糖胺聚糖对抗凝血酶III和[A103,106,108]抗凝血酶III 93 - 119与硫苷脂（Gal(3 - SO4)β1 - 1Cer）结合的特异性抑制作用。

Specific inhibition of binding of antistasin and [A103,106,108] antistasin 93-119 to sulfatide (Gal(3-SO4)beta 1-1Cer) by glycosaminoglycans.

作者信息

Brankamp R G, Manley G D, Owen T J, Krstenansky J L, Cardin A D

机构信息

Marion Merrell Dow Research Institute, Cincinnati, OH 45215.

出版信息

FEBS Lett. 1992 Jan 20;296(2):145-7. doi: 10.1016/0014-5793(92)80366-o.

DOI:10.1016/0014-5793(92)80366-o

PMID:1733769

Abstract

Leech-derived antistasin is a potent anticoagulant and antimetastatic protein that binds sulfatide (Gal(3-SO4)beta 1-1Cer) and sulfated polysaccharides. In this study, the synthetic fragment [A103,106,108] antistasin 93-119, which corresponds to the carboxyl terminus, showed specific and saturable binding to sulfatide. Binding was competitively blocked by glycosaminoglycans (GAGs) in the order: dextran sulfate 5000 congruent to dextran sulfate 500,000 greater than heparin greater than dermatan sulfate much greater than chondroitin sulfates A and C. This rank order of inhibitory potency was identical to that observed with whole antistasin. We suggest that residues 93-119 of antistasin represent a critical domain for binding GAGs and sulfated glycolipids.

摘要

源自水蛭的抗栓酶是一种强效抗凝和抗转移蛋白，它能结合硫苷脂（Gal(3-SO4)β1-1Cer）和硫酸化多糖。在本研究中，对应于羧基末端的合成片段[A103,106,108]抗栓酶93-119显示出与硫苷脂的特异性和饱和性结合。糖胺聚糖（GAGs）以如下顺序竞争性阻断结合：硫酸葡聚糖5000≅硫酸葡聚糖500,000＞肝素＞硫酸皮肤素＞＞硫酸软骨素A和C。这种抑制效力的排序与用完整抗栓酶观察到的相同。我们认为抗栓酶的93-119位残基代表了结合GAGs和硫酸化糖脂的关键结构域。