Foxall C, Watson S R, Dowbenko D, Fennie C, Lasky L A, Kiso M, Hasegawa A, Asa D, Brandley B K
Glycomed, Inc., Alameda, California 94501.
J Cell Biol. 1992 May;117(4):895-902. doi: 10.1083/jcb.117.4.895.
The selectins (lectin-EGF-complement binding-cell adhesion molecules [LEC-CAMs]) are a family of mammalian receptors implicated in the initial interactions between leukocytes and vascular endothelia, leading to lymphocyte homing, platelet binding, and neutrophil extravasation. The three known selectins, L-selectin (leukocyte adhesion molecule-1 [LECAM-1]), E-selectin (endothelial-leukocyte adhesion molecule-1 [ELAM-1]), and P-selectin (GMP-140) share structural features that include a calcium-dependent lectin domain. The sialyl Lewis(x) carbohydrate epitope has been reported as a ligand for both E- and P-selectins. Although L-selectin has been demonstrated to bind to carbohydrates, structural features of potential mammalian carbohydrate ligand(s) have not been well defined. Using an ELISA developed with a sialyl Lewis(x)-containing glycolipid and an E-selectin-IgG chimera, we have demonstrated the direct binding of the L-selectin-IgG chimera to sialyl Lewis(x). This recognition was calcium dependent, and could be blocked by Mel-14 antibody but not by other antibodies. Recognition was confirmed by the ability of cells expressing the native L-selectin to adhere to immobilized sialyl Lewis(x). These data suggest that the sialyl Lewis(x) oligosaccharide may form the basis of a recognition domain common to all three selectins.
选择素（凝集素-表皮生长因子-补体结合细胞粘附分子[LEC-CAMs]）是一类哺乳动物受体，参与白细胞与血管内皮细胞之间的初始相互作用，导致淋巴细胞归巢、血小板结合和中性粒细胞渗出。已知的三种选择素，L-选择素（白细胞粘附分子-1[LECAM-1]）、E-选择素（内皮细胞-白细胞粘附分子-1[ELAM-1]）和P-选择素（GMP-140）具有共同的结构特征，包括一个钙依赖性凝集素结构域。唾液酸化路易斯（x）碳水化合物表位已被报道为E-选择素和P-选择素的配体。尽管L-选择素已被证明能与碳水化合物结合，但潜在的哺乳动物碳水化合物配体的结构特征尚未明确界定。利用一种用含唾液酸化路易斯（x）的糖脂和E-选择素-IgG嵌合体开发的酶联免疫吸附测定（ELISA），我们证明了L-选择素-IgG嵌合体与唾液酸化路易斯（x）的直接结合。这种识别是钙依赖性的，并且可以被Mel-14抗体阻断，但不能被其他抗体阻断。通过表达天然L-选择素的细胞粘附于固定化唾液酸化路易斯（x）的能力证实了这种识别。这些数据表明，唾液酸化路易斯（x）寡糖可能构成所有三种选择素共同的识别结构域的基础。
