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Melanoma-associated Gangliosides in the Fish Genus Xiphophorus¹

Institut für Physiologische Chemie, Philipps-Universität Marburg, Karl-von-Frisch-Strasse, D-3550 Marburg [B. F-H., H. W.]; Genetisches Institut, Justus-Liebig-Universität Giessen Heinrich-Buff-Ring, D-6300 Giessen [A. A.]; Institut für Innere Medizin, Johannes Gutenberg-Universität Mainz, Langenbeckstrasse, D-6500 Mainz [W. G. D], Federal Republic of Germany; and La Jolla Cancer Research Foundation, La Jolla, California 92037 [W. B. S.]

Gangliosides from benign and malignant melanomas and from normal skin of the fish genus Xiphophorus were isolated and analyzed by thin-layer chromatography. Individual ganglioside components were characterized by mapping according to their sialic acid content and by cleavage with neuraminidases. In all three tissues examined, sulfatide and the gangliosides NeuAc-GalCer (G_M4), II³NeuAc-LacCer (G_M3), II³NeuAc-GgOse₃Cer (G_M2), and II³(NeuAc)₂-LacCer (G_D3) were found. Ganglioside G_D3 yielded a positive reaction, following immunoadsorption with mouse monoclonal antibody R24 on thin-layer plates. Two alkali-labile disialoganglioside species were specifically recognized by mouse monoclonal antibody D1.1, thus indicating the presence of O-acetyl-neuraminic acid residues. One of them, a major ganglioside component of the malignant melanoma, was identified as O-acetyl-G_D3, since it could be converted to the R24-positive G_D3 ganglioside after alkaline saponification. The other one appears to be restricted to the malignant tumor and represents a novel melanoma-associated ganglioside derivative. It was characterized as O-acetyl(NeuAc)₂-nLc₄Cer by exoglycosidase cleavage, by proving its neutral carbohydrate backbone as type II-chain lacto-series oligosaccharide using mouse monoclonal antibody 1B2, and by its cross-reaction with antibody R24 following alkaline treatment. Using antibody R24 and cryopreserved tissue sections of both benign and malignant amelanotic melanomas from albino fishes, it was demonstrated that one of the main melanoma-associated gangliosides, G_D3, was exposed predominantly in the malignant tumor. Thus, the chemical nature and even the immunohistochemical localization of the gangliosides in fish melanomas proved to be very similar to those of the known gangliosides in the phylogenetically distant human melanomas.

¹ This work was supported by the Deutsche Forschungsgemeinschaft (Sonderforschungsbereich 103, Zellenergetik und Zelldifferenzierung, Marburg) and by Alfred and Ursula Kulemann Stiftung, Marburg. Dedicated to Friedhelm Schneider, Marburg, on the occasion of his 60th birthday.

² Present address: The Biomembrane Institute, 201 Elliott Avenue West, Seattle, WA 98119. To whom requests for reprints should be addressed.

Received 3/ 6/87. Revised 2/16/88. Accepted 3/11/88.

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