Sulfated polysaccharide purified from Ecklonia cava accelerates antithrombin III-mediated plasma proteinase inhibition
Sulfated polysaccharide purified from Ecklonia cava accelerates antithrombin III-mediated plasma proteinase inhibition
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从昆布中纯化的硫酸多糖可加速抗凝血酶 III 介导的血浆蛋白酶抑制
DOI：
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发表时间：
2007
影响因子：
3.3
通讯作者：
Y. Jeon
中科院分区：
文献类型：
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作者：
Won‐Kyo Jung;Yasantha Athukorala;Young;Seon;Chi;T. Vasanthan;Kwang;S. Yoo;Se;Y. Jeon
表面等离子体共振是研究分子相互作用的一项重要技术，研究了从褐藻Ecklonia cava （ECA）酶解物中纯化的抗凝血硫酸酸化多糖与凝血因子的分子相互作用。在直接结合实验中，ECA/抗凝血酶III （ATIII）与活化凝血因子的结合亲和力顺序为：VIIa因子(FVIIa) > Xa因子(FXa) >凝血酶（FIIa）；动力学分析确定了FVIIa、FXa和FIIa的ECA KD值分别为15.1、45.0和65.0 nM。因此，ECA强烈和选择性地（FVII、FX和FII）增强了外源性和常见凝血途径中atiii介导的凝血因子抑制。这可能有助于其体外高抗凝血活性。ECA对静脉内皮细胞系（ECV-304）的低细胞毒性也扩大了其在未来体内研究中的价值。然而，为了利用它作为新型抗凝剂的模型，必须解决它与其他抗凝机制的可能干扰。
Surface plasmon resonance is an important technique for studying molecular interactions and was used to investigate the molecular interaction of anticoagulant sulfated polysaccharides purified from an enzymatic hydrolysate of the brown alga Ecklonia cava (ECA) with blood coagulation factors. In a direct binding assay, binding affinity between ECA/antithrombin III (ATIII) and activated blood coagulation factors was in the order: factor VIIa (FVIIa) > factor Xa (FXa) > thrombin (FIIa); kinetic analysis determined KD values of ECA for FVIIa, FXa, and FIIa of 15.1, 45.0 and 65.0 nM, respectively. Therefore, ECA strongly and selectively (FVII, FX, and FII) enhanced ATIII-mediated coagulation factor inhibition in both the extrinsic and common coagulation pathways. This may contribute to its high anticoagulant activity in vitro. The low cytotoxicity of ECA to venous endothelial cell line (ECV-304) also expands its value in future in vivo studies. However, to utilize it as a model for novel anticoagulant agents, its possible interference with other anticoagulant mechanisms must be addressed.
影响因子：
2.9
作者：
DAVIE, EW;FUJIKAWA, K;KISIEL, W
通讯作者：
KISIEL, W