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Cell adhesion molecule

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208:. The integrins contain multiple divalent cation binding sites in the extracellular domain ). 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. 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. However, extracellular Ca2+ binding may exert different effects depending on the type of integrin and the cation concentration. Integrins regulate their activity within the body by changing conformation. Most exist at rest in a low 45:. 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. 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. 409:. 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. 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. Through these interactions they play a crucial role in orchestrating circulating lymphocytes. 425: 200:, as they consist of an alpha and beta subunit. There are currently 18 alpha subunits and 8 beta subunits, which combine to make up 24 different integrin combinations. Within each of the alpha and beta subunits there is a large extracellular domain, a transmembrane domain and a short cytoplasmic domain. The extracellular domain is where the 108:
One classification system involves the distinction between calcium-independent CAMs and calcium-dependent CAMs. The Ig-superfamily CAMs do not depend on Ca while integrins, cadherins and selectins depend on Ca. In addition, integrins participate in cell–matrix interactions, while other CAM families
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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
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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".
397:), 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. 315:. 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 ( 311:. 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 413:
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.
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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
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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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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
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state, which can be altered to high affinity through an external agonist which causes a conformational change within the integrin, increasing their affinity.
1531: 61:, a transmembrane domain, and an extracellular domain. These proteins can interact in several different ways. The first method is through 2075: 94: 1680: 16:
This article is about cell adhesion molecules. For the role of CAMs in the formation and stabilization of neural synapses, see
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Korthuis RJ, Anderson DC, Granger DN (March 1994). "Role of neutrophil-endothelial cell adhesion in inflammatory disorders".
319:), brain (B-cadherins and T-cadherins), and muscle (M-cadherins). Many cell types express combinations of cadherin types. 1486:
Andreoli, Thomas E.; Brown, A. M.; Fambrough, D. M.; Hoffman, Joseph F.; Schultz, Stanley G.; Welsh, Michael J. (2013).
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Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James (2000-01-01).
2049: 209: 2070: 1517: 1579: 972:"Crystal Structure of the Extracellular Segment of Integrin alpha Vbeta 3 in Complex with an Arg-Gly-Asp Ligand" 1283:
Cavallaro U, Christofori G (February 2004). "Cell adhesion and signalling by cadherins and Ig-CAMs in cancer".
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Dai, Aguang; Ye, Feng; Taylor, Dianne W.; Hu, Guiqing; Ginsberg, Mark H.; Taylor, Kenneth A. (November 2015).
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Buxton RS, Magee AI (June 1992). "Structure and interactions of desmosomal and other cadherins".
186: 312: 54: 17: 393:). The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 ( 1736: 1509: 1487: 769: 703:"Distinct calcium-independent and calcium-dependent adhesion systems of chicken embryo cells" 448: 57:
and are composed of three conserved domains: an intracellular domain that interacts with the
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domain has major repeats called extracellular cadherin domains (ECD). Sequences involved in
1708: 1694: 1027:"The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand" 983: 714: 177:
and the intracellular signalling pathways, which can play roles in cell behaviours such as
157:, one of the major classes of receptors within the ECM, mediate cell–ECM interactions with 38: 8: 1573: 646: 987: 718: 1463: 1430: 1368: 1348: 1316: 1260: 1233: 1169: 1136: 1112: 1077: 1053: 1026: 1007: 907: 851: 826: 683: 253: 1210: 1078:"The Calcium-Sensing Receptor and Integrins in Cellular Differentiation and Migration" 971: 809: 737: 702: 554: 537: 295:
Cadherins are notable in embryonic development. For example, cadherins are crucial in
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GarcĂ­a AJ (December 2005). "Get a grip: integrins in cell-biomaterial interactions".
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Brown, K; Yamada, K (1995), "The Role of Integrins during Vertebrae Development",
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Chothia C, Jones EY (1997). "The molecular structure of cell adhesion molecules".
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binding, meaning a CAM on one cell will bind with different CAMs on another cell.
1446: 761: 443: 430: 78: 2064: 1856: 1454: 1407: 1356: 1304: 1160: 1103: 1094: 606: 563: 538:"Cell adhesion: the molecular basis of tissue architecture and morphogenesis" 514: 438: 338: 323: 265: 102: 42: 1043: 995: 1827: 1823: 1819: 1815: 1608: 1472: 1312: 1269: 1178: 1121: 1062: 1003: 915: 860: 628: 490: 453: 362: 341:. The cytoplasmic domain has specific regions where catenin proteins bind. 296: 58: 1415: 1364: 1218: 956: 746: 727: 679: 614: 571: 522: 227:
trigger the integrin into its high affinity state, which causes increased
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binding, where CAMs bind with the same CAMs. They are also capable of
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Picker, Louis (1 June 1994). "Control of lymphocyte homing".
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filament network through specific linking proteins called
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There are four major superfamilies or groups of CAMs: the
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Brackenbury R, Rutishauser U, Edelman GM (January 1981).
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are a family of heterophilic CAMs that are dependent on
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Tharmalingam, Sujeenthar; Hampson, David R. (2016).
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Humphries JD, Byron A, Humphries MJ (October 2006).
491:"The molecular structure of cell adhesion molecules" 420: 1075: 1429:Gorfu G, Rivera-Nieves J, Ley K (September 2009). 1489:Molecular Biology of Membrane Transport Disorders 795: 2062: 820: 818: 173:. Integrins provide essential links between the 874: 872: 870: 400: 1525: 1192: 1190: 1188: 1024: 815: 635:. College of Pharmacy, University of Michigan 1422: 1276: 657: 488: 1196: 1135:Zhang, Kun; Chen, JianFeng (January 2012). 922: 867: 337:binding between the ECDs are necessary for 105:are also considered to be a class of CAMs. 1532: 1518: 1231: 1185: 928: 887: 694: 651: 578: 369:for binding. The three family members are 1492:. Springer Science & Business Media. 1462: 1259: 1249: 1168: 1134: 1111: 1093: 1052: 1042: 946: 893: 850: 736: 726: 553: 475:at the U.S. National Library of Medicine 215:An example of this is the aggregation of 81:super family of cell adhesion molecules ( 1552: 789: 535: 878: 231:binding, causing platelet aggregation. 109:participate in cell–cell interactions. 2063: 1759: 1385: 762:"Cell–Cell Adhesion and Communication" 112: 95:C-type of lectin-like domains proteins 37:of cells with other cells or with the 1513: 969: 138: 72: 13: 2076:Single-pass transmembrane proteins 1349:10.1111/j.1600-065X.1989.tb00010.x 908:10.1016/j.biomaterials.2005.05.029 489:Chothia, C.; Jones, E. Y. (1997). 204:binds through the use of divalent 14: 2087: 935:Eur J Obstet Gynecol Reprod Biol 672:10.1146/annurev.biochem.66.1.823 507:10.1146/annurev.biochem.66.1.823 423: 53:CAMs are typically single-pass 23:Subset of cell adhesion proteins 1479: 1379: 1327: 1232:Soncin, F.; Ward, M.C. (2011). 1225: 1128: 1069: 1031:Journal of Biological Chemistry 1018: 963: 881:Integrin, Adhesion/cell-matrix 827:"Integrin ligands at a glance" 753: 621: 536:Gumbiner, B. M. (1996-02-09). 529: 482: 466: 1: 1388:Current Opinion in Immunology 1211:10.1016/s1043-4682(10)80012-1 1141:Cell Adhesion & Migration 810:10.1016/s1044-5781(06)80016-2 555:10.1016/s0092-8674(00)81279-9 495:Annual Review of Biochemistry 459: 1400:10.1016/0952-7915(94)90118-X 948:10.1016/0028-2243(94)01987-I 931:"Integrins and reproduction" 707:Proc. Natl. Acad. Sci. U.S.A 599:10.1016/0883-9441(94)90032-9 344: 234: 143: 117: 48: 7: 970:Xiong, J.-P. (2002-04-05). 416: 401:Biological function of CAMs 282:intermediate cell junctions 133:Fibronectin type III domain 41:(ECM), in a process called 10: 2092: 1998:Lymphocyte homing receptor 1447:10.2174/156652409789105525 348: 280:) are concentrated at the 238: 147: 129:Immunoglobulin superfamily 121: 15: 1990: 1958: 1883: 1855: 1802: 1776: 1767: 1758: 1671: 1560: 1551: 929:Vinatier D (March 1995). 299:for the formation of the 268:. The classic cadherins ( 175:extracellular environment 93:, and the Superfamily of 2030:Carcinoembryonic antigen 1884:Unconventional/ungrouped 1095:10.3389/fphys.2016.00190 477:Medical Subject Headings 2071:Cell adhesion molecules 1545:cell adhesion molecules 1082:Frontiers in Physiology 1044:10.1074/jbc.M115.682377 996:10.1126/science.1069040 473:Cell+Adhesion+Molecules 55:transmembrane receptors 27:Cell adhesion molecules 777:Cite journal requires 313:synaptic stabilization 18:Synaptic stabilization 1737:Glycoprotein IIb/IIIa 1337:Immunological Reviews 798:Developmental Biology 728:10.1073/pnas.78.1.387 449:Immunological synapse 365:carbohydrates, e.g., 1709:Macrophage-1 antigen 1695:Integrin alphaXbeta2 1251:10.3390/genes2010229 883:. Seattle: Elsevier. 284:, which link to the 39:extracellular matrix 1574:Myelin protein zero 1553:Calcium-independent 1037:(45): 27168–27175. 988:2002Sci...296..151X 879:Schnapp, L (2006). 719:1981PNAS...78..387B 647:Membranome database 219:; Agonists such as 113:Calcium-independent 660:Annu. Rev. Biochem 2058: 2057: 1986: 1985: 1954: 1953: 1760:Calcium-dependent 1754: 1753: 1541:Membrane proteins 1499:978-1-4613-1143-0 1153:10.4161/cam.18702 982:(5565): 151–155. 843:10.1242/jcs.03098 837:(Pt 19): 3901–3. 139:Calcium-dependent 2083: 1774: 1773: 1765: 1764: 1558: 1557: 1534: 1527: 1520: 1511: 1510: 1504: 1503: 1483: 1477: 1476: 1466: 1426: 1420: 1419: 1383: 1377: 1376: 1331: 1325: 1324: 1285:Nat. Rev. Cancer 1280: 1274: 1273: 1263: 1253: 1229: 1223: 1222: 1199:Semin. Cell Biol 1194: 1183: 1182: 1172: 1132: 1126: 1125: 1115: 1097: 1073: 1067: 1066: 1056: 1046: 1022: 1016: 1015: 967: 961: 960: 950: 926: 920: 919: 891: 885: 884: 876: 865: 864: 854: 822: 813: 812: 793: 787: 786: 780: 775: 773: 765: 757: 751: 750: 740: 730: 698: 692: 691: 655: 649: 644: 642: 640: 625: 619: 618: 582: 576: 575: 557: 533: 527: 526: 486: 480: 470: 433: 428: 427: 336: 335: 334: 263: 261: 260: 73:Families of CAMs 2091: 2090: 2086: 2085: 2084: 2082: 2081: 2080: 2061: 2060: 2059: 2054: 1982: 1950: 1879: 1851: 1798: 1750: 1667: 1547: 1538: 1508: 1507: 1500: 1484: 1480: 1427: 1423: 1384: 1380: 1332: 1328: 1297:10.1038/nrc1276 1281: 1277: 1230: 1226: 1195: 1186: 1133: 1129: 1074: 1070: 1023: 1019: 968: 964: 927: 923: 892: 888: 877: 868: 823: 816: 794: 790: 778: 776: 767: 766: 758: 754: 699: 695: 656: 652: 638: 636: 627: 626: 622: 583: 579: 534: 530: 487: 483: 471: 467: 462: 429: 422: 419: 403: 353: 347: 333: 331: 330: 329: 327: 259: 257: 256: 255: 252: 251:are homophilic 243: 237: 183:differentiation 152: 146: 141: 126: 120: 115: 75: 51: 24: 21: 12: 11: 5: 2089: 2079: 2078: 2073: 2056: 2055: 2053: 2052: 2047: 2042: 2037: 2032: 2026: 2025: 2009: 2004: 1994: 1992: 1988: 1987: 1984: 1983: 1981: 1980: 1975: 1970: 1964: 1962: 1956: 1955: 1952: 1951: 1949: 1948: 1943: 1938: 1933: 1928: 1923: 1918: 1913: 1908: 1903: 1898: 1893: 1887: 1885: 1881: 1880: 1878: 1877: 1872: 1867: 1861: 1859: 1853: 1852: 1850: 1849: 1831: 1808: 1806: 1800: 1799: 1797: 1796: 1791: 1786: 1780: 1778: 1771: 1762: 1756: 1755: 1752: 1751: 1749: 1748: 1734: 1720: 1706: 1692: 1677: 1675: 1669: 1668: 1666: 1665: 1664: 1663: 1658: 1653: 1648: 1643: 1638: 1628: 1627: 1626: 1621: 1616: 1611: 1601: 1596: 1591: 1577: 1566: 1564: 1555: 1549: 1548: 1537: 1536: 1529: 1522: 1514: 1506: 1505: 1498: 1478: 1435:Curr. Mol. Med 1421: 1394:(3): 394–406. 1378: 1326: 1275: 1244:(1): 229–259. 1224: 1184: 1127: 1068: 1017: 962: 921: 902:(36): 7525–9. 886: 866: 814: 788: 779:|journal= 752: 693: 650: 620: 577: 548:(3): 345–357. 528: 481: 464: 463: 461: 458: 457: 456: 451: 446: 444:Cell migration 441: 435: 434: 431:Biology portal 418: 415: 402: 399: 349:Main article: 346: 343: 332: 258: 239:Main article: 236: 233: 196:Integrins are 148:Main article: 145: 142: 140: 137: 122:Main article: 119: 116: 114: 111: 79:immunoglobulin 74: 71: 50: 47: 22: 9: 6: 4: 3: 2: 2088: 2077: 2074: 2072: 2069: 2068: 2066: 2051: 2048: 2046: 2043: 2041: 2038: 2036: 2033: 2031: 2028: 2027: 2023: 2019: 2015: 2014: 2010: 2008: 2005: 2003: 1999: 1996: 1995: 1993: 1989: 1979: 1976: 1974: 1971: 1969: 1966: 1965: 1963: 1961: 1957: 1947: 1944: 1942: 1939: 1937: 1934: 1932: 1929: 1927: 1924: 1922: 1919: 1917: 1914: 1912: 1909: 1907: 1904: 1902: 1899: 1897: 1894: 1892: 1889: 1888: 1886: 1882: 1876: 1873: 1871: 1868: 1866: 1863: 1862: 1860: 1858: 1857:Protocadherin 1854: 1847: 1843: 1839: 1835: 1832: 1829: 1825: 1821: 1817: 1813: 1810: 1809: 1807: 1805: 1801: 1795: 1792: 1790: 1787: 1785: 1782: 1781: 1779: 1775: 1772: 1770: 1766: 1763: 1761: 1757: 1746: 1742: 1738: 1735: 1732: 1728: 1724: 1721: 1718: 1714: 1710: 1707: 1704: 1700: 1696: 1693: 1690: 1686: 1682: 1679: 1678: 1676: 1674: 1670: 1662: 1659: 1657: 1654: 1652: 1649: 1647: 1644: 1642: 1639: 1637: 1634: 1633: 1632: 1629: 1625: 1622: 1620: 1617: 1615: 1612: 1610: 1607: 1606: 1605: 1602: 1600: 1597: 1595: 1592: 1589: 1585: 1581: 1578: 1575: 1571: 1568: 1567: 1565: 1563: 1559: 1556: 1554: 1550: 1546: 1542: 1535: 1530: 1528: 1523: 1521: 1516: 1515: 1512: 1501: 1495: 1491: 1490: 1482: 1474: 1470: 1465: 1460: 1456: 1452: 1448: 1444: 1441:(7): 836–50. 1440: 1436: 1432: 1425: 1417: 1413: 1409: 1405: 1401: 1397: 1393: 1389: 1382: 1374: 1370: 1366: 1362: 1358: 1354: 1350: 1346: 1342: 1338: 1330: 1322: 1318: 1314: 1310: 1306: 1302: 1298: 1294: 1291:(2): 118–32. 1290: 1286: 1279: 1271: 1267: 1262: 1257: 1252: 1247: 1243: 1239: 1235: 1228: 1220: 1216: 1212: 1208: 1205:(3): 157–67. 1204: 1200: 1193: 1191: 1189: 1180: 1176: 1171: 1166: 1162: 1158: 1154: 1150: 1146: 1142: 1138: 1131: 1123: 1119: 1114: 1109: 1105: 1101: 1096: 1091: 1087: 1083: 1079: 1072: 1064: 1060: 1055: 1050: 1045: 1040: 1036: 1032: 1028: 1021: 1013: 1009: 1005: 1001: 997: 993: 989: 985: 981: 977: 973: 966: 958: 954: 949: 944: 940: 936: 932: 925: 917: 913: 909: 905: 901: 897: 890: 882: 875: 873: 871: 862: 858: 853: 848: 844: 840: 836: 832: 828: 821: 819: 811: 807: 803: 799: 792: 784: 771: 763: 756: 748: 744: 739: 734: 729: 724: 720: 716: 713:(1): 387–91. 712: 708: 704: 697: 689: 685: 681: 677: 673: 669: 665: 661: 654: 648: 634: 630: 624: 616: 612: 608: 604: 600: 596: 592: 588: 581: 573: 569: 565: 561: 556: 551: 547: 543: 539: 532: 524: 520: 516: 512: 508: 504: 500: 496: 492: 485: 478: 474: 469: 465: 455: 452: 450: 447: 445: 442: 440: 439:Cell membrane 437: 436: 432: 426: 421: 414: 410: 408: 398: 396: 392: 388: 384: 380: 376: 372: 368: 364: 360: 359: 352: 342: 340: 339:cell adhesion 325: 324:extracellular 320: 318: 314: 310: 306: 302: 298: 293: 291: 287: 283: 279: 275: 271: 267: 266:glycoproteins 262: 250: 249: 242: 232: 230: 226: 222: 218: 213: 211: 207: 203: 199: 198:heterodimeric 194: 192: 191:transcription 188: 184: 180: 176: 172: 168: 164: 160: 156: 151: 136: 134: 130: 125: 110: 106: 104: 103:Proteoglycans 100: 96: 92: 88: 84: 80: 70: 68: 64: 60: 56: 46: 44: 43:cell adhesion 40: 36: 32: 28: 19: 2011: 1544: 1488: 1481: 1438: 1434: 1424: 1391: 1387: 1381: 1340: 1336: 1329: 1288: 1284: 1278: 1241: 1237: 1227: 1202: 1198: 1147:(1): 20–29. 1144: 1140: 1130: 1085: 1081: 1071: 1034: 1030: 1020: 979: 975: 965: 941:(1): 71–81. 938: 934: 924: 899: 896:Biomaterials 895: 889: 880: 834: 830: 804:(2): 69–77, 801: 797: 791: 770:cite journal 755: 710: 706: 696: 663: 659: 653: 637:. Retrieved 632: 623: 593:(1): 47–71. 590: 586: 580: 545: 541: 531: 498: 494: 484: 468: 454:Trogocytosis 411: 404: 356: 354: 321: 297:gastrulation 294: 246: 244: 214: 195: 153: 127: 107: 98: 76: 67:heterophilic 66: 62: 59:cytoskeleton 52: 30: 26: 25: 1834:Desmocollin 1343:(1): 5–18. 831:J. Cell Sci 639:October 20, 587:J Crit Care 501:: 823–862. 375:endothelial 363:fucosylated 317:R-cadherins 264:-dependent 171:vitronectin 167:fibronectin 2065:Categories 2007:L-selectin 1978:P-selectin 1973:L-selectin 1968:E-selectin 1891:T-cadherin 1812:Desmoglein 1804:Desmosomal 666:: 823–62. 633:membranome 460:References 387:P-selectin 379:L-selectin 371:E-selectin 229:fibrinogen 163:fibrinogen 63:homophilic 1960:Selectins 1777:Classical 1769:Cadherins 1673:Integrins 1604:L1 family 1455:1566-5240 1408:0952-7915 1357:1600-065X 1305:1474-1768 1161:1933-6918 1104:1664-042X 607:0883-9441 564:0092-8674 515:0066-4154 407:addressin 383:leukocyte 358:selectins 345:Selectins 248:cadherins 235:Cadherins 217:platelets 179:apoptosis 155:Integrins 144:Integrins 118:IgSF CAMs 91:Integrins 87:Cadherins 49:Structure 2013:integrin 1562:IgSF CAM 1473:19860663 1373:37831094 1321:18383054 1313:14964308 1270:24710147 1179:22647937 1122:27303307 1063:26391523 1012:24339086 1004:11884718 916:16002137 861:16988024 417:See also 391:platelet 351:Selectin 309:ectoderm 305:endoderm 301:mesoderm 290:catenins 241:Cadherin 225:collagen 221:thrombin 210:affinity 187:survival 159:collagen 150:Integrin 124:IgSF CAM 1464:2770881 1416:7917107 1365:2670744 1261:3924836 1219:1623205 1170:3364134 1113:4880553 1088:: 190. 1054:4646401 984:Bibcode 976:Science 957:7781865 852:3380273 747:6165990 715:Bibcode 688:6298053 680:9242926 615:8199653 572:8608588 523:9242926 385:), and 206:cations 35:binding 1875:PCDH19 1870:PCDH15 1741:ITGA2B 1631:Nectin 1609:L1-CAM 1599:PE-CAM 1594:VCAM-1 1496:  1471:  1461:  1453:  1414:  1406:  1371:  1363:  1355:  1319:  1311:  1303:  1268:  1258:  1217:  1177:  1167:  1159:  1120:  1110:  1102:  1061:  1051:  1010:  1002:  955:  914:  859:  849:  745:  738:319058 735:  686:  678:  613:  605:  570:  562:  521:  513:  479:(MeSH) 395:PSGL-1 367:mucins 307:, and 202:ligand 189:, and 169:, and 83:IgCAMs 2050:EpCAM 2045:CD146 2022:LFA-1 2018:VLA-4 1991:Other 1946:CDH10 1936:CDH17 1931:CDH16 1926:CDH15 1921:CDH12 1916:CDH11 1865:PCDH1 1745:ITGB3 1727:CD49d 1723:VLA-4 1713:CD11b 1699:CD11c 1685:CD11a 1681:LFA-1 1661:CD155 1656:CADM3 1651:CADM1 1646:PVRL3 1641:PVRL2 1636:PVRL1 1619:NFASC 1614:NRCAM 1570:N-CAM 1369:S2CID 1317:S2CID 1238:Genes 1008:S2CID 684:S2CID 286:actin 99:CTLDs 2040:CD44 2035:CD24 2002:CD44 1941:CDH9 1911:CDH8 1906:CDH6 1901:CDH5 1896:CDH4 1846:DSC3 1842:DSC2 1838:DSC1 1828:DSG4 1824:DSG3 1820:DSG2 1816:DSG1 1794:CDH3 1789:CDH2 1784:CDH1 1731:CD29 1717:CD18 1703:CD18 1689:CD18 1624:CHL1 1580:ICAM 1494:ISBN 1469:PMID 1451:ISSN 1412:PMID 1404:ISSN 1361:PMID 1353:ISSN 1309:PMID 1301:ISSN 1266:PMID 1215:PMID 1175:PMID 1157:ISSN 1118:PMID 1100:ISSN 1059:PMID 1000:PMID 953:PMID 912:PMID 857:PMID 783:help 743:PMID 676:PMID 641:2018 611:PMID 603:ISSN 568:PMID 560:ISSN 542:Cell 519:PMID 511:ISSN 355:The 322:The 276:and 245:The 31:CAMs 1459:PMC 1443:doi 1396:doi 1345:doi 1341:108 1293:doi 1256:PMC 1246:doi 1207:doi 1165:PMC 1149:doi 1108:PMC 1090:doi 1049:PMC 1039:doi 1035:290 992:doi 980:296 943:doi 904:doi 847:PMC 839:doi 835:119 806:doi 733:PMC 723:doi 668:doi 645:in 595:doi 550:doi 503:doi 377:), 223:or 101:). 85:), 2067:: 2020:, 2000:: 1844:, 1840:, 1826:, 1822:, 1818:, 1586:, 1543:: 1467:. 1457:. 1449:. 1437:. 1433:. 1410:. 1402:. 1390:. 1367:. 1359:. 1351:. 1339:. 1315:. 1307:. 1299:. 1287:. 1264:. 1254:. 1240:. 1236:. 1213:. 1201:. 1187:^ 1173:. 1163:. 1155:. 1143:. 1139:. 1116:. 1106:. 1098:. 1084:. 1080:. 1057:. 1047:. 1033:. 1029:. 1006:. 998:. 990:. 978:. 974:. 951:. 939:59 937:. 933:. 910:. 900:26 898:. 869:^ 855:. 845:. 833:. 829:. 817:^ 800:, 774:: 772:}} 768:{{ 741:. 731:. 721:. 711:78 709:. 705:. 682:. 674:. 664:66 662:. 631:. 609:. 601:. 589:. 566:. 558:. 546:84 544:. 540:. 517:. 509:. 499:66 497:. 493:. 328:Ca 303:, 292:. 278:P- 274:N- 272:, 270:E- 254:Ca 193:. 185:, 181:, 165:, 161:, 89:, 2024:) 2016:( 1848:) 1836:( 1830:) 1814:( 1747:) 1743:+ 1739:( 1733:) 1729:+ 1725:( 1719:) 1715:+ 1711:( 1705:) 1701:+ 1697:( 1691:) 1687:+ 1683:( 1590:) 1588:5 1584:1 1582:( 1576:) 1572:( 1533:e 1526:t 1519:v 1502:. 1475:. 1445:: 1439:9 1418:. 1398:: 1392:6 1375:. 1347:: 1323:. 1295:: 1289:4 1272:. 1248:: 1242:2 1221:. 1209:: 1203:3 1181:. 1151:: 1145:6 1124:. 1092:: 1086:7 1065:. 1041:: 1014:. 994:: 986:: 959:. 945:: 918:. 906:: 863:. 841:: 808:: 802:6 785:) 781:( 764:. 749:. 725:: 717:: 690:. 670:: 643:. 617:. 597:: 591:9 574:. 552:: 525:. 505:: 389:( 381:( 373:( 97:( 29:( 20:.

Index

Synaptic stabilization
binding
extracellular matrix
cell adhesion
transmembrane receptors
cytoskeleton
immunoglobulin
IgCAMs
Cadherins
Integrins
C-type of lectin-like domains proteins
Proteoglycans
IgSF CAM
Immunoglobulin superfamily
Fibronectin type III domain
Integrin
Integrins
collagen
fibrinogen
fibronectin
vitronectin
extracellular environment
apoptosis
differentiation
survival
transcription
heterodimeric
ligand
cations
affinity

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