</bdi>.</cite></span>

</li>

</ol></div></div>

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</style><div id="Membrane_proteins:_cell_adhesion_molecules183" style="font-size:114%;margin:0 4em"><a href="Membrane_protein" title="Membrane protein">Membrane proteins</a>: </div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a class="mw-selflink-fragment" href="#Calcium-independent">Calcium-independent</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="IgSF_CAM" title="IgSF CAM">IgSF CAM</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Neural_cell_adhesion_molecule" title="Neural cell adhesion molecule">N-CAM</a> (<a href="Myelin_protein_zero" title="Myelin protein zero">Myelin protein zero</a>)</li>

<li><a href="L1_family" title="L1 family">L1 family</a>

<li><a href="NRCAM" title="NRCAM">NRCAM</a></li>

<li><a href="NFASC" title="NFASC">NFASC</a></li>

<li><a href="Nectin" title="Nectin">Nectin</a>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Integrin" title="Integrin">Integrins</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<li><a href="Integrin_alphaXbeta2" class="mw-redirect" title="Integrin alphaXbeta2">Integrin alphaXbeta2</a> (<a href="CD11c" class="mw-redirect" title="CD11c">CD11c</a>+<a href="CD18" class="mw-redirect" title="CD18">CD18</a>)</li>

<li><a href="Macrophage-1_antigen" title="Macrophage-1 antigen">Macrophage-1 antigen</a> (<a href="CD11b" class="mw-redirect" title="CD11b">CD11b</a>+<a href="CD18" class="mw-redirect" title="CD18">CD18</a>)</li>

<li><a href="Glycoprotein_IIb/IIIa" title="Glycoprotein IIb/IIIa">Glycoprotein IIb/IIIa</a> (<a href="ITGA2B" class="mw-redirect" title="ITGA2B">ITGA2B</a>+<a href="ITGB3" class="mw-redirect" title="ITGB3">ITGB3</a>)</li></ul>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a class="mw-selflink-fragment" href="#Calcium-dependent">Calcium-dependent</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Cadherin" title="Cadherin">Cadherins</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">Classical</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Desmosome" title="Desmosome">Desmosomal</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Desmoglein" title="Desmoglein">Desmoglein</a> (<a href="Desmoglein-1" title="Desmoglein-1">DSG1</a>, <a href="Desmoglein-2" title="Desmoglein-2">DSG2</a>, <a href="Desmoglein-3" title="Desmoglein-3">DSG3</a>, <a href="Desmoglein-4" title="Desmoglein-4">DSG4</a>)</li>

<li><a href="Desmocollin" title="Desmocollin">Desmocollin</a> (<a href="DSC1" title="DSC1">DSC1</a>, <a href="DSC2" title="DSC2">DSC2</a>, <a href="DSC3" title="DSC3">DSC3</a>)</li></ul>

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Protocadherin" title="Protocadherin">Protocadherin</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

</div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Unconventional/ungrouped</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="T-cadherin" title="T-cadherin">T-cadherin</a></li>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="Selectin" title="Selectin">Selectins</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="E-selectin" title="E-selectin">E-selectin</a></li>

<li><a href="L-selectin" title="L-selectin">L-selectin</a></li>

<li><a href="P-selectin" title="P-selectin">P-selectin</a></li></ul>

</div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em">

<ul><li><a href="Lymphocyte_homing_receptor" title="Lymphocyte homing receptor">Lymphocyte homing receptor</a>: <a href="CD44" title="CD44">CD44</a></li>

<li><a href="L-selectin" title="L-selectin">L-selectin</a></li>

<li><i><a href="Integrin" title="Integrin">integrin</a></i> (<a href="VLA-4" title="VLA-4">VLA-4</a>, <a href="LFA-1" class="mw-redirect" title="LFA-1">LFA-1</a>)</li></ul>

<ul><li><a href="Carcinoembryonic_antigen" title="Carcinoembryonic antigen">Carcinoembryonic antigen</a></li>

<li><a href="Epithelial_cell_adhesion_molecule" title="Epithelial cell adhesion molecule">EpCAM</a></li></ul>

</div></td></tr></tbody></table></div></div><div><div class="zim-footer">

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