The monoclonal antibody TER-119 recognizes a molecule associated with glycophorin A and specifically marks the late stages of murine erythroid lineage
The monoclonal antibody TER-119 recognizes a molecule associated with glycophorin A and specifically marks the late stages of murine erythroid lineage
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DOI：
10.1046/j.1365-2141.2000.02037.x
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发表时间：
2000-05-01
影响因子：
6.5
通讯作者：
Katsura, Y
中科院分区：
文献类型：
--
作者：
Kina, T;Ikuta, K;Katsura, Y
研究了鼠单克隆抗体TER-119的抗原特异性。在成年小鼠中，TER-119与成熟红细胞、20-25%的骨髓细胞和2-3%的脾细胞反应，但不与胸腺细胞或淋巴结细胞反应。在胎儿造血组织中，30-40%的第10天卵黄囊细胞、80-90%的第14天胎肝细胞和40-50%的新生儿肝细胞与TER-119反应。成人骨髓中的TER-119（+）细胞表达显著水平的CD 45，但不表达髓样（Mac-1，Gr-1）或B细胞（B220）标记物。对分离的TER-119（+）细胞的形态学检查和造血集落形成试验表明，TER-119与从早期原红细胞到成熟红细胞的分化阶段的红系细胞反应，但不与具有典型红系原始细胞形成单位（BFU-E）和红系集落形成单位（CFU-E）活性的细胞反应。红白血病细胞系即使在用二甲基亚砜刺激后也不表达TER-119抗原。TER-119从红细胞膜上免疫沉淀出分子量为110 kDa、60 kDa、52 kDa和32 kDa的蛋白条带，而在Western blot分析中，TER-119仅检测到分子量为52 kDa的条带。进一步的分子和细胞分析表明，TER-119抗原是一种与细胞表面血型糖蛋白A相关的分子，但不与血型糖蛋白A本身相关。
The antigen specificity of a rat monoclonal antibody TER-119 was investigated. In adult mice, TER-119 reacted with mature erythrocytes, 20-25% of bone marrow cells and 2-3% of spleen cells but not with thymocytes nor lymph node cells. In fetal haematopoietic tissues, 30-40% of d 10 yolk sac cells, 80-90% of d 14 fetal liver cells and 40-50% of newborn liver cells were reactive with TER-119. TER-119(+) cells in adult bone marrow ex-pressed significant levels of CD45 but not myeloid (Mac-1, Gr-1) or B-cell (B220) markers. Morphological examination and haematopoietic colony-forming assays for isolated TER-119(+) cells revealed that TER-119 reacts with erythroid cells at differentiation stages from early proerythroblast to mature erythrocyte, but not with cells showing typical erythroid blast-forming unit (BFU-E) and erythroid colony-forming unit (CFU-E) activities. Erythroleukaemia cell lines do not express the TER-119 antigen even after stimulation with dimethylsulphoxide. TER-119 immunoprecipitated protein bands with molecular masses of 110 kDa, 60 kDa, 52 kDa and 32 kDa from erythrocyte membrane, whereas only a 52-kDa band was detected by TER-119 in Western blot analysis. Further molecular and cellular analyses indicated that the TER-119 antigen is a molecule associated with cell-surface glycophorin A but not with glycophorin A itself.