Brain-specific expression of a novel human UDP-GalNAc :polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9)
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作者:
Toba, S
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机构:Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
Toba, S
Tenno, M
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机构:Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
Tenno, M
Konishi, M
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机构:Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
Konishi, M
Mikami, T
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机构:Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
Mikami, T
Itoh, N
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机构:Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
Itoh, N
Kurosaka, A
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Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, JapanKyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
Kurosaka, A
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机构:
[1] Kyoto Sangyo Univ, Fac Engn, Dept Biotechnol, Kita Ku, Kyoto 6038555, Japan
[2] Kyoto Univ, Grad Sch Pharmaceut Sci, Dept Biochem Genet, Sakyo Ku, Kyoto 6068501, Japan
We isolated cDNA coding for the ninth of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-T9) from human brain by the polymerase chain reaction. The polypeptide encoded by GalNAc-T9 contained the structural features characteristic of GalNAc transferases, such as a GT1 motif. a Gal/GalNAc transferase motif, (QXW)(3) repeats, and conserved His, Cys, and acidic amino acid residues. Northern blot analysis revealed the mRNA expression of the enzyme to be confined to the brain. The brain-specific expression of GalNAc-T9 suggested that this isozyme catalyzes O-glycosylation in the brain. (C) 2000 Elsevier Science B.V. All rights reserved.