Fukushi Y, Hakomori S, Nudelman E, Cochran N
J Biol Chem. 1984 Apr 10;259(7):4681-5.
A series of glycolipids having the X determinant (Gal beta 1----4 [Fuc alpha----3]GlcNAc) at the terminus and a fucosyl alpha 1----3 residue at the internal GlcNAc residue have been isolated and characterized from tumor tissues (Hakomori, S., Nudelman, E., Levery, S.B., and Kannagi, R. (1984) J. Biol. Chem. 259, 4672-4680. A series of monoclonal antibodies that differentially recognize glycolipids with mono-, di-, and trifucosylated type 2 chain have been isolated and characterized. The antibody FH4 shows a remarkable preferential reactivity towards di-/or trifucosylated type 2 chain, i.e. it does not react with monofucosylated structures, including lactofucopentaosyl (III) ceramide (III3FucnLc4), monofucosyl neolactonorhexaosylceramide (y2, V3FucnLc6), and monofucosyl neolactonoroctaosylceramide (Z1, VII3FucnLc8), but reacts well with di- and trifucosylated type 2 chain structures such as difucosyl neolactonorhexaosylceramide (III3V3Fuc2nLc6) and trifucosyl neolactonoroctaosylceramide (III3V3VII3Fuc3nLc8). Two other monoclonal antibodies, FH5 and ACFH18, preferentially react with trifucosylated type 2 chain structure (III3V3VII3Fuc3nLc8), although cross-reactivity with difucosylated type 2 chain (III3V3Fuc2nLc6) was observed. They showed a minimal cross-reaction with monofucosylated type 2 chain. In contrast, the antibody FH1 does not react with III3FucnLc4 but reacts with V3FucnLc6, III3V3Fuc2nLc6, and III3V3VII3Fuc3nLc8. Two monoclonal antibodies, FH2 and FH3, do not discriminate among various glycolipids having fucosylated type 2 chain, and their reactivities are essentially similar to previously established antibodies directed to the X determinant, such as anti-SSEA-1, WGHS 29, VEP8 and 9, My-1, etc. This series of antibodies will be useful to detect the specific type of glycolipid with fucosylated type 2 chain accumulating in human cancer and in undifferentiated cells.
一系列在末端具有X决定簇（Galβ1----4 [Fucα----3]GlcNAc）且在内侧GlcNAc残基上有岩藻糖基α1----3残基的糖脂已从肿瘤组织中分离并鉴定（羽田盛，S.，努德尔曼，E.，勒弗里，S.B.，和金谷，R.（1984年）《生物化学杂志》259，4672 - 4680）。一系列能分别识别单岩藻糖基化、双岩藻糖基化和三岩藻糖基化2型链糖脂的单克隆抗体已被分离并鉴定。抗体FH4对双岩藻糖基化/或三岩藻糖基化2型链表现出显著的优先反应性，即它不与单岩藻糖基化结构反应，包括乳岩藻五糖基（III）神经酰胺（III3FucnLc4）、单岩藻糖基新乳糖神经六糖基神经酰胺（γ2，V3FucnLc6）和单岩藻糖基新乳糖神经八糖基神经酰胺（Z1，VII3FucnLc8），但与双岩藻糖基化和三岩藻糖基化2型链结构如双岩藻糖基新乳糖神经六糖基神经酰胺（III3V3Fuc2nLc6）和三岩藻糖基新乳糖神经八糖基神经酰胺（III3V3VII3Fuc3nLc8）反应良好。另外两种单克隆抗体FH5和ACFH18优先与三岩藻糖基化2型链结构（III3V3VII3Fuc3nLc8）反应，尽管观察到与双岩藻糖基化2型链（III3V3Fuc2nLc6）有交叉反应。它们与单岩藻糖基化2型链的交叉反应最小。相比之下，抗体FH1不与III3FucnLc4反应，但与V3FucnLc6、III3V3Fuc2nLc6和III3V3VII3Fuc3nLc8反应。两种单克隆抗体FH2和FH3不能区分具有岩藻糖基化2型链的各种糖脂，它们的反应性与先前建立的针对X决定簇的抗体如抗SSEA - 1、WGHS 29、VEP8和9、My - 1等基本相似。这一系列抗体将有助于检测在人类癌症和未分化细胞中积累的具有岩藻糖基化2型链的特定类型糖脂。
