This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gorelik, E. Articles by Galili, U. Search for Related Content PubMed PubMed Citation Articles by Gorelik, E. Articles by Galili, U.

Reduction of Metastatic Properties of BL6 Melanoma Cells Expressing Terminal Fucose1-2-Galactose after 1,2-Fucosyltransferase cDNA Transfection¹

University of Pittsburgh Cancer Institute and Department of Pathology, University of Pittsburgh, Pittsburgh, Pennsylvania 15213 [E. G., F. X.]; and Department of Microbiology and Immunology, Medical College of Pennsylvania-Hahnemann School of Medicine, Allegheny University, Philadelphia, Pennsylvania 19129 [T. H., F. A., U. G.]

We reported previously that transfection of BL6 melanoma cells that do not express the 1,3-galactosyltransferase (1,3GT) gene with the 1,3GT cDNA resulted in synthesis and expression of -galactosyl epitopes (Gal1-3Galß1-4GlcNAc-R) and an impairment of their metastatic potentials. It was of interest to test whether inhibition of metastatic properties of BL6 melanoma cells is specifically associated with the appearance of the terminal -Gal or whether capping N-acetyllactosamine with another oligosaccharide would also affect the metastatic properties of BL6 melanoma cells. For this purpose, BL6-2 clone isolated from B16BL6 melanoma was transfected with the 1,2-fucosyltransferase (1,2FT) cDNA. The 1,2FT catalyzes a transglycosylation reaction, resulting in syntheses of the Fuca1-2Galß1-4GlcNAc-R structure, which is known as the H antigen of O blood group in humans and is also synthesized in some cells of mice. Transfection of BL6 melanoma cells with the 1,2FT cDNA resulted in the appearance of the terminal Fuc1-2Galß1-4GlcNAc-R epitopes reacting with the Ulex europaeus agglutinin lectin. In parallel, the transfected cells showed a decrease in N-acetyllactosamine sialylation. Decline in sialylation of the transfected cells is likely to be the result of competition between 1,2FT and 2,3- or 2,6-sialyltransferases for the common substrate N-acetyllactosamine (Galß1-4GlcNAc-R) on N-linked carbohydrate chains of glycoproteins and glycolipids. The 1,2FT-transfected BL6-2 cells showed an increase in homotypic aggregation. In parallel, metastatic ability of the 1,2FT-transfected BL6-2 cells was reduced significantly in the immunocompetent as well as immunosuppressed (X-irradiated) mice. Thus, these data imply that capping N-acetyllactosamine with Gal or Fuc and the corresponding reduction in sialylation of BL6-2 melanoma cells were associated with reduction of their metastatic potential.

¹ This study is supported by NIH Grant CA59903.

² To whom requests for reprints should be addressed, at Biomedical Science Tower, W954, University of Pittsburgh Cancer Institute, Pittsburgh, PA 15213. Phone: (412) 624-0346; Fax: (412) 624-7736.

Received 8/26/96. Accepted 11/13/96.

This article has been cited by other articles:

				E. Assa-Kunik, D. Fishman, S. Kellman-Pressman, S. Tsory, S. Elhyany, O. Baharir, and S. Segal Alterations in the Expression of MHC Class I Glycoproteins by B16BL6 Melanoma Cells Modulate Insulin Receptor-Regulated Signal Transduction and Augments Resistance to Apoptosis J. Immunol., September 15, 2003; 171(6): 2945 - 2952. [Abstract] [Full Text] [PDF]

				Y. Oda, T. Senaha, Y. Matsuno, K. Nakajima, R. Naka, M. Kinoshita, E. Honda, I. Furuta, and K. Kakehi A New Fungal Lectin Recognizing {alpha}(1-6)-linked Fucose in the N-Glycan J. Biol. Chem., August 22, 2003; 278(34): 32439 - 32447. [Abstract] [Full Text] [PDF]

				M. Aubert, L. Panicot, C. Crotte, P. Gibier, D. Lombardo, M.-O. Sadoulet, and E. Mas Restoration of {{alpha}}(1,2) Fucosyltransferase Activity Decreases Adhesive and Metastatic Properties of Human Pancreatic Cancer Cells Cancer Res., March 1, 2000; 60(5): 1449 - 1456. [Abstract] [Full Text]

				M. Eckhardt, B. Gotza, and R. Gerardy-Schahn Mutants of the CMP-sialic Acid Transporter Causing the Lec2 Phenotype J. Biol. Chem., August 7, 1998; 273(32): 20189 - 20195. [Abstract] [Full Text] [PDF]