Abstract
Cellular recognition of the extracellular matrix (ECM) is fundamentally important for development, the maintenance of normal adult tissue architecture and function, and for the pathogensis of diesease. The ECM exerts its effects in large part, by serving as an exoskeleton for cells within tissues, thereby providing structural, and other, information to cells that serve to regulate normal cell fuction. Understanding subtle changes in the cellular recognition of the ECM that occur as a result of malignant cell transformation can provide important information regarding the altered biology of tumor celss and could lead to novel therapeutic and/or diagnostic strategies for the altered biology of tumor invasion and metastasis, two features of many malignancies that contribute to the mortality of cancer patients.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
Abbreviations
- CS :
-
Chondroitin Sulfate;
- ECM :
-
Extracellular Matrix;
- FN :
-
Fibronectin;
- FN-C/H-I, FN-C/H-II, FN-C/H-III :
-
Fibronectin-derived Cell Adhesion/Heparin Binding Peptides I., II, III;
- GAG :
-
Glycosaminoglycan;
- MAb :
-
Monoclonal Antibody;
- OVA :
-
Ovalbumin;
- αDX :
-
p-nitrophenyl-α-D-xylopyranoside;
- βDX :
-
p-nitrophenyl-β-D-xylopyranoside
References
Albelda, S.M. and Buck, C.A., 1990, Integrins and other cell adhesion molecules. FASEB J. 4:2868–2880.
Brennan, M.J., Oldberg, A., Hayman, E.G., and Ruoslahti, E., 1983, Effect of a proteoglycan produced by rat tumor cells on their adhesion to fibronectin-collagen substrata. Cancer Res. 43:4302–4307.
Bober-Barkalow, F.J. and Schwarzbauer, J.E., 1991, Localization of the major heparinbinding site in fibronectin. J. Biol. Chem. 266:7812–7818.
Bumol, T.F. and Reisfeld, R.A., 1982, Unique glycoprotein-proteoglycan complex defined by monoclonal antibody on human melanoma cells. Proc. Natl. Acad. Sci. USA 79:1245–1249.
Buck, C.A. and Horwitz, A.F., 1987, Cell surface receptors for extracellular matrix molecules Annu. Rev. Cell Biol. 3:179–205.
Couchman, J.R. and Höök, M., 1988, Proteoglycans and wound repair, in “The Molecular and Cellular Biology of Wound Repair,” RAF. Clark and P. Henson, eds., Plenum Press, New York, pp 437–470.
Drake, S.L, Klein, D.J., Mickelson, D.J., Oegema, T.R., Furcht, L.T., and McCarthy, J.B., 1992, Cell surface phosphatidylinositol-anchored heparan sulfate proteoglycan initiates mouse melanoma cell adhesion to a fibronectin-derived, heparin-binding synthetic peptide. J. Cell Biol. 117:1331–1342.
Faassen, A.E., Drake, S.L., Iida, J., Knutson J.R., and McCarthy, J.B, 1992a, Mechanisms of normal cell adhesion to the extracellular matrix and alterations associated with tumor invasion and metastasis. Adv. Pathol. Lab. Med. 5:229–260.
Faassen, A.E., Schrager, J.A., Klein, D.J., Oegema, T.R., Couchman J.R., and McCarthy, J.B., 1992b, A cell surface chondroitin sulfate proteoglycan, immunologically related to CD44, is involved in type I collagen-mediated melanoma cell motility and invasion. J. Cell Biol. 116:521–532.
Fidler, I J., 1986, Rational and methods for the use of nude mice to study the biology and therapy of human cancer metastasis. Cancer Metast. Rev. 5:29–49.
Gallagher, J.T., 1989, The extended family of proteoglycans: Social residents of the pericellular zone. Curr. Opin. Cell Biol. 1:1201–1218.
Garrigues, H.J., Lark, M.W., Lara, S., Hellström, I., Hellström K.E., and Wight, T.N., 1986, The melanoma proteoglycan: restricted expression on microspikes, a specific microdomain of the cell surface. J. Cell Biol. 103:1699–1710.
Guan, J-L. and Hynes, R.O., 1990, Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor α4β1. Cell 60:51–63.
Guan, J-L., Trevithick, J.E., and Hynes, R.O., 1991, Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Reg. 2:951–964.
Haugen, P.K., McCarthy, J.B., Skubitz, A.P.N., Furcht, L.T., and Letourneau, P.C., 1990, Recognition of the A chain carboxy-terminal heparin binding region of fibronectin involves multiple sites: Two contiguous sequences act independently to promote neural cell adhesion. J. Cell Biol. 111:2733–2745.
Höök, M., Kjellen, L., Johansson S., and Robinson, J., 1984, Cell surface proteoglycans. Annu. Rev. Biochem. 53:847–869.
Humphries, M.J., Komoriya, A., Akiyama, S.K., Olden K., and Yamada, K.M., 1987, Identification of two distinct regions of the type IIICS connecting segment of human plasma fibronectin that promote cell type-specific adhesion. J. Biol. Chem. 262:6886–6892.
Humphries, M.J., 1990, The molecular basis and specificity of integrin-ligand interactions. J. Cell Sci. 97:585–592.
Hynes, R.O., 1987, Integrins: A family of cell surface receptors. Cell 48:549–554.
Hynes, R.O., 1992, Integrins: Versatility, modulation, and signalling in cell adhesion. Cell 69:11–25.
Iida, J., Skubitz, A.P.N., Furcht, L.T., Wayner E.A., and McCarthy, J.B., 1992, Coordinate role for cell surface chondroitin sulfate proteoglycan and α4β1 integrin in mediating melanoma cell adhesion to fibronectin. J. Cell Biol. 118:431–444.
Kato, Y., Kimata, K., Ito, K., Karasawa K., and Suzuki, S., 1978, Effect of β-D-xyloside and cycloheximide on the synthesis of two types of proteochondroitin sulfate in chick embryo cartilage. J. Biol. Chem. 253:2784–2789.
Kornblihtt, A.R., Umezawa, K., Vibe-Pedersen, K., and Baralle, F.E., 1985, Primary structure of human fibronectin: Differential splicing may generate at least 10 polypeptides from a single gene. EMBO J. 4:1755–1759.
Kornberg, L.T., Earp, H.S., Turner, C.E., Prockop, C,. and Juliano, R.L., 1991, Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of β1 integrins. Proc. Natl. Acad. Sci. USA 88:8392–8396.
Kyte, J. and Doolittle, R.F., 1982, A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105–132.
Lark, M.W., Laterra, J., and Culp, L.A., 1985, Close and focal contact adhesions of fibroblasts to a fibronectin-containing matrix. Fed. Proc. 44:394–403.
Liao, N.S., St.John, I., McCarthy, J.B., Furcht, L.T., and Cheung, H.T., 1989, Adhesion of lymphoid cells to the carboxyl-terminal heparin-binding domains of fibronectin. Exp. Cell Res. 181:348–361.
Lohmander, S., Madsen, K., and Hinek, A., 1979, Secretion of proteoglycans by chondrocytes: Influence of colchicin, cytochalasin β and β-D-xyloside. Arch. Biochem. Biophys. 192:148–157.
McCarthy, J.B., Hagen S.T., and Furcht, L.T., 1986, Human fibronectin contains distinct adhesion and motility promoting domains for metastatic melanoma cells. J. Cell Biol. 102:179–188.
McCarthy, J.B., Chelberg, M.K., Mickelson D.J., and Furcht, L.T., 1988a, Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities. Biochemistry 27:1380–1388.
McCarthy, J.B., Skubitz, A.P.N., Palm, S.L., and Furcht, L.T., 1988b, Metastasis inhibition of different tumor types by purified laminin fragments and a heparin binding fragments of fibronectin. J. Natl. Cancer Inst. 80:108–116.
McCarthy, J.B., Skubitz, A.P.N., Zhao, Q., Yi, X-Y., Mickelson, DJ. and Furcht, L.T., 1990, RGD-independent cell adhesion to the carboxy-terminal heparin binding fragment of fibronectin involves heparin-dependent and-independent activities. J. Cell Biol. 110:777–787.
Mooradian, D.L., McCarthy, J.B., Cameron, D.J., and Furcht, L.T., 1992, Rabbit corneal epithelial cell adhere to two distinct heparin-binding synthetic peptides derived from fibronectin. Invest Opthalmol Vis. Sci. (in press).
Mould, A.P., Wheldon, L.A., Komoriyama, A., Wayner, E.A., Yamada, K.M., and Humphries, M.J., 1990, Affinity Chromatographie isolation of the melanoma cell adhesion receptor for the IIICS region of fibronectin and its identification as the integrin α4β1. J. Biol. Chem. 265:4020–4024.
Mould, A.P. and Humphries, M.J., 1991, Identification of a novel recognition sequence for the integrin a4b1 in the COOH-terminal heparin-binding domain of fibronectin. EMBO J. 10:4089–4095.
Robinson, J. and Gospodarowicz, D., 1984, Effect of p-nitrophenyl-β-D-xyloside on proteoglycan synthesis and extracellular matrix formation by bovine corneal endothelial cell cultures. J. Biol. Chem. 259:3818–3824.
Rogers, S.L., Letourneau, P.C., Peterson, B.A., Furcht, L.T., and McCarthy, J.B., 1987, Selective interaction of peripheral and central nervous system cells with two distinct cell-binding domains of fibronectin. J. Cell Biol. 105:1435–1442.
Ross, A.H., Cossu, G., Herlyn, M., Bell, J.R., Steplewski, Z., and Koprowski, H., 1983, Isolation and chemical characterization of a melanoma-associated proteoglycan antigen. Arch. Biochem. Biophy. 225:370–383.
Ruoslahti, E., 1991, Integrins. J. Clin. Invest. 87:1–5.
Saunders, S. and Bernfield, M., 1988, Cell surface proteoglycan binds mouse mammary epithelial cells to fibronectin and behaves as a receptor for interstitial matrix. J. Cell Biol. 106:423–430.
Schwartz, N.B., 1977, Regulation of chondroitin sulfate synthesis. J. Biol. Chem. 252:6316–6321.
Springer, T.A., 1990, Adhesion receptors of the immune system. Nature 346:425–434.
Stewart, J.M. and Young, J.D., 1984, “Solid Phase Peptide Synthesis,” 2nd ed. Pierce Chemical Co., Rockford, IL.
Visser, M.R., Vercellotti, G.M., McCarthy, J.B., Goodman, J.L., Herbst, T.J., Furcht, L.T., and Jacob, H.S., 1989, Herpes simplex virus inhibits endothelial cell attachment and migration to extracellular matrix proteins. Am. J. Pathol. 134:223–230.
Wait, K.A., Mugnai, G., and Culp, L.A., 1987, A second cell binding domain on fibronectin (RGDS-independent) for neurite extension of neuroblastoma cells. Exp. Cell Res. 169:311–327.
Wasteson, A., 1971, A method for the determination of the molecular weight and molecular-weight distribution of chondroitin sulfate. J. Chromatogr. 59:87–97.
Wayner, E.A., Garcia-Pardo, A., Humphries, M.J., McDonald, J.A., and Carter, W.G., 1989, Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin. J. Cell Biol. 109:1321–1330.
Wayner, E.A. and Kovach, N.L., 1992, Activation-dependent recognition by hematopoietic cells for the LDV sequence in the V region of fibronectin. J. Cell Biol. 116:489–497.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Plenum Press, New York
About this chapter
Cite this chapter
McCarthy, J.B., Skubitz, A.P.N., Furcht, L.T., Wayner, E.A., Iida, J. (1993). Coordinate Role for Proteoglycans and Integrins in Cell Adhesion. In: Hemler, M.E., Mihich, E. (eds) Cell Adhesion Molecules. Pezcoller Foundation Symposia, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2830-2_9
Download citation
DOI: https://doi.org/10.1007/978-1-4615-2830-2_9
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-44496-8
Online ISBN: 978-1-4615-2830-2
eBook Packages: Springer Book Archive