Branched Sialylated N-glycans Are Accumulated in Brain Synaptosomes and Interact with Siglec-H.

IF 2 4区 生物学 Q4 CELL BIOLOGY
Cell structure and function Pub Date : 2018-08-25 Epub Date: 2018-07-20 DOI:10.1247/csf.18009
Mai Handa-Narumi, Takeshi Yoshimura, Hiroyuki Konishi, Yuko Fukata, Yoshiyuki Manabe, Katsunori Tanaka, Guang-Ming Bao, Hiroshi Kiyama, Koichi Fukase, Kazuhiro Ikenaka
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引用次数: 10

Abstract

Proper N-glycosylation of proteins is important for normal brain development and nervous system function. Identification of the localization, carrier proteins and interacting partners of N-glycans is essential for understanding the roles of glycoproteins. The present study examined the N-glycan A2G'2F (Galβ1-3GlcNAcβ1-2Manα1-6[Galβ1-3GlcNAcβ1-2Manα1-3]Manβ1-4GlcNAcβ1-4[Fucα1-6]GlcNAc-). A2G'2F has a branched sialic acid structural feature, and branched sialylated A2G'2F is a major N-glycan in the mouse brain. Its expression in the mouse brain increases during development, suggesting that branched sialylated N-glycans play essential roles during brain development. However, the carrier proteins, interacting partners and localization of branched sialylated N-glycans remain unknown. We previously improved our method for analyzing N-glycans from trace samples, and here we succeeded in detecting A2G'2F in small fragments excised from the two-dimensional electrophoresis gels of subcellular fractionated mouse brain proteins. A2G'2F was accumulated in mouse brain synaptosomes. We identified calreticulin as one of the candidate A2G'2F carriers and found calreticulin expression in both the endoplasmic reticulum and synaptosomal fractions. Calreticulin was observed in dendritic spines of cultured cortical neurons. Synthesized branched sialylated glycan clusters interacted with sialic acid-binding immunoglobulin-like lectin H (Siglec-H), which is known to be a microglia-specific molecule. Taken together, these results suggest that branched sialylated A2G'2F in synaptosomes plays a role in the interaction of dendritic spines with microglia.Key words: N-glycan, subcellular fractionation, calreticulin, dendritic spine, Siglec-H.

分支唾液化n -聚糖在脑突触体中积累并与siglece - h相互作用。
适当的蛋白质n -糖基化对正常的大脑发育和神经系统功能至关重要。鉴定n -聚糖的定位、载体蛋白和相互作用伙伴对了解糖蛋白的作用至关重要。本研究检测了n -聚糖A2G'2F (Galβ1-3GlcNAcβ1-2Manα1-6[Galβ1-3GlcNAcβ1-2Manα1-3]Manβ1-4GlcNAcβ1-4[Fucα1-6]GlcNAc-)。A2G'2F具有支链唾液酸结构特征,支链唾液化的A2G'2F是小鼠脑内主要的n -聚糖。其在小鼠大脑中的表达在发育过程中增加,表明支链唾液化n -聚糖在大脑发育过程中起重要作用。然而,支链唾液化n -聚糖的载体蛋白、相互作用伙伴和定位仍然未知。我们之前改进了从痕量样品中分析n -聚糖的方法,在这里我们成功地检测了从亚细胞分离小鼠脑蛋白的二维电泳凝胶中切除的小片段中的A2G'2F。A2G'2F在小鼠脑突触体中积累。我们发现钙网蛋白是A2G'2F的候选载体之一,在内质网和突触体中均有钙网蛋白的表达。在培养的皮质神经元树突棘中观察到钙网蛋白。合成的支链唾液化聚糖簇与唾液酸结合免疫球蛋白样凝集素H (siglecl -H)相互作用,这是一种已知的小胶质细胞特异性分子。综上所述,这些结果表明突触体中分支唾液化的A2G'2F在树突棘与小胶质细胞的相互作用中起作用。关键词:n -聚糖,亚细胞分离,钙网蛋白,树突棘,siglece - h
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来源期刊
Cell structure and function
Cell structure and function 生物-细胞生物学
CiteScore
2.50
自引率
0.00%
发文量
6
审稿时长
>12 weeks
期刊介绍: Cell Structure and Function is a fully peer-reviewed, fully Open Access journal. As the official English-language journal of the Japan Society for Cell Biology, it is published continuously online and biannually in print. Cell Structure and Function publishes important, original contributions in all areas of molecular and cell biology. The journal welcomes the submission of manuscripts on research areas such as the cell nucleus, chromosomes, and gene expression; the cytoskeleton and cell motility; cell adhesion and the extracellular matrix; cell growth, differentiation and death; signal transduction; the protein life cycle; membrane traffic; and organelles.
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