Molecular cloning of brain-specific GD1α synthase (ST6GalNAc V) containing CAG/glutamine repeats

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

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76 Citations (Scopus)


A novel member of the mouse CMP-NeuAc: β-N-acetyl-galactosaminide α2,6-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 α2,6- sialyltransferase almost exclusively for GM1b, but not toward glycoproteins. Sialidase treatment and thin layer chromatography immunostaining revealed that the product was GD1α 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 GD1α in the nervous tissues, and the CAG repeats may have implications in neurodegenerative diseases.

Original languageEnglish
Pages (from-to)30557-30562
Number of pages6
JournalJournal of Biological Chemistry
Issue number43
Publication statusPublished - 1999 Oct 22


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