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J Biol Chem, Vol. 274, Issue 43, 30557-30562, October 22, 1999

Molecular Cloning of Brain-specific GD1 Synthase (ST6GalNAc V) Containing CAG/Glutamine Repeats

Tetsuya Okajima, Satoshi Fukumoto^§, Hiromi Ito^¶, Makoto Kiso^¶, Yoshio Hirabayashi, Takeshi Urano, Keiko Furukawa, and Koichi Furukawa

From the  Department of Biochemistry II, Nagoya University School of Medicine, Tsurumai, Nagoya 466-0065, ^§ the Department of Pediatric Dentistry, Nagasaki University School of Dentistry, Sakamoto, Nagasaki 852-8501, the ^¶ Department of Applied Bio-organic Chemistry, Faculty of Agriculture, Gifu University, Gifu 501-1193, and the  Laboratory for Cellular Glycobiology, Frontier Research Program (RIKEN), Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan

A novel member of the mouse CMP-NeuAc: -N-acetylgalactosaminide 2,6-sialyltransferase (ST6GalNAc) subfamily, designated ST6GalNAc V, was identified by BLAST analysis of expressed sequence tags. The sequence of the longest cDNA clone of ST6GalNAc V encoded a type II membrane protein with 8 amino acids comprising the cytoplasmic domain, 21 amino acids comprising the transmembrane region, and 306 amino acids comprising the catalytic domain. The predicted amino acid sequence showed homology to the previously cloned ST6GalNAc III and IV, with common amino acid sequences in sialyl motifs L and S among these three enzymes. Eleven CAG repeats were found in the stem region. A fusion protein with protein A and extracts from L cells transfected with ST6GalNAc V in a expression vector showed enzyme activity of 2,6-sialyltransferase almost exclusively for GM1b, but not toward glycoproteins. Sialidase treatment and thin layer chromatography immunostaining revealed that the product was GD1. Northern blotting revealed that three transcripts of the gene were expressed specifically in brain tissues. It is concluded that this enzyme is involved in the synthesis of GD1 in the nervous tissues, and the CAG repeats may have implications in neurodegenerative diseases.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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