Lectin binding to neural crest cells. Changes of the cell surface during differentiation in vitro
Lectin binding to neural crest cells. Changes of the cell surface during differentiation in vitro
复制标题
凝集素与神经嵴细胞结合。
作者：
M. Sieber;A. M. Cohen
为了检测细胞表面碳水化合物的可能变化，在体外培养的神经脊细胞分化过程中，不同时间应用荧光凝集素。随着脊细胞发育为黑素细胞和肾上腺素能细胞，几种凝集素的结合方式和强度发生了变化。在整个培养过程中，相当数量的刀豆蛋白A(ConA)和小麦胚凝集素(WGA)结合到所有无色素细胞上。然而，黑素细胞与这些凝集素的结合要少得多。与ConA和WGA不同，大豆凝集素(SBA)只在发育后期与无色素细胞结合，组织化学检测到儿茶酚胺的时候。神经氨酸酶可诱导较年轻培养的细胞结合SBA。然而，即使用神经氨酸酶处理，黑素细胞也不能结合可检测到的SBA。SBA结合部位通常集中在细胞质延伸和相邻细胞之间的接触点，即使当受体的流动性受到细胞预先固定或0℃下凝集素吸附的限制时，这三种凝集素都特别大量地结合到类似神经纤维的细胞突起上。
To examine possible changes in cell surface carbohydrates, fluorescent lectins were applied at various times during differentiation of neural crest cells in vitro. The pattern and intensity of binding of several lectins changed as the crest cells developed into melanocytes and adrenergic cells. Considerable amounts of concanavalin A (Con A) and wheat germ agglutinin (WGA) bound to all unpigmented cells throughout the culture period. Melanocytes, however, bound much less of these lectins. Soy bean agglutinin (SBA), unlike Con A and WGA, only bound later in development to unpigmented cells at about the time when catecholamines were detected histochemically. Binding of SBA could be induced in younger cultures by pretreating the cells with neuraminidase. Melanocytes, however, did not bind detectable amounts of SBA even if treated with neuraminidase. The SBA-binding sites were often concentrated on cytoplasmic extensions and on contact points between neighboring cells, even when receptor mobility was restricted by prefixation of the cells or adsorption of lectin at 0 degrees C. All three lectins bound to cell processes resembling nerve fibers in particularly high amounts.