Abstract
In order to achieve effective targeting of antibody-drug conjugates to specific types of cells, a comprehensive understanding of the chemical, physical, and dynamic properties of cell surface structures is essential. Glycosphingolipids (briefly, glycolipids), as discussed here, are potentially useful to achieve effective targeting for the following reasons: (i) They are an integral part of the lipid bilayer, and the majority are assumed to be inserted at the outer leaflet of the plasma membrane; (ii) their structure and organization in membranes differ from one type of cell to another and constitute characteristic cell surface specificity of each type of cell? and (iii) they may be more readily internalized than other membrane components, since receptor carbohydrates are directly inserted in membranes.
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References
S. Hakomori, Glycosphingolipids in cellular interaction, differentiation, and oncogenesis, Ann. Rev. Biochem. 50:733 (1981).
S. Hakomori, Aberrant glycosylation in cancer cell membranes as focused on glycolipids: Overview and perspectives, Cancer Res. 45:2405 (1985).
J. Sundsmo and S. Hakomori, Laco-N-neotetraosylceramide (“paraglaoboside”) as a possible tumor-associated surface antigen of hamster NILpy tumor, Biochem. Biophys. Res. Commun. 68:799 (1976).
G. Rosenfelder, W.W. Young, Jr., and S. Hakomori, Association of the glycolipid pattern with antigenic alterations in mouse fibroblasts transformed by murine sarcoma virus, Cancer Res. 37:1333 (1977).
S. Hakomori and W.W. Young, Jr., Tumor-associated glycolipid antigens and modified blood group antigens, Scand. J. Immunol. Supplement 6:97 (1978).
J.L. Magnani, B. Nilsson, M. Brockhaus, D. Zopf, Z. Steplewski, H. Koprowski, and V. Ginsburg, A monoclonal antibody-defined antigen associated with gastrointestinal cancer is a ganglioside containing sialylated lacto-N-fucopentaose II, J. Biol. Chem. 257:14365 (1982).
K. Fukushima, M. Hirota, P.I. Terasaki, A. Wakisaka, H. Togashi, D. Chia, N. Suyhama, Y. Fukushi, E. Nudelman, and S. Hakomori, Characterization of sialosylated Lewisx as a new tumor-associated antigen, Cancer Res. 44:5279 (1984).
Y. Fukushi, E. Nudelman, S.B. Levery, H. Rauvala, and S. Hakomori, Novel fucolipids accumulating in human cancer. III. A hybridoma antibody (FH6) defining a human cancer-assoicated difucoganglioside (VI3NeuAcV3III3Fuc2nLc6), J. Biol. Chem. 259:10511 (1984).
Y. Fukushi, S. Hakomori, E. Nudelman, and N. Cochran, Novel fucolipids accumulating in human adenocarcinoma. II. Selective isolation of hybridoma antibodies that differentially recognize mono-, di-, and trifucosylated type 2 chain, J. Biol. Chem. 259:4681 (1984).
K. Abe, J.M. McKibbin, and S. Hakomori, The monoclonal antibody directed to difucosylated type 2 chain (Fucα1→2Galβl→4[fucα1→3] GlcNAβl→R; Y determinant), J. Biol. Chem. 258:11793 (1983).
A. Brown, T. Feizi, H.C. Gooi, M.J. Emblton, J.K. Picard, and R.W. Baldwin, A monoclonal antibody against human colonic adenoma recognizes difucosylated type 2 blood group chains. Biosci. Rep. 3:163 (1983).
K.O. Lloyd, G. Larson, N. Stromberg, J. Thurin, and K.-A. Karlsson, Mouse monoclonal antibody F-3 recognizes difucosyl type 2 blood group structure, Immunogenetics 17:537 (1983).
Y. Fukushi, S. Hakomori, and T. Shepard, Localization and alteration of mono-, di-, and trifucosyl α1→3 type 2 chain structures during embryogenesis and in human cancer, J. Exp. Med. 159:506 (1984).
Y. Fukushi, R. Kannagi, S. Hakomori, T. Shepard, B.G. Kulander, and J.W. Singer, Localization and distribution of difucoganglioside (VI3NeuAcV3III3Fuc2nLc5) in normal and tumor tissues defined by its monoclonal antibody FH6, Cancer Res. 45:3711 (1985).
S. Hakomori, and R. Kannagi, Glycosphingolipids as tumor-associated and differentiation markers, J. Natl. Cancer Inst. 71:231 (1983).
E. Nudelman, S. Hakomori, R. Kannagi, S. Levery, M.-Y. Yeh, K.E. Hellström, and I. Hellström, Characterization of a human melanoma-associated ganglioside antigen defined by a monoclonal antibody, 4.2, J. Biol. Chem. 257:12752 (1982).
C.S. Pukel, K.O. Lloyd, L.R. Trabassos, W.G. Dippold, H.F. Oettgen, and L.J. Old, GD3, a prominent ganglioside of human melanoma: Detection and characterization by mouse monoclonal antibody, J. Exp. Med. 155:1133 (1982).
L.D. Cahan, R. Irie, R. Singh, A. Cassidenti, and J.C. Paulson, Identification of a human neuroectodermal tumor antigen (OFA-I-2) as ganglioside GD2, Proc. Natl. Acad. Sci. USA 79:7629 (1982).
K. Watanabe, C.S. Pukel, H. Takeyama, K.O. Lloyd, H. Shiku, L.T.C. Li, L.R. Trabassos, H.F. Oettgen, and L.J. Old, Human melanoma antigen AH is an autoantigen ganglioside related to GD2, J. Exp. Med. 156:1884 (1982).
O. Nillson, J.-E. Mansson, T. Brezicka, J. Holmgren, L. Lindholm, S. Sorenson, F. Yngvason, and L. Svennerholm, Fucosyl GM1, a ganglioside associated with small cell lung carcinomas, Glycoconjugate J., 1:43 (1984).
E.G. Bremer, S.B. Levery, S. Sonnino, R. Ghidoni, S. Canevari, R. Kannagi, and S. Hakomori, Characterization of a glycosphingolipid antigen defined by the monoclonal antibody MBr1 expressed in normal and neoplastic epithelial cells of human mammary gland, J. Biol. Chem. 259:14773 (1984).
D.L. Urdal, and S. Hakomori, Tumor-associated ganglio-N-triosylceramide: Target for antibody dependent, avidin-mediated drug killing of tumor cells, J. Biol. Chem. 255:10509 (1980).
S. Hakomori, W.W. Young, Jr., and D. Urdal, Glycolipid tumor cell markers and their monoclonal antibodies: Drug targeting and immunosuppression, in: “Monoclonal Antibodies in Drug Development”, T. August, ed., Johns Hopkins University Press, Baltimore (1982).
G. Weissman, D. Bloomgarden, R. Kaplan, C. Cohen, S. Hoffstein, T. Collins, A. Gotlieb, and D. Nagle, A general method for the introduction of enzymes, by means of immunoglobulin-coated liposomes, into lysosomes of deficient cells, Proc. Natl. Acad. Sci. USA 72:88 (1975).
C.M. Cohen, G. Weissmann, S. Hoffstein, Y.C., Awasthi, and S.K. Srivastava, Introduction of purified hexosaminidase A into Tay-Sachs leukocytes by means of immunoglobulin-coated liposomes, Biochemistry 15:452 (1976).
G. Gregoriadis, and E.D. Neerunjun, Homing of liposomes to target cells, Biochem. Biophys. Res. Commun. 65:537 (1975).
G. Gregoriadis, E.D. Neerunjun, and R. Hunt, Fate of liposome-associated agent injected into normal and tumor-bearing rodents: Attempts to improve localization in tumor tissues, Life Sci. 21:374 (1977).
L. Huang, and S.J. Kennel, Binding of immunoglobulin G to phospholipid vesicles by sonication, Biochemistry 18:1702 (1979).
D. Sinha, and P. Karush, Attachment to membranes of exogenous immunoglobulin conjugated to a hydrophobic anchor, Biochem. Biophys. Res. Commun. 90:554 (1979).
T.D. Heath, R.T. Farley, and D. Papahadjopoulous, Antibody targeting of liposomes: Cell specificity obtained by conjugation of F(ab’)2 to vesicle surface, Science 210:539 (1980).
W.W. Young, Jr., and S. Hakomori, Therapy of mouse lymphoma with monoclonal antibodies to glycolipid: Selection of low antigenic variants in-vivo, Science 211:487 (1981).
J. Brown, R.G. Woodbury, C.E. Hart, I. Hellstrom, and K. Hellstrom, Quantitative analysis of melanoma-assoicated antigen p97 in normal and neoplastic tissues, Proc. Natl. Acad. Sci. USA 78:539 (1981).
A.C. Morgan, D.R. Galloway, and R.A. Reisfeld, Production and characterization of monoclonal antibody to melanoma-specific glycoproteins, Hybridoma 1:27 (1981).
J. Wiels, S. Junqua, P. Dujardin, J.-B. LePecq, and T. Tursz, Properties of immunotoxins against a glycolipid antigen associated with Burkitt’s lymphoma, Cancer Res. 44:129 (1984).
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© 1986 Plenum Press, New York
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Hakomori, Si. (1986). Tumor-Associated Glycolipid Markers: Possible Targets for Drug and Immuno-Toxin Delivery. In: Gregoriadis, G., Senior, J., Poste, G. (eds) Targeting of Drugs With Synthetic Systems. NATO ASI Series, vol 113. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5185-6_3
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DOI: https://doi.org/10.1007/978-1-4684-5185-6_3
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