Specificity of fucose transfer to GlcNAc residues of extended chain neolacto-series glycolipids catalyzed by human alpha 1-->3fucosyltransferases: effect of the lipidic environment on the myeloid enzyme form.
Specificity of fucose transfer to GlcNAc residues of extended chain neolacto-series glycolipids catalyzed by human alpha 1-->3fucosyltransferases: effect of the lipidic environment on the myeloid enzyme form.
复制标题
由人α1→3岩藻糖基转移酶催化的岩藻糖转移至延长链新乳糖系列糖脂的GlcNAc残基的特异性：脂质环境对骨髓酶形式的影响。
DOI：
10.1006/abbi.1993.1132
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发表时间：
1993
影响因子：
3.9
通讯作者：
Macher,BA
中科院分区：
文献类型：
--
作者：
Holmes,EH;Macher,BA
多种α1 → 3岩藻糖基转移酶存在于人类基因组中，其中刘易斯（FucT-ITI）、髓样（FucTIV）和血浆（FucT-V）酶形式受到最大关注。本文研究了人早幼粒细胞白血病HL-60细胞髓系α1 → 3岩藻糖基转移酶的受体性质。岩藻糖转移到糖脂受体被洗涤剂G-3634-A或牛磺脱氧胆酸盐激活，导致有效转移到中性受体，但转移到唾液酸化受体的能力较差，这是骨髓型酶的特征。岩藻糖转移到nLc 6产生单和二岩藻糖基衍生物在两种洗涤剂条件下。通过TLC免疫染色和快速原子轰击-质谱分析分离并分析nLc 6单岩藻糖基产物。发现G3634-A单岩藻糖基产物仅由V3 FucnLc 6组成，而牛磺脱氧胆酸盐的产物被确定为III 3FucnLc 6和V3 FucnLc 6以接近相等的量的混合物。使用磷脂酶活化的反应产物分析表明，磷脂酰乙醇胺和磷脂酰肌醇的行为与G-3634-A相似。相比之下，磷脂酰甘油产生的结果类似的牛磺脱氧胆酸盐。岩藻糖转移到VI 3 NeuAcnLc 6产生约75%的产物作为IIIGlcNAc单岩藻糖基衍生物，而不管使用的去污剂或磷脂条件如何。使用牛磺脱氧胆酸盐对来自科洛205细胞的由刘易斯酶催化的岩藻糖转移至nLc 6的分析仅产生IIIGlcNAc单岩藻糖基衍生物，而G-3634-A的主要产物是V-GlcNAc岩藻糖基化。相反，在两种条件下，用来自NCI-H69细胞的酶仅发现V-GlcNAc单岩藻糖基化产物。结果表明，人α1 → 3岩藻糖基转移酶之间存在细微的内在差异。通过膜环境的性质对酶特异性的调节可以参与不同细胞表面抗原表达的调节。
Multiple α1 → 3fucosyltransferases occur in the human genome of which the Lewis (FucT-ITI), myeloid (FucTIV), and plasma (FucT-V) enzyme forms have received the greatest attention. In this paper, the acceptor properties of the myeloid α1 → 3fucosyltransferase from human promyelocytic leukemia HL-60 cells have been studied. Fucose transfer into glycolipid acceptors was activated by detergents G-3634-A or taurodeoxycholate resulting in efficient transfer to neutral acceptors but poor transfer to sialylated acceptors, characteristic of the myeloid-type enzyme. Fucose transfer to nLc6yielded both mono- and difucosyl derivatives under both detergent conditions. The nLc6monofucosyl products were isolated and analyzed by TLC immunostaining and fast atom bombardment-mass spectroscopy analysis. The G3634-A monofucosyl product was found to be composed solely of V3FucnLc6, whereas that with taurodeoxycholate was determined to be a mixture of III3FucnLc6and V3FucnLc6in near equal amounts. Analysis of reaction products using enzyme activation by phospholipids indicated that phosphatidylethanolamine and phosphatidylinositol behaved similarly to G-3634-A. In contrast, phosphatidylglycerol yielded results similar those of taurodeoxycholate. Fucose transfer to VI3NeuAcnLc6yielded approximately 75% of the product as the IIIGlcNAc monofucosyl derivative regardless of the detergent or phospholipid condition used. Analysis of fucose transfer to nLc6catalyzed by the Lewis enzyme from Colo 205 cells using taurodeoxycholate yielded solely the IIIGlcNAc monofucosyl derivative, whereas the predominant product with G-3634-A was V-GlcNAc fucosylated. In contrast, under both conditions only the V-GlcNAc monofucosylation product was found with the enzyme from NCI-H69 cells. The results indicate that subtle intrinsic differences exist between human α1 → 3fucosyltransferases. Modulation of enzyme specificity via the nature of the membrane environment could participate in regulation of expression of distinct cell surface antigens.