Skip to main content
SpringerLink
Log in

The role of cell adhesion proteins—laminin and fibronectin—in the movement of malignant and metastatic cells

  • Published:
Cancer and Metastasis Reviews Aims and scope Submit manuscript

Summary

Metastasizing tumor cells must traverse diverse extracellular matrices during dissemination. Extracellular matrices consist of two basic types, interstitial stroma and basement membranes. Extracellular matrices are chemically complex structures that interact with cell surfaces by a number of mechanisms. There has been a great deal of effort in recent years to understand the molecular nature of extracellular matrices, especially as it relates to the adhesion of normal and malignant cell types. Adhesive noncollagenous glycoproteins, such as laminin and fibronectin, serve pivotal roles in basement membrane and stromal matrices, respectively. These proteins participate in establishing the architecture of extracellular matrices as well as in attaching to the surface of cells and affecting cellular phenotype. This phenotypic effect ranges from adhesion and motility to growth and differentiation. Changes in adhesive characteristics and motility of cells have long been suspected to play a role in mediating the spread of malignant neoplasms. This article is designed to review extracellular matrix constituents that are currently known that can mediate the adhesion and motility of malignant neoplasms. The adhesion of normal and malignant cells to matrices is a complex process mediated by several distinct mechanisms which are initially manifested by changes in cytoskeletal architecture. The topic of normal and malignant cell adhesion to matrices will also be discussed in this regard, since any explanation of tumor cell migration must account for the complex dynamic interactions of the cell surface with the substratum as well as with the cytoskeleton. Finally, current efforts designed to understant the molecular nature of tumor cell:matrix interactions that contribute to metastatic behavior will also be discussed. The rationale behind these studies is that selective inhibition of specific tumor:extracellular matrix interactions can provide an avenue for therapeutic intervention of metastatic cancer.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Nicolson GL, Poste G: Tumor implantation and invasion at metastatic sites. Int Rev Exp Path 25: 78–181, 1984.

    Google Scholar 

  2. Hart IR, Fidler IJ: The implications of tumor heterogeneity for studies on the biology and therapy of cancer metastasis. Biochimica et Biophysica Acta 651: 37–50, 1981.

    Google Scholar 

  3. Weiss L: Overview of the metastatic cascade In: Honn KV, and Sloane BF (eds) Homeostatic Mechanisms and Metastasis. Martinus Nijhoff, Boston, 1984, pp 15–38.

    Google Scholar 

  4. Coman DR: Decreased mutual adhesiveness, a property of cells from squamous cell carcinomas. Cancer Res 4: 625–629, 1944.

    Google Scholar 

  5. Pauli BU, Schwarz DE, Thonar EJ-M, Kuettner KE: Tumor invasion and host extracellular matrix. Cancer Met Rev 2: 129–152, 1983.

    Google Scholar 

  6. Weiss L, PMWard: Cell detachment and metastasis. Cancer Met Rev 2: 111–123, 1983.

    Google Scholar 

  7. Carter SB: Principles of cell motility: the direction of cell movement and cancer invasion. Nature (Lond) 208: 1183–1187, 1965.

    Google Scholar 

  8. Varani J; Chemotaxis of metastatic tumor cells. Cancer Met Rev 1: 17–28, 1982.

    Google Scholar 

  9. Suh O, Weiss L: The development of a technique for the morphometric analysis of invasion in cancer. J Theor Biol 107: 547–561, 1984.

    Google Scholar 

  10. Strauli P, Haemmerli G: The role of cell motility in invasion. Cancer Met Rev 3: 127–141, 1984.

    Google Scholar 

  11. WoodJr S: Pathogenesis of metastasis formation observed in vivo in the rabbit ear chamber. Arch Path 66: 550–568, 1958.

    Google Scholar 

  12. Yamada KM: Cell surface interactions with extracellular matrix materials. Ann Rev Biochem 52: 761–799, 1983.

    Google Scholar 

  13. Hay ED: Cell biology of extracellular matrix. Plenum Press, New York, 1982.

    Google Scholar 

  14. Kleinman HK, Klebe RJ, Martin GR: Role of collagenous matrices in the adhesion and growth of cells. J Cell Biol 88: 473–486, 1981.

    Google Scholar 

  15. Furcht LT: Structure and function of the adhesive glycoprotein fibronectin. Mod Cell Biol 1: 53–117, 1983.

    Google Scholar 

  16. Hawkes S, Wang JL (eds): Extracellular Matrix. Academic Press, New York, 1982.

    Google Scholar 

  17. Trinkhaus JP: Cells Into Organs. Prentice-Hall, Englewood Cliff, NJ, 1984.

    Google Scholar 

  18. Kuhn K: Chemical properties of collagen. In: Furthmayr H (ed) Immunochemistry of the extracellular matrix, Volume I. CRC Press, Boca Raton, FL, 1982, pp. 1–30.

    Google Scholar 

  19. Bornstein P, Sage H: Structurally distinct collagen types. Annu Rev Biochem 49: 957–1003, 1980.

    Google Scholar 

  20. Glanville RW: A comparison of models for the macromolecular structure of interstitial and basement membrane collagens. Arzneim Forsch/Drug Res 32: 1353–1357, 1982.

    Google Scholar 

  21. Sage H: Collagens of basement membranes. J Invest Dermatol 79: 51s-59s, 1982.

    Google Scholar 

  22. Hessle H, Engvall E: Type VI collagen: studies on its localization, structure, and biosynthetic form with monoclonal antibodies. J Biol Chem 259: 3955–3961, 1984.

    Google Scholar 

  23. Kuhn K, Wiedemann H, Timpl R, Ristelli J, Dieringer H, Voss T, Glanville R: Macromolecular structure of basement membrane collagens. Identification of 7s collagen as a crosslinking domain of type IV collagen. FEBS Lett 125: 123–128, 1981.

    Google Scholar 

  24. Timpl R, Wiedemann H, VanDelden V, Furthmayer H, Kuhn K. A network model for the organization of type IV collagen molecules in basement membranes. Eur J Biochem 120: 203–211, 1981.

    Google Scholar 

  25. Grotendorst GR, Seppa HEJ, Kleinman HK, Martin GR: Attachment of smooth muscle cells to collagen and their migration toward platelet derived growth factor. Proc Natl Acad Sci USA 78: 3669–3672, 1981.

    Google Scholar 

  26. Uitto V-J, Schwartz D, Veis A: Degradation of basement membrane collagen by neutral proteases from human leukocytes. Eur J Biochem 105: 409–417, 1980.

    Google Scholar 

  27. Mainardi CL, Dixit SN, Kang AH: Degradation of type IV (basement membrane) collagen by a proteinase isolated from human polymorphonuclear leukocyte granules. J Bio Chem 255: 5435–5441, 1980.

    Google Scholar 

  28. Liotta LA, Abe S, Gehron-Robey P, Martin GR: Preferential digestion of basement membrane collagen by an enzyme derived from a metastatic murine tumor. Proc Natl Acad Sci USA 76: 2268–2272, 1979.

    Google Scholar 

  29. Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, Shafie S: Metastatic potential correlated with enzymatic degradation of basement membrane collagen. Nature 284: 67–68, 1980.

    Google Scholar 

  30. Kalebic T, Garbisa S, Glaser B, Liotta LA: Basement membrane collagen: degradation by migrating endothelial cells. Science 221: 281–283, 1983.

    Google Scholar 

  31. Liotta LA, Thorgeirrson VP, Garbisa S: Role of collagenases in tumor cell invasion. Cancer Met Rev 1: 277–288, 1982.

    Google Scholar 

  32. Lindahl V, Hook M: Glycosaminoglycans and their binding to biological macromolecules. Ann Rev Biochem 47: 385–417, 1978.

    Google Scholar 

  33. Iozzo RV: Proteoglycans and neoplastic-mesenchymal cell interactions. Human Pathology 15: 2–10, 1984.

    Google Scholar 

  34. Hassell JR, Gehron-Robey P, Barrach H-J, Wilczek J, Rennard SI, Martin GR: Isolation of a heparan sulfate containing proteoglycan from basement membrane. Proc Natl Acad Sci 77: 4494–4498, 1980.

    Google Scholar 

  35. Farquhar MG: The glomerular basement membrane: a selective macromolecular filter. In: Hay ED (ed) Cell Biology of Extracellular Matrix. Plenum Press, New York, 1981, p 335.

    Google Scholar 

  36. Hook M, Kjellen L, Johansson S, Robinson J: Cell-surface glycosaminoglycans. Ann Rev Biochem 53: 847–869, 1984.

    Google Scholar 

  37. Kramer RH, Vogel KG, Nicolson GL: Solubilization and degradation of subendothelial matrix glycoproteins and proteoglycans by metastatic tumor cells. J Biol Chem 257: 2678–2686, 1982.

    Google Scholar 

  38. Kramer RH, Vogel KG: Selective degradation of basement membrane macromolecules by metastatic melanoma cells. JNCI 72: 889–897, 1984.

    Google Scholar 

  39. Brennan MJ, Oldberg A, Hayman EG, Ruoslahti E: Effect of a proteoglycan produced by rat tumor cells on their adhesion to fibronectin-collagen substrata. Cancer Res 43: 4302–4307, 1953.

    Google Scholar 

  40. Hynes RO, Yamada KM: Fibronectins: multifunctional modular glycoproteins. J Cell Biol 95: 369–377, 1982.

    Google Scholar 

  41. Mosher DF: Physiology of fibronectin. Ann Rev Med 35: 561–575, 1984.

    Google Scholar 

  42. Hormann H: Fibronectin-mediator between cells and connective tissue. Klin Wodenschr 60: 1265–1277, 1982.

    Google Scholar 

  43. Repesh LA, Fitzgerald TJ, Furcht LT: Fibronectin involvement in granulation tissue and wound healing in rabbits. J Histochem Cytochem 30: 351–358, 1982.

    Google Scholar 

  44. Donaldson DJ, Mahan JT: Fibrinogen and fibronectin as substrates for epidermal cell migration during wound closure. J Cell Sci 62: 117–127, 1983.

    Google Scholar 

  45. Nishida T, Nakagawa S, Awata T, Ohashi Y, Watanabe K, Manabe R: Fibronectin promotes the epithelial migration of cultured rabbit cornea in situ. J Cell Biol 97: 1653–1657, 1983.

    Google Scholar 

  46. Alitalo KT, Hovi T, Vaheri A: Fibronectin is produced by human macrophages. J Exp Med 151: 602–613, 1980.

    Google Scholar 

  47. Villiger B, Kelley DG, Engleman W, Kuhn C, McDonald JA: Human alveolar macrophage fibronectin-synthesis, secretion and ultrastructural localization during gelatincoated latex particle binding. J Cell Biol 90: 711–720, 1981.

    Google Scholar 

  48. Menzel EJ, Smolen JS, Liotta L, Reid KBM: Interaction of fibronectin with clq and its collagen-like fragment (CLF). FEBS Lett 29: 188–192, 1980.

    Google Scholar 

  49. Hautanen A, Keski-Oja J: Interaction of fibronectin with complement component c3. Scand J Immunol 17: 225–230, 1983.

    Google Scholar 

  50. Norris DA, Clark RAF, Swigard LM, Huff JC, Weston WL, Howell SE: Fibronectin fragment(s) are chemotactic for human peripheral blood monocytes. J Immunol 129: 1612–1618, 1982.

    Google Scholar 

  51. Czop J, Kadish J, Austen F: Augmentation of human monocyte opsonin-independent phagocytosis by fragments of human plasma fibronectin. Proc Natl Acad Sci USA 78: 3649–3653, 1981.

    Google Scholar 

  52. Perri RT, Kay NE, McCarthy J, Vessella RL, Jacob HS, Furcht LT: Fibronectin enhances in vitro monocytemacrophage mediated tumoricidal activity. Blood 60: 430–435, 1982.

    Google Scholar 

  53. Ruoslahti E: Fibronectin in cell adhesion and invasion. Cancer Met Rev 3: 43–51, 1984.

    Google Scholar 

  54. Hynes RO: Cell surface proteins and malignant transformation. Biochim Biophys Acta 458: 73–107, 1976.

    Google Scholar 

  55. Furcht LT: Role of cell adhesion on molecules in promoting migration of normal and malignant cells. In: McCullough JJ and Sandler GR (eds) Advances in Immunobiology: blood cell antigens and bone marrow transplantation. Alan R Liss, New York, 1984, pp 15–33.

    Google Scholar 

  56. Grinnell F: Fibroblast receptor for cell-substratum adhesion: studies on the interaction of baby hamster kidney cells with latex beads by cold insoluble globuline (plasma fibronectin). J Cell Biol 86: 104–112, 1980.

    Google Scholar 

  57. Carter WGH, Rauvala H, and Hakomori S-I: Studies on cell adhesion and recognition II. The kinetics of cell adhesion and cell spreading on surfaces coated with carbohydrate-reactive protein (glycosidases and lectins) and fibronectin. J Cell Biol 88: 138–148, 1981.

    Google Scholar 

  58. McCarthy JB, Furcht LT: Laminin and fibronectin promote the haptotactic migration of B16 mouse melanoma cells in vitro. J Cell Biol 98: 1474–1480.

  59. Smith DE, Furcht LT: Localization of two unique heparin binding domains of human plasma fibronectin with monoclonal antibodies. J Biol Chem 257: 6518–6523, 1982.

    Google Scholar 

  60. Smith DE, Mosher DF, Johnson RB, Furcht LT: Immunological identification of two sulfhydryl-containing fragments of human plasma fibronectin. J Biol Chem 257: 5831–5838, 1982.

    Google Scholar 

  61. Pierschbacher MD, Hayman EG, Ruoslahti E: Location of the cell attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule. Cell 26: 259–267, 1981.

    Google Scholar 

  62. Pierschbacher MD, Ruoslahti E: Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309: 30–33, 1984.

    Google Scholar 

  63. Petersen TE, Thogersen HC, Skorstengaard K, Vibe-Petersen K, Sahl P, Sottrup-Jensen L, Magnusson S: Partial primary structure of bovine plasma fibronectin: three types of internal homology. Proc Natl Acad Sci 80: 137–141, 1983.

    Google Scholar 

  64. Schwarzbauer JE, Tamkun JW, Lemischka IR, Hynes RO: Three different fibronectin mRNAs arise by alternative splicing within the coding region. Cell 135: 421–431, 1983.

    Google Scholar 

  65. McKeown-Longo PJ, Mosher DF: Binding of plasma fibronectin to cell layers of human skin fibroblasts. J Cell Biol 97: 466–472, 1983.

    Google Scholar 

  66. Timpl R, Engel J, Martin GR: Laminin — a multifunctional protein of basement membranes. Trends in Bioch Sci 8: 207–209, 1983.

    Google Scholar 

  67. Leivo I, Vaheri A, Timpl R: Wartiovaara J: Appearance and distribution of collagens and laminin in the early mouse embryo. Dev Biol 76: 100–114, 1980.

    Google Scholar 

  68. Terranova VP, Rohrbach DH, Martin GR: Role of laminin in the attachment of PAM 212 (epithelial) cells to basement membrane collagen. Cell 22: 719–726, 1980.

    Google Scholar 

  69. Vlodavsky I, Gospodarowicz D: Respective roles of laminin and fibronectin in adhesion of human carcinoma and sarcoma cells. Nature (Lond) 289: 304–306, 1981.

    Google Scholar 

  70. Couchman JR, Hook M, Rees DA, Timpl R: Adhesion, growth and matrix production by fibroblasts on laminin substrates. J Cell Biol 96: 177–183, 1983.

    Google Scholar 

  71. Hogan BLM: High molecular weight extracellular proteins synthesized by endoderm cells derived from mouse teratocarcinoma cells and extraembryonic membranes. Dev Biol. 76: 275–285, 1980.

    Google Scholar 

  72. Alitalo K, Kurkinen M, Vaheri A, Krieb T, Timpl R: Extracellular matrix components synthesized by human amniotic epithelial cells in culture. Cell 19: 1053–1062, 1980.

    Google Scholar 

  73. Palm SL, Furcht LT: Production of laminin and fibronectin by Schwannoma cells: cell-protein interactions in vitro and protein localization in peripheral nerve in vivo. J Cell Biol 96: 1218–1226, 1983.

    Google Scholar 

  74. Gospodarowicz D, Greenburg G, Foidart JM, Savian V: The production and localization of laminin in cultural vascular and corneal endothelial cells. J Cell Physiol 107: 171–183, 1981.

    Google Scholar 

  75. Wicha MS, Huard TK: Macrophages express cells surface laminin. Exp Cell Res 143: 475–478, 1983.

    Google Scholar 

  76. Rao CN, Margulies IMK, Tralka TS, Terranova VP, Macki JA, Liotta LA: Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment. J Biol Chem 257: 9740–9744, 1982.

    Google Scholar 

  77. Cooper AR, Kurkinen M, Taylor A, Hogan BLM: Studies on the biosynthesis of laminin by murine parietal endoderm cells. Eur J Biochem 119: 189–197, 1981.

    Google Scholar 

  78. Ott U, Odermatt E, Engel J, Furthmayr H, Timpl R: Protease resistance and the conformation of laminin. Eur J Biochem 123: 63–72, 1982.

    Google Scholar 

  79. Palm SL, McCarthy JB, Furcht LT: Changes in the model of the laminin molecule based on binding of a monoclonal antibody. Submitted.

  80. Timpl R, Johansson S, vanDelden V, Oberbaumer I, Hook M: Characterization of protease-resistant fragments of laminin mediating attachment and spreading of rat hepatocytes. J Biol Chem 256: 8922–8927, 1983.

    Google Scholar 

  81. Edgar D, Timpl R, Thoenen H: The heparin binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival. EMBO Journal 3: 1463–1468, 1984.

    Google Scholar 

  82. Rogers SL, McCarthy JB, Palm SL, Furcht LT, Letourneau PC: Neuron specific interactions with neurite promoting fragments of fibronectin. J Neuroscience 5: 369–378, 1985.

    Google Scholar 

  83. Mahan JT, Donaldson DJ, Hasty DL, McCarthy JB, Furcht LT: Location of a fibronectin domain involved in newt epidermal cell migration. J Cell Biol. In press, 1985.

  84. Terranova VP, Liotta LA, Russo RG, Martin GR: Role of laminin in the attachment and metastasis of murine tumor cells. Cancer Res 42: 2265–2269, 1982.

    Google Scholar 

  85. Varani J, McCoy JP, Shibata S, Maddox DE, Goldstein IJ, Wicha M: Differential expression of alaminlike substance by high-and low-metastatic tumor cells. Am J Path 111: 27–34, 1983.

    Google Scholar 

  86. Terranova VP, Rao CN, Kalebic T, Margulies IM, Liotta LA: Laminin receptor on the human breast carcinoma cells. Proc Natl Acad Sci 80: 444–448, 1983.

    Google Scholar 

  87. Rao NC, Barslay JH, Terranova VP, Liotta LA: Isolation of a tumor cell laminin receptor. Biochem Biophys Res Commun 111: 804–808, 1983.

    Google Scholar 

  88. Malinoff HL, Wicha MS: Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J Cell Biol 96: 1474–1479, 1983.

    Google Scholar 

  89. Brown SS, Malinoff HL, Wicha MS: Connectin: cell surface protein that binds both laminin and actin. Proc Natl Acad Sci 80: 5927–5930, 1983.

    Google Scholar 

  90. Hedman K, Kurkinen M, Alitalo K, Vaheri A, Johansson S, Hook M: Isolation of the pericellular matrix of human fibroblasts. J Cell Biol 81: 83–91, 1979.

    Google Scholar 

  91. Yamada KM, Weston JA: Isolation of a major surface glycoprotein from fibroblasts. Proc Natl Acad Sci 71: 3492–3496, 1974.

    Google Scholar 

  92. Carter WG, Hakomori S: A new cell surface detergent-insoluble glycoprotein matrix of human and hamster fibroblasts. The role of disulfide bonds in stabilization of the matrix. J Biol Chem 256: 6953–6960, 1981.

    Google Scholar 

  93. Carter WG: The cooperative role of the transformation sensitive glycoproteins, GP140 and fibronectin, in cell attachment and spreading. J Biol Chem 257: 3249–3257. 1982.

    Google Scholar 

  94. Lehto VP: 140,000 Dalton surface glycoprotein. A plasma membrane component of the detergent-resistant cytoskeletal preparations of cultured human fibroblasts. Exp Cell Res 143: 271–286, 1983.

    Google Scholar 

  95. Heller-Harrison RA, Carter WG: Pepsin generated type VI collagen is a degradation product of GP140. J Biol Chem 259: 6858–6864, 1984.

    Google Scholar 

  96. Bender BL, Carlin B, Jaffe R, Temple T, Chung AE: Production and distribution of entactin and GP-2 in M1536-B3 cells. Exp Cell Res 137: 415–425, 1982.

    Google Scholar 

  97. Carlin B, Jaffe R, Bender B, Chung AE: Entactin, a novel basal lamina-associated sulfated glycoprotein. J Biol Chem 256: 5209–5214, 1981.

    Google Scholar 

  98. Bender BL, Jaffe R, Carlin B, Chung AE: Immunocalization of entactin, a sulfated basement membrane component, in rodent tissues, and comparison with GP-2 (laminin). Am J Path 103: 419–425, 1981.

    Google Scholar 

  99. Enenstein J, Furcht LT: Isolation and characterization of epinectin, a novel adhesion protein for epithelial cells. J Cell Biol 99: 464–470, 1984.

    Google Scholar 

  100. Geisie GJ: Role of plasma, platelets, and endothelial cells in tumor metastasis. Cancer Met Rev 3: 99–116, 1984.

    Google Scholar 

  101. Hayman EG, Pierschbacher MD, Ohgren Y, Ruoslahti E: Serum spreading factor (vitronectin) is present at the cell surface and in tissues. Proc Natl Acad Sci USA 80: 4003–4007, 1983.

    Google Scholar 

  102. Barnes DW, Silnutzer J, See C, Shaffer M: Characterization of human serum spreading factor with monoclonal antibody. Proc Natl Acad Sci USA 80: 1362–1366, 1983.

    Google Scholar 

  103. Basara ML, McCarthy JB, Barnes DW, Furcht LT: The stimulation of haptotaxis and migration of tumor cells by serum spreading factor. Cancer Res. In press. 1985.

  104. Stenn KS. Epibolin: a protein of human plasma that supports epithelial cell movement. Proc Natl Acad Sci USA 78: 196–204, 1981.

    Google Scholar 

  105. Stenn KS, Madri JA, Tinghitella JA, Terranova VP: Multiple mechanisms of epidermal cell spreading. J Cell Biol 96: 63–67.

  106. Wylie DE, Damsky CH, Buck CA: Studies on the function of cell surface glycoproteins I. Use of antisera to surface membranes in the identification of membrane components relevant to cell-substrate adhesion. J Cell Biol 80: 386–402, 1979.

    Google Scholar 

  107. Hewitt AT, Kleinman HK, Pennypacker JP, Martin GR: Identification of an adhesion factor for chondrocytes. Proc Natl Acad Sci 77: 375–377, 1980.

    Google Scholar 

  108. Izzard CS, Lochner LR: Formation of cell-to-substrate contacts during fibroblast motility: an interference-reflexion study. J Cell Sci 42: 81–116, 1980.

    Google Scholar 

  109. Chen W-T, Singer SJ: Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts. J Cell Biol 95: 205–222, 1982.

    Google Scholar 

  110. Rollins BJ, Cathcart MK, Culp LA: Fibronectin-proteoglycan binding as the molecular basis for fibroblast adhesion to extracellular matrices. In: Horwitz M (ed) The Glycoconjugates. Academic Press, New York, 1982, pp 289–329.

    Google Scholar 

  111. Laterra J, Silbert JE, Culp LA: Cell surface heparan sulfate mediates some adhesive responses to glycos-aminoglycan binding matrices, including fibronectin. J Cell Biol 196: 112–123, 1983.

    Google Scholar 

  112. Lark MW, Culp LA: Turnover of heparan sulfate proteoglycans from substratum adhesion sites of murine-fibroblasts. J Biol Chem 219: 212–217, 1984.

    Google Scholar 

  113. Geiger B, Avnur Z, Rinnerthaler G, Hinssen H, Small VJ: Microfilament organizing centers in areas of cell contacts cytoskeletal interactions during cell attachment and locomotion. J Cell Biol 99: 835–915, 1984.

    Google Scholar 

  114. Chen W-T: Mechanism of retraction of the trailing edge during fibroblast movement. J Cell Biol 90: 187–200, 1981.

    Google Scholar 

  115. Schiffman E, Gallin JJ: Biochemistry of phagocyte chemotaxis. Curr Top Cell Regul 15: 203–261, 1979.

    Google Scholar 

  116. Snyderman R, Goetzl J: Molecular and cellular mechanisms of leukocyte chemotaxis. Science (Wash DC) 213: 830–837, 1981.

    Google Scholar 

  117. Wilkinson PC: The measurement of leucocyte chemotaxis. J Immul Meth 31: 133–148, 1982.

    Google Scholar 

  118. Romualdez AG, Wood PA. A unique complement derived chemotactic factor for tumor cells. Proc Natl Acad Sci 72: 4128–4132, 1975.

    Google Scholar 

  119. Ushijima K, Nishi H, Ishikura A, Hayashi H: Characterization of two different factors chemotactic for cancer cells from tumor tissue. Vircows Arch B Cell Path 21: 119–131, 1976.

    Google Scholar 

  120. Mundy GR, DeMartino S, Rowe DW: Collagen and collagen derived fragments are chemotactic for tumor cells. J Clin Inves 68: 1102–1105, 1981.

    Google Scholar 

  121. Mensing H, Albini A, Krieg T, Pontz BF, Muller PK: Enhanced chemotaxis of tumor-derived and virus-transformed cells to fibronectin and fibroblast conditioned medium. Int J Cancer 33: 43–48, 1984.

    Google Scholar 

  122. Orr W, Varani J, Gondek MD, Ward PA, Mundy GR: Chemotactic responses of tumor cells to products of resorbing bone. Science (Wash DC) 203: 176–179, 1979.

    Google Scholar 

  123. Wass JA, Varani J, Plantek GE, Goff D, Ward PA: Characteristics of the chemotactic factor-mediated cell swelling response of tumor cells. JNCI 166: 927–933, 1981.

    Google Scholar 

  124. Lam WC, Delikatny EJ, Orr WJ, Wass J, Varani J, Ward PA: The chemotactic response of tumor cells. A model for cancer metastasis. Am J Path 104: 69–76, 1981.

    Google Scholar 

  125. Ozaki T, Yoshida K, Ushijima K, Hayashi H: Studies on the mechanisms of invasion in cancer. II. In vivo effects of a factor chemotactic for cancer cells. Int J Cancer 7: 93–100, 1971.

    Google Scholar 

  126. Zigmond SH, Hirsch JG: Leukocyte locomotion and chemotaxis. New methods for evaluation and demonstration of a cell-derived chemotactic factor. J Exp Med 137: 387–410, 1973.

    Google Scholar 

  127. Zigmond SH: Ability of polymorphonuclear leukocytes to orient in gradients of chemotactic factors. J Cell Biol 75: 606–616, 1977.

    Google Scholar 

  128. Honn KV, Cavanaugh P, Evens C, Taylor JD, Sloane BF: Tumor cell-platelet aggregation: induced by cathepsin B-like proteinase and inhibited by prostacyclin. Science 217: 540–542, 1982.

    Google Scholar 

  129. Carter SB: Haptotaxis and the mechanism of cell motility. Nature (Lond) 213: 256–260, 1967.

    Google Scholar 

  130. Carter SB: Cell movement and cell spreading: a passive of an active process. Nature 225: 858–859, 1970.

    Google Scholar 

  131. Harris A: Behavior of cultured cells on substrata of variable adhesivenesss. Exp Cell Res 77: 285–297, 1973.

    Google Scholar 

  132. Bretscher MS: Endocytosis: relation to capping and cell locomotion. Science 224: 682–686, 1984.

    Google Scholar 

  133. Rich A, Harris AK: Anomalous preference of cultured macrophages for hydrophobic and roughened substrata. J Cell Sci 50: 1–7, 1981.

    Google Scholar 

  134. Letourneau PC: Cell to substratum adhesion and guidance of axonal elongation. Dev Biol 44: 92–101, 1975.

    Google Scholar 

  135. Ali IO, Hynes RO: Effects of LETS glycoprotein on cell motility. Cell 14: 439–446, 1978.

    Google Scholar 

  136. Lacovara J, Cramer EB, Quigley JP: Fibronectin enhancement of directed migration of B16 melanoma cells. Canc Res 44: 1657–1663, 1984.

    Google Scholar 

  137. McCarthy JB, Palm SL, Furcht LT: Migration by haptotaxis of a Schwann cell tumor line to the basement membrane glycoprotein laminin. J Cell Biol 97: 772–777, 1983.

    Google Scholar 

  138. Rogers SL, Letourneau PC, Palm SL, McCarthy J, Furcht LT: Neurite extension by peripheral and central nervous system neurons in response to substratum-bound fibronectin and laminin. Dev Biol 98: 212–220, 1983.

    Google Scholar 

  139. Baron Von Evercooren A, Kleinman HK, Ohno S, Marangoes P, Schwartz JP, Dubois-Dalcq ME: Nerve growth factor, laminin, and fibronectin promote neurite growth in human fetal sensory ganglia cultures. J Neuroscience Res 8: 179–193, 1982.

    Google Scholar 

  140. Liotta LA, Rao CV, Barsky SH: Tumor invasion and the extracellular matrix. Lab Inves 49: 636–649, 1983.

    Google Scholar 

  141. Fidler IJ, Hart IR: Biological diversity in metastatic neoplasms: origins and implications. Science 217: 998–1003, 1983.

    Google Scholar 

  142. McCarthy JB, Hagen S, Furcht LT: Identification of two cell attachment domains in fibronectin that differ in haptotactic promoting activity, 1985, submitted.

  143. Raz A, Geiger B: Altered organization of cell-substrate contacts and membrane-associated cytoskeleton in tumor cell variants exhibiting different metastatic capabilities. Cancer Res 42: 5183–5190, 1982.

    Google Scholar 

  144. Sas DF, McCarthy JB, Furcht LT: Alterations in basement membrane protein substrates by normal and tumor cells, 1985, submitted.

  145. Basara ML, McCarthy JB, Palm SL, Furcht LT: Inhibition of experimental murine tumor metastasis by laminin fragments, 1985, submitted.

  146. Barsky SH, Rao CN, Williams JE, Liotta LA: Laminin molecular domains which alter metastasis in a murine model. J Clin Inves 74: 843–848, 1984.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Laboratory Medicine and Pathology, University of Minnesota, 55455, Minneapolis, MN, USA

    James B. McCarthy, Michael L. Basara, Sally L. Palm, Daryl F. Sas & Leo T. Furcht

Authors
  1. James B. McCarthy
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Michael L. Basara
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Sally L. Palm
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Daryl F. Sas
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Leo T. Furcht
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

McCarthy, J.B., Basara, M.L., Palm, S.L. et al. The role of cell adhesion proteins—laminin and fibronectin—in the movement of malignant and metastatic cells. Cancer Metast Rev 4, 125–152 (1985). https://doi.org/10.1007/BF00050692

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00050692

Keywords

Search

Navigation