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Volume 271, Number 49, Issue of December 6, 1996 pp. 31556-31561
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Suppression of Sialyl Lewis X Expression and E-selectin-mediated Cell Adhesion in Cultured Human Lymphoid Cells by Transfection of Antisense cDNA of an alpha 1right-arrow 3 Fucosyltransferase (Fuc-T VII)

(Received for publication, June 24, 1996, and in revised form, September 10, 1996)

Nozomu Hiraiwa Dagger , Taeko Dohi § , Naoko Kawakami-Kimura Dagger , Miki Yumen Dagger , Katsuyuki Ohmori , Michiyuki Maeda par and Reiji Kannagi Dagger

From the Dagger  Program of Experimental Pathology, Research Institute, Aichi Cancer Center, Nagoya 464, the § Division of Biochemistry and Nutrition, Research Institute, International Medical Center of Japan, Tokyo 162, and the  Department of Laboratory Medicine and par  Chest Disease Institute, Kyoto University, School of Medicine, Kyoto 606, Japan

The antisense cDNA approach was used to identify the endogenous fucosyltransferase species responsible for synthesis of the sialyl Lewis X (NeuAcalpha 2right-arrow3 Galbeta 1right-arrow4[Fucalpha 1right-arrow3]GlcNAcbeta 1right-arrowR) determinant in human lymphoid cells. The cultured human adult T-cell leukemia cell line, ED40515-N, expressed the message of alpha 1right-arrow3 fucosyltransferase (Fuc-T) IV and VII, with a low level of the Fuc-T III and VI message, and manifested the sialyl Lewis X as well as Lewis X (Galbeta 1right-arrow4 [Fucalpha 1right-arrow3]GlcNAcbeta 1right-arrowR) determinant at the cell surface. Transfection of this cell line with the pRc/CMV vector containing an antisense human Fuc-T VII construct (pRc/CMV/5'FT7AS) resulted in a significant decrease of endogenous Fuc-T VII message and a marked reduction in the cell surface expression of sialyl Lewis X determinant as well as a reduction in the enzymatic activity of alpha 1right-arrow3 fucosyltransferase against sialylated type 2 chain substrate. This was accompanied by diminution of cell adhesive activity toward E-selectin on interleukin-1beta -treated endothelial cells. These results indicated that the synthesis of the sialyl Lewis X determinants that were functionally active as E-selectin ligands was mainly mediated by Fuc-T VII in these lymphoid cells. On the other hand, the message of Fuc-T IV showed no significant change in the transfectant clones, and the surface expression of the Lewis X antigen as well as the enzymatic activity of alpha 1right-arrow3 fucosyltransferase against non-sialylated type 2 chain substrate was well preserved. The clear contrast between the diminished expression of sialyl Lewis X and the conserved manifestation of Lewis X in the transfectant clones suggested that the synthesis of sialyl Lewis X and that of Lewis X are independently regulated by different fucosyltransferases in human lymphoid cells. Fuc-T VII must be involved in the synthesis of sialyl Lewis X, while the synthesis of Lewis X is mediated by an enzyme other than Fuc-T VII, most probably Fuc-T IV.


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