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. 1990 Apr 1;110(4):1227–1237. doi: 10.1083/jcb.110.4.1227

EndoCAM: a novel endothelial cell-cell adhesion molecule

PMCID: PMC2116064  PMID: 2182647

Abstract

Cell-cell adhesion is controlled by many molecules found on the cell surface. In addition to the constituents of well-defined junctional structures, there are the molecules that are thought to play a role in the initial interactions of cells and that appear at precise times during development. These include the cadherins and cell adhesion molecules (CAMs). Representatives of these families of adhesion molecules have been isolated from most of the major tissues. The notable exception is the vascular endothelium. Here we report the identification of a cell surface molecule designated "endoCAM" (endothelial Cell Adhesion Molecule), which may function as an endothelial cell-cell adhesion molecule. EndoCAM is a 130-kD glycoprotein expressed on the surface of endothelial cells both in culture and in situ. It is localized to the borders of contiguous endothelial cells. It is also present on platelets and white blood cells. Antibodies against endoCAM prevent the initial formation of endothelial cell-cell contacts. Despite similarities in size and intercellular location, endoCAM does not appear to be a member of the cadherin family of adhesion receptors. The serologic and protease susceptibility characteristics of endoCAM are different from those of the known cadherins, including an endogenous endothelial cadherin. Although the precise biologic function of endoCAM has not been determined, it appears to be one of the molecules responsible for regulating endothelial cell-cell adhesion processes and may be involved in platelet and white blood cell interactions with the endothelium.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Albelda S. M., Daise M., Levine E. M., Buck C. A. Identification and characterization of cell-substratum adhesion receptors on cultured human endothelial cells. J Clin Invest. 1989 Jun;83(6):1992–2002. doi: 10.1172/JCI114109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Behrens J., Birchmeier W., Goodman S. L., Imhof B. A. Dissociation of Madin-Darby canine kidney epithelial cells by the monoclonal antibody anti-arc-1: mechanistic aspects and identification of the antigen as a component related to uvomorulin. J Cell Biol. 1985 Oct;101(4):1307–1315. doi: 10.1083/jcb.101.4.1307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bevilacqua M. P., Stengelin S., Gimbrone M. A., Jr, Seed B. Endothelial leukocyte adhesion molecule 1: an inducible receptor for neutrophils related to complement regulatory proteins and lectins. Science. 1989 Mar 3;243(4895):1160–1165. doi: 10.1126/science.2466335. [DOI] [PubMed] [Google Scholar]
  4. Bonfanti R., Furie B. C., Furie B., Wagner D. D. PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial cells. Blood. 1989 Apr;73(5):1109–1112. [PubMed] [Google Scholar]
  5. Damsky C. H., Richa J., Solter D., Knudsen K., Buck C. A. Identification and purification of a cell surface glycoprotein mediating intercellular adhesion in embryonic and adult tissue. Cell. 1983 Sep;34(2):455–466. doi: 10.1016/0092-8674(83)90379-3. [DOI] [PubMed] [Google Scholar]
  6. Dustin M. L., Springer T. A. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature. 1989 Oct 19;341(6243):619–624. doi: 10.1038/341619a0. [DOI] [PubMed] [Google Scholar]
  7. Edelman G. M. Morphoregulatory molecules. Biochemistry. 1988 May 17;27(10):3533–3543. doi: 10.1021/bi00410a001. [DOI] [PubMed] [Google Scholar]
  8. Fleming T. P., Johnson M. H. From egg to epithelium. Annu Rev Cell Biol. 1988;4:459–485. doi: 10.1146/annurev.cb.04.110188.002331. [DOI] [PubMed] [Google Scholar]
  9. Goyert S. M., Ferrero E. M., Seremetis S. V., Winchester R. J., Silver J., Mattison A. C. Biochemistry and expression of myelomonocytic antigens. J Immunol. 1986 Dec 15;137(12):3909–3914. [PubMed] [Google Scholar]
  10. Gumbiner B., Simons K. A functional assay for proteins involved in establishing an epithelial occluding barrier: identification of a uvomorulin-like polypeptide. J Cell Biol. 1986 Feb;102(2):457–468. doi: 10.1083/jcb.102.2.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gumbiner B., Stevenson B., Grimaldi A. The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J Cell Biol. 1988 Oct;107(4):1575–1587. doi: 10.1083/jcb.107.4.1575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Harlan J. M. Leukocyte-endothelial interactions. Blood. 1985 Mar;65(3):513–525. [PubMed] [Google Scholar]
  13. Hatta K., Okada T. S., Takeichi M. A monoclonal antibody disrupting calcium-dependent cell-cell adhesion of brain tissues: possible role of its target antigen in animal pattern formation. Proc Natl Acad Sci U S A. 1985 May;82(9):2789–2793. doi: 10.1073/pnas.82.9.2789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Jaffe S., Oliver P. D., Farooqui S. M., Novak P. L., Sorgente N., Kalra V. K. Separation of luminal and abluminal membrane enriched domains from cultured bovine aortic endothelial cells: monoclonal antibodies specific for endothelial cell plasma membranes. Biochim Biophys Acta. 1987 Mar 26;898(1):37–52. doi: 10.1016/0005-2736(87)90107-6. [DOI] [PubMed] [Google Scholar]
  15. Jarrell B., Levine E., Shapiro S., Williams S., Carabasi R. A., Mueller S., Thornton S. Human adult endothelial cell growth in culture. J Vasc Surg. 1984 Nov;1(6):757–764. doi: 10.1067/mva.1984.avs0010757. [DOI] [PubMed] [Google Scholar]
  16. Johnston G. I., Cook R. G., McEver R. P. Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation. Cell. 1989 Mar 24;56(6):1033–1044. doi: 10.1016/0092-8674(89)90636-3. [DOI] [PubMed] [Google Scholar]
  17. Knudsen K. A., Rao P. E., Damsky C. H., Buck C. A. Membrane glycoproteins involved in cell--substratum adhesion. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6071–6075. doi: 10.1073/pnas.78.10.6071. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  19. Larsen E., Celi A., Gilbert G. E., Furie B. C., Erban J. K., Bonfanti R., Wagner D. D., Furie B. PADGEM protein: a receptor that mediates the interaction of activated platelets with neutrophils and monocytes. Cell. 1989 Oct 20;59(2):305–312. doi: 10.1016/0092-8674(89)90292-4. [DOI] [PubMed] [Google Scholar]
  20. LeBaron R. G., Esko J. D., Woods A., Johansson S., Hök M. Adhesion of glycosaminoglycan-deficient chinese hamster ovary cell mutants to fibronectin substrata. J Cell Biol. 1988 Mar;106(3):945–952. doi: 10.1083/jcb.106.3.945. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Muller W. A., Ratti C. M., McDonnell S. L., Cohn Z. A. A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions. J Exp Med. 1989 Aug 1;170(2):399–414. doi: 10.1084/jem.170.2.399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ohto H., Maeda H., Shibata Y., Chen R. F., Ozaki Y., Higashihara M., Takeuchi A., Tohyama H. A novel leukocyte differentiation antigen: two monoclonal antibodies TM2 and TM3 define a 120-kd molecule present on neutrophils, monocytes, platelets, and activated lymphoblasts. Blood. 1985 Oct;66(4):873–881. [PubMed] [Google Scholar]
  23. Pasdar M., Nelson W. J. Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. I. Biochemical analysis. J Cell Biol. 1988 Mar;106(3):677–685. doi: 10.1083/jcb.106.3.677. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Richa J., Damsky C. H., Buck C. A., Knowles B. B., Solter D. Cell surface glycoproteins mediate compaction, trophoblast attachment, and endoderm formation during early mouse development. Dev Biol. 1985 Apr;108(2):513–521. doi: 10.1016/0012-1606(85)90054-5. [DOI] [PubMed] [Google Scholar]
  25. Rosen E. M., Mueller S. N., Noveral J. P., Levine E. M. Proliferative characteristics of clonal endothelial cell strains. J Cell Physiol. 1981 Apr;107(1):123–137. doi: 10.1002/jcp.1041070114. [DOI] [PubMed] [Google Scholar]
  26. Schneeberger E. E., Lynch R. D. Tight junctions. Their structure, composition, and function. Circ Res. 1984 Dec;55(6):723–733. doi: 10.1161/01.res.55.6.723. [DOI] [PubMed] [Google Scholar]
  27. Siegelman M. H., van de Rijn M., Weissman I. L. Mouse lymph node homing receptor cDNA clone encodes a glycoprotein revealing tandem interaction domains. Science. 1989 Mar 3;243(4895):1165–1172. doi: 10.1126/science.2646713. [DOI] [PubMed] [Google Scholar]
  28. Stoolman L. M. Adhesion molecules controlling lymphocyte migration. Cell. 1989 Mar 24;56(6):907–910. doi: 10.1016/0092-8674(89)90620-x. [DOI] [PubMed] [Google Scholar]
  29. Takeichi M. Functional correlation between cell adhesive properties and some cell surface proteins. J Cell Biol. 1977 Nov;75(2 Pt 1):464–474. doi: 10.1083/jcb.75.2.464. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Takeichi M. The cadherins: cell-cell adhesion molecules controlling animal morphogenesis. Development. 1988 Apr;102(4):639–655. doi: 10.1242/dev.102.4.639. [DOI] [PubMed] [Google Scholar]
  31. Thornton S. C., Mueller S. N., Levine E. M. Human endothelial cells: use of heparin in cloning and long-term serial cultivation. Science. 1983 Nov 11;222(4624):623–625. doi: 10.1126/science.6635659. [DOI] [PubMed] [Google Scholar]
  32. Volk T., Geiger B. A-CAM: a 135-kD receptor of intercellular adherens junctions. I. Immunoelectron microscopic localization and biochemical studies. J Cell Biol. 1986 Oct;103(4):1441–1450. doi: 10.1083/jcb.103.4.1441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. van Mourik J. A., Leeksma O. C., Reinders J. H., de Groot P. G., Zandbergen-Spaargaren J. Vascular endothelial cells synthesize a plasma membrane protein indistinguishable from the platelet membrane glycoprotein IIa. J Biol Chem. 1985 Sep 15;260(20):11300–11306. [PubMed] [Google Scholar]

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