Distributions of glucuronyltransferases, GlcAT-P and GlcAT-S, and their target substrate, the HNK-1 carbohydrate epitope in the adult mouse brain with or without a targeted deletion of the GlcAT-P gene
Distributions of glucuronyltransferases, GlcAT-P and GlcAT-S, and their target substrate, the HNK-1 carbohydrate epitope in the adult mouse brain with or without a targeted deletion of the GlcAT-P gene
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DOI:
10.1016/j.brainres.2007.05.012
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发表时间:
2007-11-07
期刊:
影响因子:
2.9
通讯作者:
Oka, Shogo
中科院分区:
文献类型:
--
作者:
Inoue, Mitsuhiro;Kato, Keiko;Oka, Shogo
The HNK-1 carbohydrate epitope, a sulfated glucuronic acid at the non-reducing terminus of glycans, is expressed on glycoproteins and glycolipids and modulates neurite outgrowth and synaptic plasticity by affecting the adhesive and anti-adhesive properties. It is known that the HNK-1 carbohydrate is synthesized through two key enzymes, glucuronyltransferases (GlcAT-P and GlcAT-S). In the present study, we investigated the localization of GlcAT transcripts and HNK-1 carbohydrate in the adult mouse brain with or without GlcAT-P gene using in situ hybridization histochemistry and immunohistochemistry. Region-specific expression patterns of both GIcAT transcripts were observed. Strong expression of GIcAT-P and moderate expression of GlcAT-S were seen in neuronal cells of several nuclei of limbic-related regions and of the sensory system and the cerebellum. It was shown histologically that the localization of HNK-1 carbohydrate paralleled the pattern of expression of GlcAT transcripts in the brain. Additionally, the localization of HNK-1 carbohydrate was restricted partially in the brain of GlcAT-P -deficient mice, while the HNK-1 carbohydrate was widely distributed over most of the brain of wild-type mice. The present study provides a new framework for understanding the network constructed by the HNK-1 carbohydrate in the central nervous system. (c) 2007 Elsevier B.V. All rights reserved.