Misevic G N, Burger M M
Friedrich Miescher-Institut, Basel, Switzerland.
J Cell Biochem. 1990 Aug;43(4):307-14. doi: 10.1002/jcb.240430403.
A proteoglycan-like aggregation factor from the marine sponge Microciona prolifera (MAF) mediates cell-cell recognition via a cell-binding and a self-association domain. After repetitive and prolonged treatment of MAF with glycopeptide-N-glycosidase (PNGase) the specific binding of MAF to homotypic cells was decreased by 72%. Polyacrylamide gel electrophoresis and gel filtration analysis of such PNGase digests showed that: 1) the enzyme released a single glycan type of Mr = 6 X 10(3) (G-6) from MAF, 2) 1 mole of MAF contains at least 830 moles of N-linked chains of G-6 glycan. The correlation between the loss of the binding activity of MAF and the extent of the release of the repetitive G-6 polysaccharide strongly suggests its involvement in MAF-cell association via highly polyvalent interactions.
来自海洋海绵类动物扁海绵（MAF）的一种类蛋白聚糖聚集因子通过细胞结合域和自缔合域介导细胞间识别。用糖肽 - N - 糖苷酶（PNGase）对MAF进行重复且长时间处理后，MAF与同型细胞的特异性结合降低了72%。对此类PNGase消化产物进行的聚丙烯酰胺凝胶电泳和凝胶过滤分析表明：1）该酶从MAF中释放出一种单一类型的聚糖，其相对分子质量为6×10³（G - 6）；2）1摩尔MAF至少含有830摩尔G - 6聚糖的N - 连接链。MAF结合活性的丧失与重复的G - 6多糖释放程度之间的相关性强烈表明，它通过高度多价相互作用参与MAF与细胞的缔合。
