Comparison of the specificities of laminin, thrombospondin, and von Willebrand factor for binding to sulfated glycolipids.
Comparison of the specificities of laminin, thrombospondin, and von Willebrand factor for binding to sulfated glycolipids.
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层粘连蛋白、血小板反应蛋白和冯维勒布兰德因子与硫酸化糖脂结合的特异性的比较。
DOI：
10.1016/s0021-9258(19)62697-9
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Victor Ginsburg
中科院分区：
文献类型：
--
作者：
David;Roberts;C. N. Raop;Lance;Liottag;Harvey;GralnickB;Victor Ginsburg
黏附糖蛋白层粘连蛋白、凝血反应蛋白和血管性血友病因子对硫酸糖脂具有特异性和高亲和力。然而，这三种糖蛋白对硫酸单糖和多糖结合抑制的敏感性不同。肝素对凝血反应蛋白的结合有较强的抑制作用，而对层粘连蛋白和血管性血友病因子的结合只有较弱的抑制作用。岩藻聚糖强烈抑制层粘连蛋白和凝血反应蛋白的结合，但不抑制血管性血友病因子的结合。层粘连蛋白表现出单糖抑制的显著特异性，而凝血反应蛋白则没有。因此，硫酸盐酯的特定空间取向可能是三种蛋白质结合的主要决定因素。层粘连蛋白、血栓反应蛋白和血管性血友病因子对纯化的硫酸化鞘糖脂的相对结合亲和力也不同。这三种蛋白质强烈倾向于末端硫酸化的脂质，仅与硫酸化神经节三烷基神经酰胺结合，并在倒数第二半乳糖上有硫酸酯。血栓反应蛋白与半乳糖硫脂结合的亲和力最高，但与更复杂的硫脂结合的亲和力较弱，而血管性血友病因子倾向于半乳糖硫脂，但与各种硫酸糖脂结合的亲和力中等。层粘连蛋白的选择性也低于凝血反应蛋白，但对低硫脂浓度的检测不太敏感。1-5 pmol的半乳酰基硫脂可以用125i -血栓反应蛋白或125i -血管性血肿因子对高效薄层色谱分离的脂质进行染色来检测。研究了125i -血管性血友病因子作为检测组织提取物中硫酸化糖脂的试剂。大鼠肾脂含有5种表征的硫酸化糖脂：半乳糖基神经酰胺i3 -硫酸盐，乳糖基神经酰胺i3 -硫酸盐，神经节三酰神经酰胺i3 -硫酸盐，双硫酸化神经节三酰和神经节四酰神经酰胺。血管性血友病因子检测所有这些脂质以及其他几种次要的硫酸脂质。该技术可在多种人体组织（包括肾脏、红细胞和血小板）中检测到复杂的单硫酸脂质。
The adhesive glycoproteins laminin, thrombospondin, and von Willebrand factor bind specifically and with high affinity to sulfated glycolipids. These three glycoproteins differ, however, in their sensitivity to inhibition of binding by sulfated monosaccharides and polysaccharides. Heparin strongly inhibits binding of thrombospondin but only weakly inhibits binding of laminin and von Willebrand factor. Fucoidan strongly inhibits binding of both laminin and thrombospondin but not of von Willebrand factor. Laminin shows significant specificity for inhibition by monosaccharides, whereas thrombospondin does not. Thus, specific spacial orientations of sulfate esters may be primary determinants of binding for the three proteins. Laminin, thrombospondin, and von Willebrand factor also differ in their relative binding affinities for purified sulfated glycosphingolipids. The three proteins strongly prefer terminal-sulfated lipids and bind only weakly to sulfated gangliotriaosyl ceramide with a sulfate ester on the penultimate galactose. Thrombospondin binds with highest affinity to galactosyl sulfatide but only weakly to more complex sulfatides, whereas von Willebrand factor prefers galactosyl sulfatide but binds with moderate affinity to various sulfated glycolipids. Laminin also is less selective than thrombospondin but is less sensitive for detection of low sulfatide concentrations. Galactosyl sulfatide at 1-5 pmol can be detected by staining of lipids separated on high performance TLC with 125I-thrombospondin or 125I-von Willebrand factor. 125I-von Willebrand factor was examined as a reagent for detecting sulfated glycolipids in tissue extracts. Rat kidney lipids contain 5 characterized sulfated glycolipids: galactosyl ceramide I3-sulfate, lactosyl ceramide II3-sulfate, gangliotriaosyl ceramide II3-sulfate, and bis-sulfated gangliotriaosyl and gangliotetraosyl ceramides. von Willebrand factor detects all of these lipids as well as several additional minor sulfated lipids. Complex monosulfated lipids are detected in several human tissues including kidney, erythrocytes, and platelets by this technique.