The N-glycan profile of mouse myelin, a specialized central nervous system membrane.
The N-glycan profile of mouse myelin, a specialized central nervous system membrane.
复制标题
小鼠髓磷脂(一种特殊的中枢神经系统膜)的 N-聚糖谱。
DOI:
10.1111/j.1471-4159.2007.04823.x
复制
发表时间:
2007
影响因子:
4.7
通讯作者:
Pfeiffer,StevenE
中科院分区:
文献类型:
--
作者:
Ishii,Akihiro;Ikenaka,Kazuhiro;Pfeiffer,StevenE
Understanding the rich complement of sugar chains found in cellular membranes is impeded by the complexity of cell types and membrane diversity. To overcome this, we have analyzed theN‐linked sugar chain composition of the glycoproteins of CNS myelin, an elaboration of the plasma membranes of oligodendrocytes (OLs) that result in a multilamellar wrapping of neuronal axons, facilitating nerve conduction with dramatic savings of space and energy. Due to an usually high lipid to protein ratio, myelin can be separated readily from other heavier membranes on sucrose gradients and further fractionated into subdomains related to myelin structure and function, including compact myelin and myelin‐associated axolemmal membrane (Menonet al.2003). We analyzed these fractions forN‐linked sugar chains, using 2D HPLC following hydrazinolysis and pyridylamination. Our results indicate that compared with total brain homogenate, the amount ofN‐glycans is 1.3‐fold higher in the myelin‐associated axolemmal membranes, but it is 0.5‐fold less in CM. M5 [Manα1–3((Manα1–3)(Manα1–6)Manα1–6)Manβ1–4GlcNAcβ1–4GlcNAc] is the most abundant sugar chain in total brain homogenate, compact myelin, and myelin‐associated axolemma, constituting ∼20% of sugar chains. Although the types of sugar chains are similar among the fractions, their expression levels vary significantly. In addition to high mannose type oligosaccharides, the core fucosylated, biantennaryN‐glycans with bisectingN‐acetylglucosamine (GlcNAc) residue, A2G1(3)FB [Galβ1–4GlcNAcβ1–2Manα1–3(GlcNAcβ1–2Manα1–6)(GlcNAcβ1–4)Manβ1–4GlcNAcβ1–4(Fucα1–6)GlcNAc], A2G1(6)FB [GlcNAcβ1–2Manα1–3(Galβ1–4GlcNAcβ1–2Manα1–6)(GlcNAcβ1–4)Manβ1–4GlcNAcβ1–4 (Fucα1–6)GlcNAc] and BA‐1 [Manα1–3(GlcNAcβ1–2Manα1–6)(GlcNAcβ1–4)Manβ1–4GlcNAcβ1–4(Fucα1–6)GlcNAc], and A1(6)G0F [Manα1–3(GlcNAcβ1–2Manα1–6)Manβ1–4GlcNAcβ1–4(Fucα1–6) GlcNAc] are also present in relatively large proportions in compact myelin. We suggest that these differences may be related to myelin‐axolemmal function.