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Glycobiology Advance Access originally published online on June 29, 2007
Glycobiology 2007 17(9):955-962; doi:10.1093/glycob/cwm066
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Characterization and role of fucose mutarotase in mammalian cells

Dongkyu Park2, Kyoung-Seok Ryu3, Dongwook Choi2, Jaechan Kwak2 and Chankyu Park1,2

2 Department of Life Sciences, Korea Advanced Institute of Science and Technology, 373-1, Guseong-Dong, Yuseong-Gu, Daejeon 305-701, Korea
3 Magnetic Resonance Team, Korea Basic Science Institute, 52 Yeoeun-Dong, Yuseong-Gu, Daejeon 305-333, Korea

1 To whom correspondence should be addressed: Tel: +82-42-869-2629; Fax: +82-42-869-2610; e-mail: ckpark{at}kaist.ac.kr

Received on April 19, 2007; revised on June 13, 2007; accepted on June 15, 2007

L-Fucose for mammalian glycosylation contains an ano- meric carbon atom generating {alpha}- and ß-L-fucoses. Based on sequence comparison of mouse and human homologs with the prokaryotic fucose mutarotases (FucU) characterized previously, we investigated their function in mammalian cells. By nuclear magnetic resonance (NMR) measurement with saturation difference analysis, the purified mammalian mutarotases were demonstrated to be involved in an interconversion between the two anomeric forms with comparable efficiency as that of the Escherichia coli FucU. The mouse gene was widely expressed in various tissues and cell lines, including kidney, liver, and pancreas, although expression was marginal in muscle and testis. By generating stably expressed cell lines for mutarotase genes in HepG2, it was shown that fucose incorporations into cellular proteins were increased as demonstrated by an incorporation of radiolabeled fucose into the cells. Furthermore, intracellular levels of GDP-L-fucose, measured with high performance liquid chromatography (HPLC), were enhanced by an overproduction of cellular mutarotase, which was reversed by gene silencing of mutarotase based on RNA interference. The results suggest that the mammalian mutarotase is functional in facilitated incorporation of fucose through the salvage pathway.

Key words: fucose / fucose incorporation / HPLC / mutarotase / NMR


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