Abstract
It is now recognized that deaths from cancer are most frequently due to metastic development of the initial disease site, irrespective of the treatment or surgical extirpation of the primary tumor following diagnosis. The significant role played by fibronectin in the promotion and support of tumor cell migration from the primary cancer site to peripheral metastatic sites is well documented.1–6 Humphries7 pointed out that interference with the function of fibronection would probably inhibit the metastatic process and these authors identified a short peptidal fragment, GRGDS, that functioned in this manner. Unfortunately, the fragment was not stable and has a very short biological half life, requiring frequent administration of large quantities of the peptide.8 Later4 Humphries reported that both polymeric and cyclic peptides were also potent inhibitors of integrin-dependent adhesion and experimental metastasis models. Braatz et al.9 have also shown that a peptide containing the essential RGD peptide sequence retained its biological activity with an extended circulatory half-life when covalently bound to an isocyanate-containing polyurethane polymer.
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.
References
S.K. Akiyama, K. Olden, and K.M. Yamada, 1995, Fibronectin and integrins in invasion and metastasis, Cancer and Metastasis Review 14(3): 173–189.
S.K. Akiyama, K. Nagata, and K.M. Yamada, 1990, Cell surface receptors for extracellular matrix components, Biochim. Biophys. Acta 1031:91–110.
M.J. Humphries, 1990, The molecular basis and specificity of integrin-ligand interactions, J. Cell Sci 97:585–592.
M.J. Humphries, 1993, Fibronectin and cancer: Rationales for the use of antiadhesive in cancer treatment, Cancer Biology 4:293–299.
R.O. Hynes, 1992, Integrins: Versatility, modulation and signaling in cell adhesion, Cell 69:11–25.
K.M. Yamada, 1991, Adhesive recognition sequences, J. Biol. Chem 266:12809–12812.
M.J. Humphries, K. Olden, and K.M. Yamada, 1986, A synthetic peptide from fibronectin inhibitors experimental metastasis of murine melanoma cells, Science 233:467–470.
M.J. Humphries, K.M. Yamada, and K. Olden, 1988, Investigation of the biological effects of anti-cell adhesive synthetic peptides that inhibit experimental metastasis of B16-F10 melanoma cells, J. Clin. Invest 81:782–790.
J.A. Braatz, Y. Yasuda, K. Olden, K.M. Yamada, and A.H. Heifetz, 1993, Functional peptide-polyurethane conjugates with extended circulatory half lives, Bioconjug. Chem 4(4):262–267.
D.F. Mosher, 1980, Fibronectin, Prog. Hemostasis Thromb 5:111–151.
H. Forastieri, and K.C. Ingham, 1983, Fluid-phase interaction between human plasma fibronectin and gelatin determined by fluorescence polarization assay, Arch. Biochem. Biophys 227:358–366.
K.C. Ingham, S.A. Brew, and B.S. Isaacs, 1988, Interaction of fibronectin and its gelatin-binding domains with fluorescent-labeled chains of type I collagen, J. Biol. Chem 263(10):4624–4628.
A. Garcia-Pardo, and L.I. Gold, 1993, Further characterization of the binding of fibronectin to gelatin reveals the presence of different binding interactions, Arch. Biochem. Biophys 304(1): 181–188.
K. Nakamura, S. Kashiwagi, and K. Takeo, 1992, Characterization of the interaction between human plasma fibronectin and collagen by means of affinity electrophoresis, J. Chromat 597:351–356.
Y. Lou, W.P. Olson, X.X. Tian, M.E. Klegerman, and M.J. Groves, 1995, Interaction between fibronectin-bearing surfaces and Bacillus Calmette Guérin (BCG) or gelatin microparticles, J. Pharm. Pharmacol 47:177–181.
K. Nagata, M.J. Humphries, K. Olden, and K.M. Yamada, 1985, Collagen can modulate cell interactions with fibronectin, J. Cell Biol 101:386–394.
D.L. Heene, D. Zekorn, and H.G. Lasch, 1968, Gelatin plasma volume expanders: Chemistry, biological activities and clinical experiences, Proc. 11th Congr. Int. Soc. Blood Transf, Sydney 1966, Bibl. No. 29, Part 3, pp. 907–913, Karger, Basel, New York.
H.H. Schöne, 1960, Chemistry and physicochemical characterization of gelatin plasma substitutes, Modified Gelatin as Plasma Substitutes, Biol. Haemat, No. 33, pp. 78–90, Karger, Basel, New York.
D. Zekorn, 1969, Intravascular retention, dispersal, excretion and breakdown of gelatin plasma substitutes, Modified Gelatin as Plasma Substitutes, Biol. Haemat, No. 33, pp. 131–140, Karger, Basel, New York.
G. Brodin, F. Hesselvik, and H. von Schenck, 1984, Decrease of plasma fibronectin concentration following infusion of a gelatin-based plasma substitute in man, Scand. J. Clin. Lab. Invest 44:529–533.
J.M. Saddler, and P.J. Horsey, 1987, The new generation gelatins: A review of their history, manufacture and properties, Anesthesia 42:998–1004.
J.M. Vedrinne, J.P. Hoen, D. Bussery, C. Veyssere, M. Richard, and J. Motin, 1991, Plasma fibronectin and complement following infusion of colloidal solutions after spinal anaesthesia, Intensive Care Med 17:83–86.
F.A. Blumenstock, P.L. Celle, A. Herrmannsdoerfer, C. Giunta, F.L. Minnear, E. Cho, and T.M. Saba, 1993, Hepatic removal of 125I-DLT gelatin after burn injury: A model of soluble collagenous debris that interacts with plasma fibronectin, J. Leukocyte Biol 54:56–64.
X. Gao, 1996, Peptides derived from gelatin as vectors for potential cancer treatment, Ph.D. Thesis, University of Illinois at Chicago.
Y. Yamaguchi, and Y. Mizushima, 1994, Lipid microspheres for drug delivery from the pharmaceutical viewpoint, Critical Reviews in Therapeutic Drug Carrier Systems 11(4): 215–229.
D.M. Lidgate, and N.E. Byars, 1995, Development of an emulsion-based muramyl dipeptide adjuvant formulation for vaccine, Pharm. Biotechnol 6:313–324.
P.K. Hansrani, S.S. Davis, and M.J. Groves, 1983, The preparation and properties of sterile intravenous emulsions, J. Parenteral Sci. & Technol 37:145–150.
H. Endoh, Y. Hashimoto, Y. Kawashima, and Y. Suzuki, 1980, Agglutination microassay of hapten-or protein-modified liposomes using a multiple cell culture harvester, J. Immunol. Methods 36:185–195.
H. Endoh, Y. Suzuki, and Y. Hashimoto, 1981, Antibody coating of liposomes with l-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide and the effect on target specificity, 44:79–85.
J.S. Ellingson, and W.E.M. Lands, 1968, Phospholipid reactivation of plasmalogen metabolism, Lipids 3(2): 111–120.
M.E. Klegerman, P.L. Zeunert, Y. Lou, P.O. Devadoss, and M.J. Groves, 1993, Inhibition of murine sarcoma cell adherence to polystyrene substrata by Bacillus Calmette Guérin: Evidence for fibronectin-mediatiated direct antitumor activity of BCG, Cancer Invest 11(6):660–666.
F. Grinnel, D.G. Hays, and D. Minter, 1977, Cell adhesion and spreading factor: Partial purification and properties, Exp. Cell. Res 110:175–190.
K.M. Yamada, and D.W. Kennedy, 1984, Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function, J. Cell. Biol 99:29–36.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Groves, M.J., Gao, X. (1998). Surface-Modified Phospholipid-Stabilized Emulsions as Targeted Systems for Inhibition of Metastatic Cancer. In: Hıncal, A.A., Kaş, H.S. (eds) Biomedical Science and Technology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5349-6_5
Download citation
DOI: https://doi.org/10.1007/978-1-4615-5349-6_5
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7440-4
Online ISBN: 978-1-4615-5349-6
eBook Packages: Springer Book Archive