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Glycobiology Advance Access published online on January 15, 2009
Glycobiology, doi:10.1093/glycob/cwp003
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Molecular insights into β-galactoside {alpha}2,6-sialyltransferase secretion in vivo

Shinobu Kitazume1,8, Ritsuko Oka1, Kazuko Ogawa1, Satoshi Futakawa1,9, Yoshiaki Hagiwara2, Hajime Takigawa3, Michio Kato4, Akinori Kasahara5, Eiji Miyoshi6, Naoyuki Taniguchi7 and Yasuhiro Hashimoto1,9

1 Glyco-chain Functions Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan, and CREST, Japan Science and Technology Agency, Kawaguchi, Saitama 560-0082, Japan
2 Department of Biological Sciences, Immuno-Biological Laboratories, 1091-1 Naka, Fujioka-shi, Gunma 375-0005, Japan
3 Department of Medicine, Teikyo University School of Medicine, Kaga 2-11-1, Itabashi, Tokyo 173-8605, Japan
4 Department of Gastroenterology, Osaka National Hospital, 2-1-14, Ho-enzaka, Chu-oku, Osaka 540-0006, Japan
5 Department of General Medicine, Osaka University Graduate School of Medicine, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan
6 Department of Molecular Biochemistry and Clinical Investigation, Osaka University Graduate School of Medicine, 1-7, Yamada-Oka, Osaka 565-0871, Japan
7 Department of Biochemistry, Osaka University Graduate School of Medicine, 1-7, Yamada-Oka, Osaka 565-0871, Japan

8 Current address and correspondence to: Shinobu Kitazume, Disease Glycomics Team, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. Tel: +81-48-467-9616; Fax: +81-48-467-9617; E-mail: shinobuk{at}riken.jp

Received on September 12, 2008; accepted on January 6, 2009

β-Galactoside {alpha}2,6-sialyltransferase (ST6Gal I), which is highly expressed in the liver, is mainly cleaved by Alzheimer's β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) and secreted into the serum. During our studies to elucidate the molecular mechanism underlying the cleavage-secretion of ST6Gal I, we hypothesized that plasma ST6Gal I may represent a sensitive biomarker for hepatopathological situations. In the present study, we used recently developed sandwich ELISA systems that specifically detect the soluble cleaved form of ST6Gal I in plasma. We found that the level of plasma ST6Gal I was increased in two different types of liver injury models. In zone 1 hepatocyte-injured rats, the level of plasma ST6Gal I was increased together with acute phase reactions. Meanwhile, in zone 3 hepatocyte-injured rats, ST6Gal I secretion was most likely triggered by oxidative stress. Taken together, we propose two possible mechanisms for the upregulation of plasma ST6Gal I in hepatopathological situations: one accompanied by acute phase reactions to increase hepatic ST6Gal I expression and the other triggered by oxidative stress in the liver. We also found that the serum level of ST6Gal I in hepatitis C patients was correlated with the activity of hepatic inflammation.

Key words: acute phase reaction / BACE1 / hepatitis / ST6Gal I / secretion

9 Current address: School of Medicine, Department of Biochemistry, Fukushima Medical University, Hikarigaoka-1, Fukushima-shi, Fukushima 960-1295, Japan.


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