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Original Article

The Role of Integrins in Tumorigenesis and Metastasis

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Pages 329-344 | Published online: 11 Jun 2009

References

  • Fidler G., Poste IJ. The pathogenesis of cancer metastasis. Nature 1979; 283: 139–146
  • Ruoslahti E, Giancotti FG. Integrins in tumor dissemination. Cancer Cells 1989; 1: 119–126
  • Giancotti F G, Ruoslahti E. Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell 1990; 60: 849–859
  • Chan B M, Matsuura N, Takada Y, et al. In vitro and in vivo consequences of VLA-2 expression on rahbdomyosarcoma cells. Science 1991; 251: 1600–1602
  • Vleminckx K, Vakaet L, Mareel M, et al. Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell 1991; 66: 107–119
  • Fearon E R, Cho K R, Nigro J M, et al. Identification of a chromosome 18q gene that is altered in colorectal cancers. Science 1990; 247: 49–56
  • Ellisen L W, Bird J, West D C, et al. TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell 1991; 66: 649–661
  • Ruoslahti E, Pierschbacher MD. New perspective in cell adhesion: RGD and integrins. Science 1987; 238: 491–497
  • Hynes RO. Integrins: a family of cell surface receptors. Cell 1987; 48: 459–554
  • Hemler MA. VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu Rev Immunol 1990; 8: 365–400
  • Ginsberg M H, Loftus J C, Plow EF. Cytoadhesins, integrins, and platelets. Thromb Haemost 1988; 59: 1–6
  • Burridge K, Petch L A, Romer LH. Signals from focal adhesions. Curr Biol 1992; 10: 537–539
  • Wilcox M, Leptin M. Tissue-specific modulation of a set of related cell surface antigens in Drosophila. Nature 1985; 316: 351–354
  • Giancotti F G, Comoglio P M, Tarone G. Fibronectin-plasma membrane interaction in the adhesion of hemopoietic cells. J Cell Biol 1986; 103: 429–437
  • Sutherland A E, Calarco P G, Damsky CH. Expression and function of cell surface extracellular matrix receptors in mouse blasto-cyst attachment and outgrowth. J Cell Biol 1988; 106: 1331–1348
  • Reichardt L F, Bixby J L, Hall D E, et al. Integrins and cell adhesion molecules: neuronal receptors that regulate axon growth on extracellular matrices and cell surfaces. Dev Neurosci 1989; 11: 332–337
  • Krotoski D M, Domingo C, Bronner-Fraser M. Distribution of a putative cell surface receptor for fibronectin and laminin in the avian embryo. J Cell Biol 1986; 103: 318–330
  • Suzuki S, Naitoh Y. Amino acid sequence of a novel integrin β4 subunit and primary expression of the mRNA in epithelial cells. EMBO J 1990; 9: 757–763
  • Hogervorst F, Kuikman I, Von Dem Borne A EGK, et al. Cloning and sequence analysis of β4 cDNA: an integrin subunit that contains a unique 118 kD cytoplasmic domain. EMBO J 1990; 9: 765–770
  • Tamura R N, Rozzo C, Starr L, et al. Epithelial integrin α6β4: complete primary structure of α6 and variant forms of β4. J Cell Biol 1990; 111: 1593–1604
  • Beer J, Coller BD. Evidence that platelet glycoprotein IIIa has a large disulfide-bounded loop that is susceptible to proteolytic cleavage. J Biol Chem 1989; 264: 17564–17573
  • Gailit J, Ruoslahti E. Regulation of fibronectin receptor affinity by divalent cations. J Biol Chem 1988; 263: 12927–12933
  • Kirchhofer D, Gailit J, Ruoslahti E, et al. Cation-dependent changes in the binding specificity of the platelet receptor GPIIb/IIIa. J Biol Chem 1990; 265: 18525–18530
  • Kirchhofer D, Grzesiak J, Pierschbacher MD. Calcium as a potential physiological regulator of integrin-mediated cell adhesion. J Biol Chem 1991; 266: 4471–4477
  • Carrell N A, Fitzgerald L A, Steiner B, et al. Structure of human platelet membrane glycoproteins lIb and IIIa as determined by electron microscopy. J Biol Chem 1985; 260: 1743–1749
  • Kelly T, Molony L, Burridge K. Purification of two smooth muscle glycoproteins related to integrin distribution in cultured chicken embryo fibroblasts. J Biol Chem 1987; 262: 17189–17199
  • Nermut M V, Green N M, Eason P, et al. Electron microscopy and structural model of human fibronectin receptor. EMBO J 1988; 7: 4093–4099
  • Giancotti F G, Mainiero F. Integrin-mediated adhesion and signaling in tumorigenesis. Biochem Biophys Acta Rev Cancer 1994; 1198: 47–64
  • Adams J C, Watts FM. Regulation of development and differentiation by the extracellular matrix. Development 1993; 117: 1183–1198
  • Lin C Q, Bissel MJ. Multi-faceted regulation of cell differentiation via extracellular matrix. FASEB J 1993; 7: 737–743
  • Ruoslahti E, Reed JC. Anchorage dependence, integrins and apoptosis. Cell 1994; 77: 477–478
  • Juliano R L, Haskil S. Signal transduction from the extracellular matrix. J Cell Biol 1993; 120: 577–585
  • Ginsberg M H, Du X, Plow EF. Inside-out integrin signaling. Curr Opin Cell Biol 1992; 4: 766–771
  • Dustin M L, Springer TA. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 1989; 341: 619–624
  • Staatz W D, Rajpara S M, Wayner E A, et al. The membrane glyco-protein Ia-IIa (VLA-2) complex mediates the Mg++-dependent adhesion of platelets to collagan. J Cell Biol 1989; 108: 1917–1924
  • Kirchhofer D, Languino L R, Ruoslahti E, et al. Alpha 2 beta 1 integrins from different cell types show different binding specificities. J Biol Chem 1990; 265: 615–618
  • Kieffer N, Phillips DR. Platelet membrane glycoproteins: functions in cellular interactions. Annu Rev Cell Biol 1990; 6: 329–357
  • Shimizu Y, van Seventer G, Horgan K J, et al. Regulated expression and binding of three VLA (beta 1) integrin receptors on T cells. Nature 1990; 345: 250–253
  • Phillips D R, Charo I F, Scarborough RM. GPIIb-IIIa: the responsive integrin. Cell 1991; 65: 359–362
  • Chan M B, Hemler M. Multiple functional forms of the integrin VLA-2 can be derived from a single alpha 2 cDNA clone: inter-conversion of forms induced by an anti-beta 1 antibody. J Cell Biol 1993; 120: 537–543
  • Du X P, Plow E F, Frelinger I, II, et al. Ligands ‘activate’ integrin alpha IIb beta 3 (platelet GPIIb-IIIa). Cell 1991; 65: 409–416
  • Chen W T, Hasegawa E, Hasegawa T, et al. Development of cell surface linkage complexes in cultured fibroblasts. J Cell Biol 1985; 100: 1103–1114
  • Damsky C H, Knudsen K A, Bradley D, et al. Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture. J Cell Biol 1985; 100: 1528–1539
  • Giancotti F G, Comoglio P M, Tarone G. A 135,000 molecular weight plasma membrane glycoprotein involved in fibronectin-mediated cell adhesion. Exp Cell Res 1986; 163: 47–62
  • Burridge K, Fath K, Kelly T, et al. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 1988; 4: 487–525
  • Solowska J, Guan J L, Marcantonio E E, et al. Expression of normal and mutant avian integrin subunits in rodent cells. J Cell Biol 1989; 109: 853–861
  • Hayashi Y, Haimovich B, Reszka A, et al. Expression and function of chicken integrin β1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells. J Cell Biol 1990; 110: 175–184
  • Marcantonio E E, Guan J L, Trevithick J E, et al. Mapping of the functional determinants of the integrin β1 cytoplasmic domain by site-directed mutagenesis. Cell Regul 1990; 1: 597–604
  • Solowska J, Edelman J E, Albelda S M, et al. Cytoplasmic and transmembrane domains of integrin β1 and β3 subunits are functionally interchangeable. J Cell Biol 1991; 114: 1079–1088
  • Reszka A A, Hayashi Y, Horowitz AF. Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association. J Cell Biol 1992; 117: 1321–1330
  • Horvitz A, Duggan K, Buck C A, et al. Interaction of plasma membrane fibronectin receptor with talin: a transmembrane linkage. Nature 1986; 320: 532–533
  • Otey C A, Pavalko M, Burridge K. An interaction between α-actinin and β1 integrin subunit in vitro. J Cell Biol 1990; 111: 721–729
  • Chan B MC, Kasser P D, Schiro J A, et al. Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell 1992; 68: 1051–1060
  • La Flamme S E, Akiyama S K, Yamada KM. Regulation of fibronectin receptor distribution. J Cell Biol 1992; 117: 437–447
  • Takada Y, Ylanne J, Mandelman D, et al. A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques. J Cell Biol 1992; 119: 913–921
  • Singer I I, Scott S, Kawka D W, et al. Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation. J Cell Biol 1988; 106: 2171–2182
  • Dejana E, Colella S, Conforti G, et al. Fibronectin and vitronectin regulate the organization of their respective Arg-Gly-Asp adhesion receptors in cultured human endothelial cells. J Cell Biol 1988; 100: 1215–1223
  • Carter W G, Wayner A E, Bouchard T S, et al. The role of integrins alpha 2 beta 1 and alpha 3 beta 1 in cell-cell and cell-substrate adhesion of human epidermal cells. J Cell Biol 1990; 110: 1387–1404
  • Briesewitz R, Kern A, Marcantonio EE. Ligand-dependent and-independent integrin focal contact localization: the role of the alpha chain cytoplasmic domain. Mol Biol Cell 1993; 4: 593–604
  • Ylanne J, Chen Y, O'Toole T E, et al. Distinct functions of integrin alpha and beta subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J Cell Biol 1993; 122: 223–233
  • Burridge K, Mangeat P. An interaction between vinculin and talin. Nature 1984; 308: 744–746
  • Belkin A M, Koteliansky VE. Interaction of iodinated vinculin, metavinculin and alpha-actinin with cytoskeletal proteins. FEBS Lett 1987; 220: 291–294
  • Wachsstock D H, Wilkins J A, Lin S. Specific interaction of vinculin with alpha-actinin. Biochem Biophys Res Commun 1987; 146: 554–560
  • Turner C E, Glenney J R, Burridge K. Paxillin: a new vinculin-binding protein present in focal adhesions. J Cell Biol 1990; 111: 1059–1068
  • Wilkins J A, Risinger M A, Lin S. Studies on proteins that co-purify with smooth muscle vinculin: identification of immunologically related species in focal adhesions of nonmuscle and Z-lines of muscle cells. J Cell Biol 1986; 103: 1483–1494
  • Geiger B. A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell 1979; 18: 193–205
  • Burridge K, Feramisco JR. Microinjection and localization of a 130K protein in living fibroblasts: a relationship to actin and fibronectin. Cell 1980; 19: 587–595
  • Wallraff E, Schleicher M, Modersitzki M, et al. Selection of Dictyostelium mutants defective in cytoskeletal proteins: use of an antibody that binds to the ends of alpha-actinin rods. EMBO J 1986; 5: 61–67
  • Imamura M, Endo T, Kuroda M, et al. Substructure and higher structure of chicken smooth muscle alpha-actinin molecule. J Biol Chem 1988; 263: 7800–7805
  • Podlubnaya Z A, Tskhovrebova L A, Zaalishvili M M, et al. Electron microscopic study of alpha-actinin. J Mol Biol 1975; 92: 357–359
  • Burn P, Kupper A, Singer SJ. Dynamic membrane-cytoskeletal interactions: specific association of integrin and talin arises in vivo after phorbol ester treatment of peripheral blood lymphocytes. Proc Natl Acad Sci USA 1988; 85: 497–501
  • Woods A, Couchman JR. Protein kinase C involvement in focal adhesion formation. J Cell Sci 1992; 101: 277–290
  • Ridley A J, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992; 70: 389–399
  • Dustin M L, Springer TA. T-cell receptor cross-linking transiently stimulates adhesiveness through FFAI. Nature 1989; 341: 619–624
  • Danilov Y N, Juliano RL. Phorbol ester modulation of integrin-mediated cell adhesion: a postreceptor event. J Cell Biol 1989; 108: 1925–1933
  • Wilkins J A, Stupack D, Stewart S, et al. Beta I integrin-mediated lymphocyte adherence to extracellular matrix is enhanced by phorbol ester treatment. Eur J Immunol 1991; 21: 517–522
  • Hibbs M L, Xu H, Stacker S A, et al. Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit. Science 1991; 251: 1611–1613
  • Stepp M A, Spurr-Michaud S, Tisdale A, et al. α6β4 integrin heterodimer is a component of hemidesmosomes. Proc Natl Acad Sci USA 1990; 87: 8970–8974
  • Sonnenberg A, Calafat J, Janssen H, et al. Integrin α6β4 complex is located in hemidesmosomes, suggesting a major role in epidermal cell-basement membrane adhesion. J Cell Biol 1991; 113: 907–917
  • Carter W G, Kaur P, Gil S G, et al. Distinct functions for integrins α3β3 in focal adhesions and α6β4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes. J Cell Biol 1990; 111: 3141–3154
  • Spinardi L, Ren Y L, Sanders R, et al. The β4 subunit cytoplasmic domain mediates the interaction of α6β4 integrin with the cytoskeleton of hemidesmosomes. Mol Biol Cell 1993; 4: 871–884
  • Giudice G J, Emery D J, Diaz LA. Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180. J Invest Dermatol 1992; 99: 243–250
  • Westgate G E, Weaver A C, Couchman JR. Bullous pemphigoid antigen localization suggests an intracellular association with hemidesmosomes. J Invest Dermatol 1985; 84: 218–224
  • Sawamura D, Li K, Chu M L, et al. Human bullous pemphigoid antigen (BPAG1). J Biol Chem 1991; 266: 17784–17790
  • Tanaka T, Parry D AD, Klaus-Kovtun V, et al. Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin 1 confirms that they define a new family of cell adhesion junction plaque proteins. J Biol Chem 1991; 266: 12555–12559
  • Comoglio P M, Di Renzo M F, Tarone G, et al. Detection of phos-photyrosine-containing proteins in the detergent-insoluble fraction of RSV-transformed fibroblasts by azobenzene phosphonate antibodies. EMBO J 1984; 3: 483–489
  • Maher P A, Pasquale E B, Wang J YJ, et al. Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc Natl Acad Sci USA 1985; 82: 6576–6580
  • Burridge K, Turner C E, Romer LH. Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J Cell Biol 1992; 119: 893–903
  • Birge R B, Fajardo J E, Reichman C, et al. Identification and characterization of a high affinity interaction between v-crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol Cell Biol 1993; 13: 4648–4656
  • Hempstead B L, Birge R B, Fajardo J E, et al. Expression of the v-crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor- and epidermal growth factor-dependent pathways. Mol Biol Cell 1994; 14: 1964–1971
  • Guan J, Trevithick J E, Hynes RO. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Regul 1991; 2: 951–964
  • Kornberg L J, Earp H S, Turner C E, et al. Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of β1 integrins. Proc Natl Acad Sci USA 1991; 88: 8392–8396
  • Kanner S B, Reynolds A B, Vines R R, et al. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 1990; 87: 3328–3332
  • Shalloway D, Guan J. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 1992; 358: 690–692
  • Shaller M D, Borgman C A, Cobb B S, et al. pp125FAK, a structurally distinctive protein tyrosine-kinase associated with focal adhesions. Proc Natl Acad Sci USA 1992; 89: 5192–5196
  • Hanks S K, Calab M B, Harper M C, et al. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci USA 1992; 89: 8487–8491
  • Zachary I, Sinnet-Smith J, Rozengurt E. Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. J Biol Chem 1992; 267: 19031–19034
  • Huang M, Bolen J B, Barnwell J W, et al. Membrane glycoprotein IV (CD36) is physically associated with Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets. Proc Natl Acad Sci USA 1991; 88: 7844–7848
  • Symington BE. Fibronectin receptor modulates cyclin-dependent kinase activity. J Biol Chem 1992; 267: 25744–25747
  • Guadagno T M, Assoian RK. G1/S control of anchorage-independent growth in the fibroblast cell cycle. J Cell Biol 1991; 115: 1419–1425
  • Kyu-Ho Han E, Guadagno T M, Dalton R K, et al. A cell cycle and mutational analysis of anchorage-independent growth: cell adhesion and TGF-β1 control G1/S transit specifically. J Cell Biol 1993; 122: 461–471
  • Guadagno T M, Ohtsubo M, Roberts J M, et al. A link between cyclin A expression and adhesion-dependent cell cycle progression. Science 1993; 262: 1572–1575
  • Dike L E, Farmer SR. Cell adhesion induces expression of growth-associated genes in suspension-arrested fibroblasts. Proc Natl Acad Sci USA 1988; 85: 6792–6796
  • Wary K K, Mainiero F, Isakoff S J, et al. The adaptor protein she couples a class of integrins to the control of cell cycle progression. Cell 1996; 87: 733–743
  • Mainiero F, Pepe A, Wary K K, et al. Signal transduction by the α6β4 integrin: distinct β4 subunit sites mediate recruitment of she /Grb2 and association with the cytoskeleton of hemidesmo-somes. EMBO J 1995; 14: 4470–4481
  • Mainiero F, Murgia C, Wary K K, et al. The coupling of α6β4 integrin to ras-MAP kinase pathways mediated by she controls keratinocyte proliferation. EMBO J 1997; 9: 2365–2375
  • Mainiero F, Pepe A, Yeon M, et al. The intracellular functions of α6β4 integrin are regulated by EGF. J Cell Biol 1996; 134: 241–253
  • Spinardi L, Einheber S, Cullen T, et al. A recombinant tail-less integrin β4 subunit disrupts hemidesmosomes, but does not suppress α6β4-mediated cell adhesion to laminins. J Cell Biol 1995; 129: 473–487
  • Schultz G, Rotatori D S, Clark W. EGF and TGF-alpha in wound healing and repair. J Cell Biochem 1991; 45: 346–352
  • Gipson I K, Spurr-Michaud S, Tisdale A, et al. Redistribution of the hemidesmosome components alpha 6 beta 4 integrin and bullous pemphigoid antigens during epithelial wound healing. Exp Cell Res 1993; 207: 86–98
  • Ozanne B, Richards C S, Hendler F, et al. Overexpression of the EGF receptor is a hallmark of squamous cell carcinoma. J Pathol 1986; 149: 9–14
  • Pellegrini G, De Luca M, Orecchia G, et al. Expression, topography, and function of integrin receptors are severely altered in keratinocytes from involved and uninvolved psoriatic skin. J Clin Invest 1992; 89: 1783–1795
  • Schwartz M A, Lechene C, Ingber DE. Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin α5β1, independent of cell shape. Proc Natl Acad Sci USA 1991; 88: 7849–7853
  • Richter J, Ng-Sikorski J, Olsson I, et al. Tumor necrosis factor-induced degranulation in adherent human neutrophils is dependent on CD1 1b/CD18-integrin-triggered oscillations of cytosolic free Ca2+. Proc Natl Acad Sci USA 1990; 87: 9472–9476
  • Sadler I, Crawford A W, Michelsen J W, et al. Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton. J Cell Biol 1992; 119: 1573–1587
  • Spooner B S, Wessells NK. Mammalian lung development: interactions in primordium formation and bronchial morphogenesis. J Exp Zool 1970; 175: 445–454
  • Wessells NK. Mammalian lung development: interactions in formation and morphogenesis of trachael buds. J Exp Zool 1970; 175: 455–466
  • Schuger L, O'Shea S, Rheinheimer J, et al. Laminin in lung development: effects of anti-laminin antibody in murine lung morphogenesis. Dev Biol 1990; 137: 26–32
  • Roman J, Little C W, McDonald JA. Potential role of RGD-binding integrins in mammalian lung branching morphogenesis. Development 1991; 112: 551–558
  • Talhouk R S, Chin J R, Unemori E N, et al. Proteinases of the mammary gland: developmental regulation in vivo and vectorial secretion in culture. Development 1991; 112: 439–449
  • Streuli C H, Bailey N, Bissell MJ. Control of mammary epithelial differentiation: basement membrane induces tissue-specific gene expression in the absence of cell-cell interaction and morphological polarity. J Cell Biol 1991; 115: 1383–1395
  • Haskill S, Johnson C, Eierman D, et al. Adherence induces selective mRNA expression of monocyte mediators and proto-oncogenes. J Immunol 1988; 140: 1690–1694
  • Haskill S, Beg A A, Tomkins SM, et al. Characterization of an immediate-early gene induced in adherent monocytes that encode I kappa β-like activity. Cell 1991; 65: 1281–1289
  • Shaw R J, Doherty D E, Ritter A G, et al. Adherence-dependent increase in human monocyte PDGF(B) mRNA is associated with increase in c-fos, c-jun, EGFR2 mRNA. J Cell Biol 1990; 111: 2139–2148
  • Spom S A, Eierman D F, Johnson C E, et al. Monocyte adherence results in selective induction of novel genes sharing homology with mediators of inflammation and tissue repair. J Immunol 1990; 144: 4434–4441
  • Griffin G E, Leung K, Folks T M, et al. Activation of HIV gene expression during monocyte differentiation by induction of NF-kB. Nature 1989; 339: 70–73
  • Pullan S, Wilson J, Metcalf A, et al. Requirement for basement membrane for the suppression of programmed cell death in mammary epithelium. J Cell Sci 1996; 109: 631–642
  • Adams J C, Watt FM. Regulation of development and differentiation by the extracellular matrix. Development 1993; 117: 1183–1198
  • Carreiras F, Denoux Y, Staedel C, et al. Expression and localization of alpha v integrins and their ligand vitronectin in normal ovarian epithelium and in ovarian carcinomas. Gynecol Oncol 1996; 62: 260–267
  • Valea F A, Haskill S, Moore D H, et al. Immunohistochemical analysis of alpha 1-integrins in cervical cancer. Am J Obstet Gynecol 1995; 173: 808–813
  • Natali P G, Nicotra M R, Botti C, et al. Changes in expression of α6/β4 integrin heterodimer in primary and metastatic breast cancer. Br J Cancer 1992; 66: 318–322
  • Zutter M M, Mazoujian G, Santoro SA. Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast. Am J Pathol 1990; 137: 863–870
  • Koukoulis G K, Virtanen I, Korhonen M, et al. Immunohistochemical localization of integrins in normal, hyperplastic, and neoplastic breast. Am J Pathol 1991; 139: 787–799
  • Damjanovich L, Albelda S M, Mette S A, et al. Distribution of integrin cell adhesion receptors in normal and malignant lung tissue. Am J Respir Cell Mol Biol 1992; 6: 197–206
  • Koretz K, Schlag P, Boumsell L, et al. Expression of VLA-α2, VLA-α6, and VLA-β1 chains in normal mucosa and adenomas of the colon, and in colon carcinomas and their metastases. Am J Pathol 1991; 138: 741–750
  • Cress A E, Rabinovitz I, Zhu W, et al. The alpha 6 beta 1 and alpha 6 beta 4 integrins in human prostate cancer progression. Cancer Metastasis Rev 1995; 14: 219–228
  • Lessey B A, Albelda S, Buck C A, et al. Distribution of integrin cell adhesion molecules in endometrial cancer. Am J Pathol 1995; 146: 717–726
  • Gladson C L, Cheresh DA. Glioblastoma expression of vitronectin and the αvβ3 integrin. J Clin Invest 1991; 88: 1924–1932
  • Albelda S M, Mette S A, Elder D E, et al. Integrin distribution in malignant melanoma: association of the β3 subunit with tumor progression. Cancer Res 1990; 50: 6757–6764
  • Felding-Habermann B, Mueller B M, Romerdahl C A, et al. Involvement of integrin alpha v gene expression in human melanoma tumorigenicity. J Clin Invest 1992; 89: 2018–2022
  • Zambonin-Zallone A, Teti A, Grano M, et al. Immuno-cytochemical distribution of extracellular matrix receptors in human osteoclasts: a β3 integrin is colocalized with vinculin and talin in the podosomes of osteocloma giant cells. Exp Cell Res 1989; 182: 645–652
  • Chen W T, Olden K, Bernard B A, et al. Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J Cell Biol 1984; 98: 1546–1555
  • David-Pfeuty T, Singer SJ. Altered distribution of the cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 1980; 77: 6687–6691
  • Marchisio P C, Cirillo D, Teti A, et al. Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfila-ment-membrane interactions. Exp Cell Res 1987; 169: 202–214
  • Marchisio P C, Cirillo D, Naldini L, et al. Cell-substratum interaction of cultured avian osteoclasts is mediated by specific adhesion structures. J Cell Biol 1984; 99: 1696–1705
  • Tarone G, Cirillo D, Giancotti F G, et al. Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of theventral membrane called podosomes. Exp Cell Res 1985; 159: 141–157
  • Liebert M, Washington R, Stein J, et al. Expression of the VLA beta 1 integrin family in bladder cancer. Am J Pathol 1994; 144: 1016–1022
  • Paulus W, Baur I, Schuppan D, et al. Characterization of integrin receptors in normal and neoplastic human brain. Am J Pathol 1993; 143: 154–163
  • Jaskiewicz K, Chasen M R, Robson SC. Differential expression of extracellular matrix proteins and integrins in hepatocellular carcinoma and chronic liver disease. Anticancer Res 1993; 13: 2229–2237
  • Suzuki S, Takahashi T, Nakamura S, et al. Alterations of integrin expression in human lung cancer. Jpn J Cancer Res 1993; 84: 168–174
  • Inghirami G, Grignani F, Sternas L, et al. Down-regulation of LFA-1 adhesion receptors by c-myc oncogene in human B lymphoblastoid cells. Science 1990; 250: 682–686
  • Natali P G, Nicotra M R, Bartolazzi A, et al. Integrin expression in cutaneous malignant melanoma association of the alpha 3/β1 heterodimer with tumor progression. Int J Cancer 1993; 54: 68–72
  • Kramer R H, Vu M P, Cheng Y F, et al. Laminin-binding integrin alpha 7 beta 1: functional characterization and expression in normal and malignant melanocytes. Cell Regul 1991; 2: 805–817
  • Wienel R J, Rosendhal A, Neumann K, et al. Expression and function of VLA-α2, -α3, -α5, and -CC6integrin receptors in pancreatic carcinoma. Int J Cancer 1992; 52: 827–833
  • Peltonen J, Larjava H, Jaakkola S, et al. Localization of integrin receptors for fibronectin, collagen, and lamimn in human skin. Variable expression in basal and squamous cell carcinomas. J Clin Invest 1989; 84: 1916–1923
  • Savoia P, Trusolino L, Pepino E, et al. Expression and topography of integrins and basement membrane proteins in epidermal carcinomas: basal but not squamous cell carcinomas display loss of α6β4 and BM-600/nicein. J Invest Dermatol 1993; 101: 352–358
  • van Waes C, Carey TE. Overexpression of the A9 antigen/α6β4 integrin in head and neck cancer. Otolaryngol Clin North Am 1992; 25: 1117–1139
  • Ruoslahti E. Fibronectin in cell adhesion and invasion. Cancer Metastasis Rev 1984; 3: 34–51
  • Hayman E G, Engvall E, Ruoslahti E. Concomitant loss of fibronectin and laminin from transformed rat kidney cells. J Cell Biol 1981; 88: 352–357
  • Chen W T, Wang T, Hasegawa S S, et al. Regulation of fibronectin receptor distribution by transformation, exogenous fibronectin, and synthetic peptides. J Cell Biol 1986; 103: 1649–1661
  • Plantefaber L C, Hynes RO. Changes in integrin receptors on oncogenically transformed cells. Cell 1989; 56: 281–290
  • Ali I U, Hynes RO. Effects of LETS glycoprotein on cell motility. Cell 1978; 14: 439–446
  • Couchman J R, Rees D A, Green M R, et al. Fibronectin has a dual role in locomotion and anchorage of primary chick fibroblasts and can promote entry into the division cycle. J Cell Biol 1982; 93: 402–410
  • Rovasio R A, Delouvee A, Yamada K M, et al. Neural crest cell migration: requirements for exogenous fibronectin and high cell density. J Cell Biol 1983; 96: 462–473
  • McCarthy J B, Furcht LT. Laminin and fibronectin promote the hepatic migration of B16 mouse melanoma cells in vitro. J Cell Biol 1984; 98: 1474–1480
  • Symington BE. Fibronectin receptor overexpression and loss of transformed phenotype in a stable variant of the K562 cell line. Cell Regul 1990; 1: 637–648
  • Pasquale E B, Maher P A, Singer SJ. Talin is phosphorylated on tyrosine in chicken embryo fibroblasts transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 1986; 83: 5507–5511
  • Sefton B M, Hunter T, Ball E H, et al. Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell 1981; 24: 165–174
  • Raz A, Zoller M, Ben-Ze'ev A. Cell configuration and adhesive properties of metastasizing and non-metastasizing Bsp73 rat ade-nocarcinoma cells. Exp Cell Res 1986; 162: 127–141
  • Gluck U, Kwiatkowski D J, Ben-Ze'ev A. Suppression of tumorigenicity in simian virus 40-transformed 3T3 cells tranafected with alpha-actinin cDNA. Proc Natl Acad Sci USA 1993; 90: 383–387
  • Fernandez J LR, Geiger B, Salomon D, et al. Suppression of vinculin expression by antisense transfection confers changes in cell morphology, motility, and anchorage-dependent growth of 3T3 cells. J Cell Biol 1993; 122: 1285–1294
  • Liotta L A, Rao C N, Weiner WM. Biochemical interactions of tumor cells with the basement membrane. Annu Rev Biochem 1986; 55: 1037–1055
  • Peterson O W, Ronnov-Jessen L, Howlett A R, et al. Interaction with basement membrane serves to rapidly distinguish growth and differentiation pattern of normal and malignant human breast epithelial cells. Proc Natl Acad Sci USA 1992; 89: 9064–9068
  • Hewlett A R, Bailey N, Damsky C, et al. Cellular growth and survival are mediated by β1 integrins in normal human breast epithelium but not in breast carcinoma. J Cell Sci 1995; 108: 1945–1957
  • Navarro P, Gomez M, Pizarro A, et al. A role for the E-cadherin cell-cell adhesion molecule during tumor progression of mouse epidermal carcinogenesis. J Cell Biol 1991; 115: 517–533
  • Diaz-Guerra M, Haddow S, Bauluz C, et al. Expression of simple epithelial cytokeratins in mouse epidermal keratinocytes harboring Harvey ras gene alterations. Cancer Res 1992; 52: 680–687
  • McNutt NS. Ultrastructural comparison of the interface between epithelium and stroma in basal cell carcinoma and control human skin. Lab Invest 1976; 35: 132–142
  • Jones J CR, Steinman H K, Goldsmith BA. Hemidesmosomes, collagen VII, and intermediate filaments in basal cell carcinoma. J Invest Dermatol 1989; 93: 662–671
  • Kimmel K A, Carey TE. Altered expression in squamous carcinoma cells of an orientation restricted epithelial antigen detected by monoclonal antibody A9. Cancer Res 1986; 46: 3614–3623
  • Folkman J, Klagsbrun M. Angiogenic factors. Science 1987; 235: 442–447
  • Brooks P C, Clark R AF, Cheresh DA. Requirement for vascular integrin αvβ3 for angiogenesis. Science 1994; 264: 569–571
  • Brooks P C, Montgomery A MP, Rosenfeld M, et al. Integrin αvβ3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 1994; 79: 1157–1164
  • Swerlick S A, Brown E J, Xu Y, et al. Expression and modulation of the vitronectin receptor on human dermal microvascular endothelial cells. J Invest Dermatol 1992; 99: 715–722
  • Enenstein J, Walsh N S, Kramer RH. Basic FGF and TGF-β differentially modulate integrin expression of human microvascular endothelial cells. Exp Cell Res 1992; 203: 499–503
  • Klein S, Giancotti F G, Presta M, et al. Basic fibroblast growth factor modulates integrin expression in microvascular endothelial cells. Mol Biol Cell 1993; 4: 973–982
  • Albelda S M, Daise M, Levine E M, et al. Identification and characterization of cell-substratum adhesion receptors on cultured human endothelial cells. J Clin Invest 1989; 83: 1992–2002
  • Barth T, Hartschuh W, et al. In situ expression of β1, β3, and β4 integrin subunits in non-neoplastic endothelium and vascular tumors. Virchows Arch 1994; 425: 375–384, Mechtersheimer β4
  • Vijaya Mohan Rao L. Tissue factor as a tumor procoagulant. Cancer Metastasis Rev 1992; 11: 249–266
  • Karpatkin S, Pearlstein E, Ambrogio C, et al. Role of adhesive proteins on platelet tumor interaction in vitro and metastasis formation in vivo. J Clin Invest 1988; 81: 1012–1019
  • Gawaz M P, Loftus J, Bajt M L, et al. Ligand binding mediates integrin alpha lib beta 3 (platelet GPUb-IIIa) dependent homo-typic and heterotypic cell-cell interactions. J Clin Invest 1991; 88: 1128–1134
  • Boukerche H, Berthier-Vergnes O, Bailly M, et al. A monoclonal antibody (LYP18) directed against the blood platelet glycoprotein IIb/IIIa complex inhibits human melanoma growth in vivo. Blood 1989; 74: 909–912
  • Honn K V, Cicone B, Skoff A. Prostacyclin: a potent antimetastatic agent. Science 1981; 212: 1270–1272
  • Humphries M J, Olden K, Yamada KM. A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells. Science 1986; 233: 467–470
  • Altieri DC. Coagulation assembly on leukocytes in transmembrane signaling and cell adhesion. Blood 1993; 81: 569–579
  • Altieri D C, Bader R, Mannucci P M, et al. Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen. J Cell Biol 1988; 107: 1893–1900
  • Wright S D, Weitz J I, Huang A J, et al. Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen. Proc Natl Acad Sci USA 1988; 85: 7734–7738
  • Lasky L. Selectins: interpreters of cell-specific carbohydrate information during inflammation. Science 1992; 258: 964–969
  • Roossien F F, de Rijk D, Bikker A, et al. Involvement of LFA-1 in lymphoma invasion and metastasis demonstrated with LFA-1 deficient mutants. J Cell Biol 1989; 108: 1979–1985
  • Martin-Padura I, Mortarini R, Lauri D, et al. Hetergeneity in human melanoma cell adhesion to cytokine activated endothelial cell correlates with VLA-4 expression. Cancer Res 1991; 51: 2239–2241
  • Alby L, Auerbach R. Differential adhesion of tumor cells to capillary endothelial cells in vitro. Proc Natl Acad Sci USA 1984; 81: 5739–5743
  • Ruiz P, Dunon D, Sonnenberg A, et al. Suppression of mouse melanoma metastasis by EA-1, a monoclonal antibody specific for α6 integrins. Cell Adhes Commun 1993; 1: 67–81
  • Gardner M J, Jones L M, Catterall J B, et al. Expression of cell adhesion molecules on ovarian tumor cell lines and mesothelial cells, in relation to ovarian cancer metastasis. Cancer Lett 1995; 91: 229–234

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