Identification of nucleolin as a new L-selectin ligand
Identification of nucleolin as a new L-selectin ligand
复制标题
DOI：
10.1042/0264-6021:3600531
复制
发表时间：
2001-12-15
影响因子：
4.1
通讯作者：
Tauber, R
中科院分区：
文献类型：
--
作者：
Harms, G;Kraft, R;Tauber, R
除了白细胞-内皮细胞相互作用，粘附分子L-选择素介导的同型粘附的白细胞在招募过程中在急性炎症部位，以及造血祖细胞在造血过程中的细胞间粘附。有证据表明，除了P-选择素糖蛋白配体-1，其他尚未鉴定的蛋白质在人白细胞和造血祖细胞上作为L-选择素配体起作用。在本研究中，我们表明：（i）通过亲和层析L-选择素-琼脂糖;（ii）通过蛋白质鉴定使用MS;和（iii）通过共价细胞表面标记与sulphosuccinimidyl-2-（biotinamido）ethyl-1，3-dithiopropionate的多功能核蛋白核仁素是部分暴露在细胞表面上，是L-选择素在人类白细胞和造血祖细胞的配体。
Apart from leucocyte-endothelial interactions, the adhesion molecule L-selectin mediates the homotypic adhesion of leucocytes during recruitment at sites of acute inflammation, as well as intercellular adhesion of haematopoietic progenitor cells during haematopoiesis. There is evidence that, in addition to P-selectin glycoprotein ligand-1, other as-yet-un identified proteins function as L-selectin ligands on human leucocytes and haematopoietic progenitor cells. In the present study, we show: (i) by affinity chromatography on L-selectin-agarose; (ii) by protein identification using MS; and (iii) by covalent cell-surface labelling with sulphosuccinimidyl-2- (biotinamido) ethyl-1,3-dithiopropionate that the multifunctional nuclear protein nucleolin is partly exposed on the cell surface, and is a ligand of L-selectin in human leucocytes and haematopoietic progenitor cells.