Goelz S E, Hession C, Goff D, Griffiths B, Tizard R, Newman B, Chi-Rosso G, Lobb R
Biogen, Inc., Cambridge, Massachusetts 02142.
Cell. 1990 Dec 21;63(6):1349-56. doi: 10.1016/0092-8674(90)90430-m.
The LECCAMs are a family of cell adhesion molecules implicated in certain inflammatory processes. ELAM-1, a LECCAM found on the surface of activated endothelial cells, can mediate adhesion of neutrophils, monocytes, and certain cell lines to endothelial cells in vitro. No ligand for any LECCAM has yet been fully characterized. Here we report the cloning of a cDNA, ELFT (ELAM-1 ligand fucosyltransferase), that can confer ELAM-1 binding activity when transfected into nonbinding cell lines. ELFT encodes a 46 kd protein that has alpha(1,3)fucosyltransferase activity, suggesting that a fucosylated carbohydrate structure is an essential component of the ELAM-1 ligand. Furthermore, ELFT is expressed specifically in cell types that bind to ELAM-1, suggesting that this enzyme is an important regulator of inflammatory events in vivo.
LECCAM是一族与某些炎症过程相关的细胞粘附分子。ELAM-1是一种在活化内皮细胞表面发现的LECCAM，它在体外可介导嗜中性粒细胞、单核细胞及某些细胞系与内皮细胞的粘附。尚未完全鉴定出任何LECCAM的配体。在此我们报道一种cDNA即ELFT（ELAM-1配体岩藻糖基转移酶）的克隆，当将其转染到无结合活性的细胞系中时可赋予ELAM-1结合活性。ELFT编码一种具有α(1,3)岩藻糖基转移酶活性的46kd蛋白，提示岩藻糖化碳水化合物结构是ELAM-1配体的一个重要组成部分。此外，ELFT特异性地在与ELAM-1结合的细胞类型中表达，提示该酶是体内炎症事件的一个重要调节因子。
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