219:. 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
56:. 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.
420:. 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.
436:
211:, 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
119:
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
423:
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
1345:
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".
408:), 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.
326:. 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 (
322:. 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
424:
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.
142:
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
146:
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.
416:
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
1542:
223:
state, which can be altered to high affinity through an external agonist which causes a conformational change within the integrin, increasing their affinity.
2086:
1691:
1535:
1508:
72:, a transmembrane domain, and an extracellular domain. These proteins can interact in several different ways. The first method is through
2060:
2081:
1528:
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27:
This article is about cell adhesion molecules. For the role of CAMs in the formation and stabilization of neural synapses, see
596:
Korthuis RJ, Anderson DC, Granger DN (March 1994). "Role of neutrophil-endothelial cell adhesion in inflammatory disorders".
1580:
330:), brain (B-cadherins and T-cadherins), and muscle (M-cadherins). Many cell types express combinations of cadherin types.
1497:
Andreoli, Thomas E.; Brown, A. M.; Fambrough, D. M.; Hoffman, Joseph F.; Schultz, Stanley G.; Welsh, Michael J. (2013).
105:
771:
Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James (2000-01-01).
143:
2008:
139:
185:
983:"Crystal Structure of the Extracellular Segment of Integrin alpha Vbeta 3 in Complex with an Arg-Gly-Asp Ligand"
2040:
1294:
Cavallaro U, Christofori G (February 2004). "Cell adhesion and signalling by cadherins and Ig-CAMs in cancer".
487:
201:
193:
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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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994:
725:
49:
1584:
657:
483:
1379:
1327:
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Buxton RS, Magee AI (June 1992). "Structure and interactions of desmosomal and other cadherins".
1018:
694:
264:
1504:
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1371:
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963:
922:
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404:). The best-characterized ligand for the three selectins is P-selectin glycoprotein ligand-1 (
292:
45:
1520:
1498:
714:"Distinct calcium-independent and calcium-dependent adhesion systems of chicken embryo cells"
68:
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
1038:"The Structure of a Full-length Membrane-embedded Integrin Bound to a Physiological Ligand"
188:
and the intracellular signalling pathways, which can play roles in cell behaviours such as
168:, one of the major classes of receptors within the ECM, mediate cell–ECM interactions with
793:
998:
729:
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837:
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441:
89:
17:
1221:
1089:"The Calcium-Sensing Receptor and Integrins in Cellular Differentiation and Migration"
982:
820:
748:
713:
565:
548:
306:
Cadherins are notable in embryonic development. For example, cadherins are crucial in
2075:
1867:
1410:
958:
941:
905:
García AJ (December 2005). "Get a grip: integrins in cell-biomaterial interactions".
682:
609:
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53:
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464:
373:
307:
69:
807:
Brown, K; Yamada, K (1995), "The Role of
Integrins during Vertebrae Development",
669:
Chothia C, Jones EY (1997). "The molecular structure of cell adhesion molecules".
80:
binding, meaning a CAM on one cell will bind with different CAMs on another cell.
1911:
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2017:
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549:"Cell adhesion: the molecular basis of tissue architecture and morphogenesis"
525:
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352:. The cytoplasmic domain has specific regions where catenin proteins bind.
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trigger the integrin into its high affinity state, which causes increased
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97:
1442:"Role of beta7 integrins in intestinal lymphocyte homing and retention"
1245:"The Function of E-Cadherin in Stem Cell Pluripotency and Self-Renewal"
300:
1163:
853:
76:
binding, where CAMs bind with the same CAMs. They are also capable of
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44:) are a subset of cell surface proteins that are involved in the
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2012:
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Picker, Louis (1 June 1994). "Control of lymphocyte homing".
640:"Single-pass transmembrane adhesion and structural proteins"
299:
filament network through specific linking proteins called
88:
There are four major superfamilies or groups of CAMs: the
1148:"The regulation of integrin function by divalent cations"
712:
Brackenbury R, Rutishauser U, Edelman GM (January 1981).
372:
are a family of heterophilic CAMs that are dependent on
1087:
Tharmalingam, Sujeenthar; Hampson, David R. (2016).
836:
Humphries JD, Byron A, Humphries MJ (October 2006).
502:"The molecular structure of cell adhesion molecules"
2001:
1969:
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1440:Gorfu G, Rivera-Nieves J, Ley K (September 2009).
1500:Molecular Biology of Membrane Transport Disorders
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184:. Integrins provide essential links between the
885:
883:
881:
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1203:
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1199:
646:. College of Pharmacy, University of Michigan
8:
1146:Zhang, Kun; Chen, JianFeng (January 2012).
348:binding between the ECDs are necessary for
116:are also considered to be a class of CAMs.
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1543:
1529:
1521:
380:for binding. The three family members are
1503:. Springer Science & Business Media.
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486:at the U.S. National Library of Medicine
226:An example of this is the aggregation of
92:super family of cell adhesion molecules (
1563:
476:
242:binding, causing platelet aggregation.
120:participate in cell–cell interactions.
1770:
789:
778:
773:"Cell–Cell Adhesion and Communication"
106:C-type of lectin-like domains proteins
48:of cells with other cells or with the
7:
2087:Single-pass transmembrane proteins
1360:10.1111/j.1600-065X.1989.tb00010.x
919:10.1016/j.biomaterials.2005.05.029
500:Chothia, C.; Jones, E. Y. (1997).
215:binds through the use of divalent
25:
946:Eur J Obstet Gynecol Reprod Biol
683:10.1146/annurev.biochem.66.1.823
518:10.1146/annurev.biochem.66.1.823
434:
64:CAMs are typically single-pass
34:Subset of cell adhesion proteins
1243:Soncin, F.; Ward, M.C. (2011).
1042:Journal of Biological Chemistry
892:Integrin, Adhesion/cell-matrix
838:"Integrin ligands at a glance"
547:Gumbiner, B. M. (1996-02-09).
1:
1399:Current Opinion in Immunology
1222:10.1016/s1043-4682(10)80012-1
1152:Cell Adhesion & Migration
821:10.1016/s1044-5781(06)80016-2
566:10.1016/s0092-8674(00)81279-9
506:Annual Review of Biochemistry
1411:10.1016/0952-7915(94)90118-X
959:10.1016/0028-2243(94)01987-I
942:"Integrins and reproduction"
718:Proc. Natl. Acad. Sci. U.S.A
610:10.1016/0883-9441(94)90032-9
981:Xiong, J.-P. (2002-04-05).
412:Biological function of CAMs
293:intermediate cell junctions
144:Fibronectin type III domain
52:(ECM), in a process called
2103:
2009:Lymphocyte homing receptor
1458:10.2174/156652409789105525
359:
291:) are concentrated at the
249:
158:
140:Immunoglobulin superfamily
132:
26:
940:Vinatier D (March 1995).
310:for the formation of the
279:. The classic cadherins (
186:extracellular environment
104:, and the Superfamily of
2041:Carcinoembryonic antigen
1895:Unconventional/ungrouped
1106:10.3389/fphys.2016.00190
488:Medical Subject Headings
2082:Cell adhesion molecules
1556:cell adhesion molecules
1093:Frontiers in Physiology
1055:10.1074/jbc.M115.682377
1007:10.1126/science.1069040
484:Cell+Adhesion+Molecules
66:transmembrane receptors
38:Cell adhesion molecules
18:Cell adhesion molecules
788:Cite journal requires
324:synaptic stabilization
29:Synaptic stabilization
1748:Glycoprotein IIb/IIIa
1348:Immunological Reviews
809:Developmental Biology
739:10.1073/pnas.78.1.387
460:Immunological synapse
376:carbohydrates, e.g.,
1720:Macrophage-1 antigen
1706:Integrin alphaXbeta2
1262:10.3390/genes2010229
894:. Seattle: Elsevier.
295:, which link to the
50:extracellular matrix
1585:Myelin protein zero
1564:Calcium-independent
1048:(45): 27168–27175.
999:2002Sci...296..151X
890:Schnapp, L (2006).
730:1981PNAS...78..387B
658:Membranome database
230:; Agonists such as
124:Calcium-independent
671:Annu. Rev. Biochem
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1996:
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1771:Calcium-dependent
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1552:Membrane proteins
1510:978-1-4613-1143-0
1164:10.4161/cam.18702
993:(5565): 151–155.
854:10.1242/jcs.03098
848:(Pt 19): 3901–3.
150:Calcium-dependent
16:(Redirected from
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1377:
1373:
1369:
1365:
1361:
1357:
1353:
1349:
1341:
1338:
1333:
1329:
1325:
1321:
1317:
1313:
1309:
1305:
1302:(2): 118–32.
1301:
1297:
1290:
1287:
1282:
1278:
1273:
1268:
1263:
1258:
1254:
1250:
1246:
1239:
1236:
1231:
1227:
1223:
1219:
1216:(3): 157–67.
1215:
1211:
1204:
1202:
1200:
1196:
1191:
1187:
1182:
1177:
1173:
1169:
1165:
1161:
1157:
1153:
1149:
1142:
1139:
1134:
1130:
1125:
1120:
1116:
1112:
1107:
1102:
1098:
1094:
1090:
1083:
1080:
1075:
1071:
1066:
1061:
1056:
1051:
1047:
1043:
1039:
1032:
1029:
1024:
1020:
1016:
1012:
1008:
1004:
1000:
996:
992:
988:
984:
977:
974:
969:
965:
960:
955:
951:
947:
943:
936:
933:
928:
924:
920:
916:
912:
908:
901:
898:
893:
886:
884:
882:
878:
873:
869:
864:
859:
855:
851:
847:
843:
839:
832:
830:
826:
822:
818:
814:
810:
803:
800:
795:
782:
774:
767:
764:
759:
755:
750:
745:
740:
735:
731:
727:
724:(1): 387–91.
723:
719:
715:
708:
705:
700:
696:
692:
688:
684:
680:
676:
672:
665:
662:
659:
645:
641:
635:
632:
627:
623:
619:
615:
611:
607:
603:
599:
592:
589:
584:
580:
576:
572:
567:
562:
558:
554:
550:
543:
540:
535:
531:
527:
523:
519:
515:
511:
507:
503:
496:
493:
489:
485:
480:
477:
470:
466:
463:
461:
458:
456:
453:
451:
450:Cell membrane
448:
447:
443:
437:
432:
427:
425:
421:
419:
411:
409:
407:
403:
399:
395:
391:
387:
383:
379:
375:
371:
370:
363:
355:
353:
351:
350:cell adhesion
336:
335:extracellular
331:
329:
325:
321:
317:
313:
309:
304:
302:
298:
294:
290:
286:
282:
278:
277:glycoproteins
273:
261:
260:
253:
245:
243:
241:
237:
233:
229:
224:
222:
218:
214:
210:
209:heterodimeric
205:
203:
202:transcription
199:
195:
191:
187:
183:
179:
175:
171:
167:
162:
154:
149:
147:
145:
141:
136:
128:
123:
121:
117:
115:
114:Proteoglycans
111:
107:
103:
99:
95:
91:
83:
81:
79:
75:
71:
67:
59:
57:
55:
54:cell adhesion
51:
47:
43:
39:
30:
19:
2022:
1555:
1499:
1492:
1449:
1445:
1435:
1402:
1398:
1392:
1351:
1347:
1340:
1299:
1295:
1289:
1252:
1248:
1238:
1213:
1209:
1158:(1): 20–29.
1155:
1151:
1141:
1096:
1092:
1082:
1045:
1041:
1031:
990:
986:
976:
952:(1): 71–81.
949:
945:
935:
910:
907:Biomaterials
906:
900:
891:
845:
841:
815:(2): 69–77,
812:
808:
802:
781:cite journal
766:
721:
717:
707:
674:
670:
664:
648:. Retrieved
643:
634:
604:(1): 47–71.
601:
597:
591:
556:
552:
542:
509:
505:
495:
479:
465:Trogocytosis
422:
415:
367:
365:
332:
308:gastrulation
305:
257:
255:
225:
206:
164:
138:
118:
109:
87:
78:heterophilic
77:
73:
70:cytoskeleton
63:
41:
37:
36:
1845:Desmocollin
1354:(1): 5–18.
842:J. Cell Sci
650:October 20,
598:J Crit Care
512:: 823–862.
386:endothelial
374:fucosylated
328:R-cadherins
275:-dependent
182:vitronectin
178:fibronectin
2076:Categories
2018:L-selectin
1989:P-selectin
1984:L-selectin
1979:E-selectin
1902:T-cadherin
1823:Desmoglein
1815:Desmosomal
677:: 823–62.
644:membranome
471:References
398:P-selectin
390:L-selectin
382:E-selectin
240:fibrinogen
174:fibrinogen
74:homophilic
1971:Selectins
1788:Classical
1780:Cadherins
1684:Integrins
1615:L1 family
1466:1566-5240
1419:0952-7915
1368:1600-065X
1316:1474-1768
1172:1933-6918
1115:1664-042X
618:0883-9441
575:0092-8674
526:0066-4154
418:addressin
394:leukocyte
369:selectins
356:Selectins
259:cadherins
246:Cadherins
228:platelets
190:apoptosis
166:Integrins
155:Integrins
129:IgSF CAMs
102:Integrins
98:Cadherins
60:Structure
2024:integrin
1573:IgSF CAM
1484:19860663
1384:37831094
1332:18383054
1324:14964308
1281:24710147
1190:22647937
1133:27303307
1074:26391523
1023:24339086
1015:11884718
927:16002137
872:16988024
428:See also
402:platelet
362:Selectin
320:ectoderm
316:endoderm
312:mesoderm
301:catenins
252:Cadherin
236:collagen
232:thrombin
221:affinity
198:survival
170:collagen
161:Integrin
135:IgSF CAM
1475:2770881
1427:7917107
1376:2670744
1272:3924836
1230:1623205
1181:3364134
1124:4880553
1099:: 190.
1065:4646401
995:Bibcode
987:Science
968:7781865
863:3380273
758:6165990
726:Bibcode
699:6298053
691:9242926
626:8199653
583:8608588
534:9242926
396:), and
217:cations
46:binding
1886:PCDH19
1881:PCDH15
1752:ITGA2B
1642:Nectin
1620:L1-CAM
1610:PE-CAM
1605:VCAM-1
1507:
1482:
1472:
1464:
1425:
1417:
1382:
1374:
1366:
1330:
1322:
1314:
1279:
1269:
1228:
1188:
1178:
1170:
1131:
1121:
1113:
1072:
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1021:
1013:
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870:
860:
756:
749:319058
746:
697:
689:
624:
616:
581:
573:
532:
524:
490:(MeSH)
406:PSGL-1
378:mucins
318:, and
213:ligand
200:, and
180:, and
94:IgCAMs
2061:EpCAM
2056:CD146
2033:LFA-1
2029:VLA-4
2002:Other
1957:CDH10
1947:CDH17
1942:CDH16
1937:CDH15
1932:CDH12
1927:CDH11
1876:PCDH1
1756:ITGB3
1738:CD49d
1734:VLA-4
1724:CD11b
1710:CD11c
1696:CD11a
1692:LFA-1
1672:CD155
1667:CADM3
1662:CADM1
1657:PVRL3
1652:PVRL2
1647:PVRL1
1630:NFASC
1625:NRCAM
1581:N-CAM
1380:S2CID
1328:S2CID
1249:Genes
1019:S2CID
695:S2CID
297:actin
110:CTLDs
2051:CD44
2046:CD24
2013:CD44
1952:CDH9
1922:CDH8
1917:CDH6
1912:CDH5
1907:CDH4
1857:DSC3
1853:DSC2
1849:DSC1
1839:DSG4
1835:DSG3
1831:DSG2
1827:DSG1
1805:CDH3
1800:CDH2
1795:CDH1
1742:CD29
1728:CD18
1714:CD18
1700:CD18
1635:CHL1
1591:ICAM
1505:ISBN
1480:PMID
1462:ISSN
1423:PMID
1415:ISSN
1372:PMID
1364:ISSN
1320:PMID
1312:ISSN
1277:PMID
1226:PMID
1186:PMID
1168:ISSN
1129:PMID
1111:ISSN
1070:PMID
1011:PMID
964:PMID
923:PMID
868:PMID
794:help
754:PMID
687:PMID
652:2018
622:PMID
614:ISSN
579:PMID
571:ISSN
553:Cell
530:PMID
522:ISSN
366:The
333:The
287:and
256:The
42:CAMs
1470:PMC
1454:doi
1407:doi
1356:doi
1352:108
1304:doi
1267:PMC
1257:doi
1218:doi
1176:PMC
1160:doi
1119:PMC
1101:doi
1060:PMC
1050:doi
1046:290
1003:doi
991:296
954:doi
915:doi
858:PMC
850:doi
846:119
817:doi
744:PMC
734:doi
679:doi
656:in
606:doi
561:doi
514:doi
388:),
234:or
112:).
96:),
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339:Ca
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289:P-
285:N-
283:,
281:E-
265:Ca
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