Abstract
HNK-1 carbohydrate is highly expressed in the nervous system and is involved in higher-order brain functions such as learning and memory. HNK-1 has a unique structure with sulfated glucuronic acid attached to the non-reducing end of N-acetyllactosamine (HSO3-3GlcA β1-3Gal β1-4GlcNAc-). Two glucuronyltransferases and a sulfotransferase play key roles in its biosynthesis. We focused on how these enzyme activities are regulated in terms of HNK-1 expression. We revealed that the transferases form a hetero-complex for the efficient biosynthesis and that the activity is regulated by well-controlled intracellular localization. These facts indicate that HNK-1 expression is strictly regulated through multiple control mechanisms of the biosynthetic enzyme activity.
Original language | English |
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Pages (from-to) | 194-199 |
Number of pages | 6 |
Journal | Trends in Glycoscience and Glycotechnology |
Volume | 22 |
Issue number | 126 |
DOIs | |
Publication status | Published - 2010 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Organic Chemistry