Summary
Human melanoma represents one of the most metastatic cancers in man. The capacity of melanoma cells to invade a variety of tissues and extracellular matrices is, in part, due to their repertoire of adhesion receptors. To this end, human melanoma cells express multiple integrin cell adhesion receptors among these is the vitronectin receptor, αvβ3. This adhesion receptor enables melanoma cells to attach to a wide variety of extracellular matrix components containing the sequence Arg-Gly-Asp. This review will focus on the biosynthetic, biochemical and biological properties of this receptor expressed on the surface of human melanoma cells.
Similar content being viewed by others
References
Hynes, RO: Integrins: a family of cell surface receptors. Cell 48: 549–554, 1987
Chen, WT, Hasegawa, T, Hasegawa, C, Weinstock, C, Yamada, KM: Development of cell surface lineage complexes in cultivated fibroblasts. J Cell Biol 100: 1103–1114, 1985
Damsky, CM, Knudsen, KA, Bradley, D, Buck, CA, Horwitz, A: Distribution of the CSAT cell-matrix antigen on myogenic and fibroblastic cells in culture. J Cell Biol 100: 1528–1539, 1985
Burridge, K, Fath, K, Kelly, T, Nuckolls, G, Turner, C: Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 4: 487–525, 1988
Dejanna, E, Colella, S, Conforti, G, Abbadini, M, Gaboli, M, Marchisio, PC: Fibronectin and vitronectin regulate the organization of their respective Arg-Gly-Asp adhesion receptors in cultured human endothelial cells. J Cell Biol 107: 1215–1223, 1988
Singer, II, Scott, S, Kawka, DW, Kazazis, DM, Gailit, J, Rouslahti, E: Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation. J Cell Biol 106: 2171–2182, 1988
Carter, WG, Wayner, EA, Bouchard, TS, Kaur, P: The role of integrins α3β1 and α3β1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 110: 1387–1404, 1990
Geiger, B: A 130-K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells. Cell 18: 193–205, 1979
Horwitz, A, Duggan, K, Buck, CA, Beckerle, MC, Burridge, K: Interaction of plasma membrane fibronectin receptor with talin—a transmembrane linkage. Nature (Lond) 320: 531–533, 1986
Tapley, P, Horwitz, AF, Buck, CA, Burridge, K, Duggan, K, Hirst, R, Rohrschneider, L: Analysis of the avian fibronectin receptor (integrin) as direct substrate for pp60 v-src. Oncogene 4: 325–333, 1989
Nuckolls, GH, Turner, CE, Burridge, K: Functional studies of the domains of talin. J Cell Biol 110: 1635–1644, 1990
Otey, CA, Pavalko, FM, Burridge, K: An interaction between α-actinin and the β1 integrin subunit in vitro. J Cell Biol 111: 721–729, 1990
Cheresh, DA, Spiro, RC: Biosynthetic and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma cell attachment to vitronectin, fibrinogen and von Willebrand factor. J Biol Chem 262: 17703–17711, 1987
Cheresh, DA: Human endothelial cells synthesize and express an Arg-Gly-Asp-directed receptor involved in attachment to fibrinogen and von Willebrand factor. Proc Natl Acad Sci USA 84: 6471–6475, 1987
Lawler, J, Weinstein, R, Hynes, RO: Cell attachment to thrombospondin: the role of RGD and integrin receptors. J Cell Biol 107: 2351–2361, 1988
Reinholt, FP, Hultenby, K, Oldberg, A, Heinegard, D: Osteopontin—a possible anchor of osteoclasts to bone. Proc Natl Acad Sci USA 87: 4473–4475, 1990
Charo, IF, Nannizzi, L, Smith, JW, Cheresh, DA: The vitronectin receptor α5β1 binds fibronectin and acts in concert with αvβ3 in promoting cellular attachment and spreading on fibronectin. J Cell Biol 111: 2795–2800, 1991
Kramer, RH, Cheng, Y-F, Clyman, R: Human microvascular endothelial cells use β1 and β3 integrin receptor complexes to attach to laminin. J Cell Biol 111: 1223–1243, 1990
Cheresh, DA, Berliner, SA, Vicente, C, Ruggeri, ZM: Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells. Cell 58: 945–953, 1989
Smith, JW, Ruggeri, ZM, Kunicki, TJ, Cheresh, DA: Interaction of Integrins αvβ3 and glycoprotein IIb–IIIa with fibrinogen. Differential peptide recognition accounts for distinct binding sites. J Biol Chem 265: 12267–12271, 1990
Albeda SM, Mette SA, Elder DE, Stewart R, Damjanovich L, Herlyn M, Buck CA: Integrin distribution in malignant melanoma: Association of the β3 subunit with tumor progression. Cancer Res 1990
Bodary, SC, McClean, JW: The integrin β1 subunit associates with the vitronectin receptor 10–4 subunit to form a novel vitronectin receptor in a human embryonic kidney cell line. J Biol Chem 265: 5938–5941, 1990
Vogel, BE, Tarone, G, Giancotti, FG, Gailit, J, Ruoslahti, E: A novel fibronectin receptor with an unexpected subunit composition αvβ1. J Biol Chem 265: 5934–5937, 1990
Cheresh, DA, Smith, JW, Cooper, HM, Quaranta, V: A novel vitronectin receptor integrin αvβx is responsible for distinct adhesive properties of carcinoma cells. Cell 57: 59–69, 1989
Smith, JW, Vestal, DJ, Irwin, SV, Burke, T, Cheresh, DA: Purification and functional characterization of integrin αvβ5: An adhesion receptor for vitronectin. J Biol Chem 256: 11008–11013, 1990
Ramaswamy, Hemler, ME: Cloning, primary structure and properties of a novel human integrin β subunit. EMBO J 9: 1561–1568, 1990
McClean, JW, Vestal, DJ, Cheresh, DA, Bodary, SC: cDNA sequence of the human integrin β5 subunit. J Biol Chem 265: 17126–17131, 1990
Boukerche, H, Berthier-Vergnes, O, Bailly, M, Dore, JF, Leung, LK, McGregor, JL: A monoclonal antibody (LYP18) directed against the blood platelet glycoprotein IIb/IIIa complex inhibits human melanoma growth in vivo. Blood 74: 909–912, 1989
Gehlson, KR, Argraves, WS, Pierschbacher, MD, Ruoslahti, E: Inhibition of in vitro tumor invasion by Arg-Gly-Asp-containing peptides. J Cell Biol 106: 925–930, 1988
Humphries, MJ, Olden, K, Yamada, KM: A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells. Science 233: 467–470, 1986
Saiki, I, Murata, J, Lida, J, Nishi, N, Sugimura, K, Azuma, I: The inhibition of murine lung metastasis by synthetic polypeptides [poly (RGD) and poly (YIGSR)] with a core sequence of cell adhesion molecules. Br J Cancer 59: 194–197, 1988
Humphries, MJ, Yamada, KM, Olden, K: Investigation of the biological effects of the anti-cell adhesion synthetic peptides that inhibit experimental metastasis of B16-F10 murine melanoma cells. J Clin Invest 81: 782–790, 1988
Cheresh, DA, Harper, JA: Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130 kDa α-subunit. J Biol Chem 262: 1434–1437, 1987
Smith, JW, Cheresh, DA: The RGD binding domain of the vitronectin receptor: Photoaffinity crosslinking implicates residues 61–203 of the β subunit. J Biol Chem 263: 18726–18731, 1988
Smith, JW, Cheresh, DA: Integrin αvβ3-ligand interaction: Identification of a divalent cation-dependent, heterodimeric RGD binding site on the vitronectin receptor. J Biol Chem 256: 2168–2172, 1990
D'Souza, SE, Ginsberg, MH, Lam, S, Plow, E: Chemical crosslinking of arginyl-glycyl-aspartic acid peptides on adhesion receptors on platelets. Science 242: 91–93, 1988
Cheresh, DA, Pierschbacher, MD, Herzig, MA, Mujoo, K: Disialogangliosides GD2 and GD3 are involved in the attachment of human melanoma and neuroblastoma cells to extracellular matrix proteins. J Cell Biol 102: 688–696, 1986
Cheresh, DA, Klier, FG: Disialoganglioside GD2 distributes preferentially into substrate-associated microprocesses on human melanoma cells during their attachment to fibronectin. J Cell Biol 102: 1887–1897, 1986
Cheresh, DA, Pytela, R, Klier, FG, Pierschbacher, MD, Ruoslahti, E, Reisfeld, RA: An Arg-Gly-Asp-directed receptor on the surface of human melanoma cells exists in a functional complex with the disialoganglioside GD2. J Cell Biol 105: 1163–1173, 1987
Stallcup, WB: Involvement of gangliosides and glycoprotein fibronectin receptors in cellular adhesion to fibronectin. Exp Cell Res 177: 90–102, 1988
Conforti, G, Zanetti, A, Pasquali-Ronchetti, I, Quaglino, D, Neyroz, P, Dejanna, E: Modulation of vitronectin receptor binding by membrane lipid composition. J Biol Chem 265: 4011–4019, 1990
Brown E, Hooper L, Ho T, Gresham H: Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins. J Cell Biol 1990, in press
Wayner EA, Orlando RA, Cheresh DA: Integrins αvβ3 and αvβ5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface. J Cell Biol 1991, in press
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Cheresh, D.A. Structure, function and biological properties of integrin αvβ3on human melanoma cells. Cancer Metast Rev 10, 3–10 (1991). https://doi.org/10.1007/BF00046839
Issue Date:
DOI: https://doi.org/10.1007/BF00046839