Glycosphingolipid carriers of carbohydrate antigens of human myeloid cells recognized by monoclonal antibodies.
Glycosphingolipid carriers of carbohydrate antigens of human myeloid cells recognized by monoclonal antibodies.
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单克隆抗体识别的人骨髓细胞碳水化合物抗原的鞘糖脂载体。
DOI：
10.1016/0167-4889(85)90106-5
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Feizi,T
中科院分区：
文献类型：
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作者：
Uemura,K;Macher,BA;DeGregorio,M;Scudder,P;Buehler,J;Knapp,W;Feizi,T
六种单克隆抗体与已知的特异性的碳水化合物抗原i，X或Y，和七个抗髓样抗体（决定簇未知）选择其不同的反应模式与人白细胞进行了测试，在色谱结合试验与髓样细胞糖脂反应来自正常人粒细胞和慢性髓性白血病细胞。抗原性仅在微量糖脂上发现，这些糖脂用地衣酚-硫酸染色几乎检测不到或根本检测不到。其中，中性鞘糖脂与抗i抗体Den结合，经色谱分析为神经酰胺八糖，Galβ1 → 4GlcNAcβ1 → 3Galβ1 → 4GlcNAc β1 → 3Galβ1 → 4GlcNAc β 1 → 3Gal β1 → 4Glc-Cer。结果表明，中性鞘糖脂中含有6 ~ 10个以上单糖，分别为Galβ1 → 4（Fucα1 → 3）GlcNAc和Fucα1 → 2Galβ1 → 4（Fucα1 → 3）GlcNAc。此外，在髓样细胞糖脂中检测到三种新类型的碳水化合物特异性。两个与中性糖脂相关：第一个由抗髓样抗体Vim-1和Vim-10识别，在具有六个或更多个单糖的糖脂上表达，第二个由Vim-8识别，在具有十个以上单糖的糖脂上表达。第三种特异性，由抗髓系抗体Vim-2识别，在具有聚-N-乙酰乳糖胺型骨架结构的缓慢迁移唾液酸糖脂上表达，该结构易被内切-β-半乳糖苷酶降解。因此，我们的结论是，i和Y抗原之间发生的糖脂的正常髓细胞和慢性髓细胞性白血病细胞和高比例的杂交瘤抗体提出了针对分化抗原的髓细胞是针对碳水化合物结构。
Six monoclonal antibodies with known specificities for the carbohydrate antigens i, X or Y, and seven anti-myeloid antibodies (determinants unknown) selected for their differing reaction patterns with human leucocytes were tested in chromatogram binding assays for reactions with myeloid cell glycolipids derived from normal human granulocytes and chronic myelogenous leukemia cells. Antigenicities were found exclusively on minor glycolipids which were barely or not at all detectable with orcinol-sulphuric acid stain. Among these, a neutral glycosphingolipid bound the anti-i antibody Den and chromatographed as the ceramide octasaccharide, Galβ1 → 4GlcNAcβ1 → 3Galβ1 → 4GlcNAcβ1 → 3Galβ1 → 4GlcNAcβ1 → 3Galβ1 → 4Glc-Cer. Several species of neutral glycosphingolipids with six to more than ten monosaccharides were detected which carry the X antigen and others the Y antigen: Galβ1 → 4(Fucα1 → 3)GlcNAc and Fucα1 → 2Galβ1 → 4(Fucα1 → 3)GlcNAc, respectively. In addition, three new types of carbohydrate specificities were detected among the myeloid cell glycolipids. Two were associated with neutral glycolipids: the first, recognised by anti-myeloid antibodies VIM-1 and VIM-10, was expressed on a distinct set of glycolipids with six or more monosaccharides, and the second, recognized by VIM-8, was expressed on glycolipids with more than ten monosaccharides. The third specificity, recognised by the anti-myeloid antibody VIM-2, was expressed on slow migrating sialoglycolipids with backbone structures of the poly-N-acetyllactosamine type that are susceptible to degradation with endo-β-galactosidase. Thus, we conclude that the i and Y antigens occur among the glycolipids of normal myeloid and chronic myelogenous leukemia cells and that a high proportion of hybridoma antibodies raised against differentiation antigens of myeloid cells are directed at carbohydrate structures.