Hemostatic properties and serum lipoprotein binding of a heparan sulfate proteoglycan from bovine aorta.
Hemostatic properties and serum lipoprotein binding of a heparan sulfate proteoglycan from bovine aorta.
复制标题
牛主动脉硫酸乙酰肝素蛋白多糖的止血特性和血清脂蛋白结合。
DOI：
10.1016/0304-4165(83)90011-9
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Berenson,GS
中科院分区：
文献类型：
--
作者：
Vijayagopal,P;Srinivasan,SR;Radhakrishnamurthy,B;Berenson,GS
比较了牛主动脉两种主要蛋白多糖硫酸乙酰肝素蛋白多糖和硫酸软骨素-硫酸皮肤素蛋白多糖的生物学特性。通过弹性蛋白酶消化或通过 4.0 M 盐酸胍提取主动脉组织来分离硫酸乙酰肝素蛋白多糖，通过 CsCl 等密度离心进行分级，并通过软骨素酶 ABC 处理进行纯化。第一种方法的产量（约占组织总硫酸乙酰肝素蛋白多糖的 70%）比第二种方法（占总量的 12%）高得多。硫酸软骨素-硫酸皮肤素蛋白多糖通过主动脉组织的4.0 M盐酸胍提取，然后CsCl等密度离心获得。两种硫酸乙酰肝素蛋白多糖制剂的化学成分相似。与在 Sepharose CL-6B 柱的空隙体积中洗脱的硫酸软骨素-硫酸皮肤素蛋白多糖不同，硫酸乙酰肝素蛋白多糖制剂分别分解为高分子量级分（kav=0.18 和 0.13）和低分子量级分（kav=0.47 和 0.36）。硫酸乙酰肝素蛋白多糖制剂表现出比硫酸软骨素-硫酸皮肤素蛋白多糖显着更强的抗凝血和血小板聚集抑制活性。蛋白多糖分子的蛋白质核心似乎对其止血特性并不重要。在Ca2+存在和不存在的情况下，硫酸乙酰肝素蛋白多糖与血清低密度脂蛋白(LDL)形成复合物的能力远小于硫酸软骨素-硫酸皮肤素蛋白多糖。硫酸乙酰肝素蛋白多糖和低密度脂蛋白之间的相互作用对介质离子强度的变化也比硫酸软骨素-硫酸皮肤素蛋白多糖和脂蛋白之间的相互作用更加敏感。由于两种蛋白聚糖的总硫酸盐含量几乎相似，因此硫酸乙酰肝素蛋白聚糖的分子尺寸较小，因此总体电荷密度较低，这似乎是其对 LDL 亲和力较低的部分原因。两种蛋白多糖生物学特性的差异可能对心血管疾病的病理生理学产生影响。
The biologic properties of two major proteoglycans of bovine aorta, heparan sulfate proteoglycan and chondroitin sulfate-dermatan sulfate proteoglycan were compared. The heparan sulfate proteoglycan was isolated either by elastase digestion or by 4.0 M guanidine hydrochloride extraction, of aorta tissue, fractionated by CsCl isopycnic centrifugation and purified by chondrointinase ABC treatment. The first method resulted in considerably greater yield (about 70% of the total heparan sulfate proteoglycan of the tissue) than the second procedure (12% of total). The chondroitin sulfate-dermatan sulfate proteoglycan was obtained by 4.0 M guanidine-HCl extraction of aorta tissue followed by CsCl isopycnic centrifugation. The chemical composition of both heparan sulfate proteoglycan preparations was similar. Unlike the chondroitin sulfate-dermatan sulfate proteoglycan, which eluted in the void volume of Sepharose CL-6B column, the heparan sulfate proteoglycan preparations were each resolved into a high molecular weight fraction (kav= 0.18 and 0.13) and a low molecular weight fraction (kav= 0.47 and 0.36). The heparan sulfate proteoglycan preparations exhibited significantly more potent anticoagulant and platelet aggregation inhibitory activities than the chondroitin sulfate-dermatan sulfate proteoglycan. The protein core of the proteoglycan molecules did not seem to be essential for their hemostatic properties. The complex forming ability of the heparan sulfate proteoglycan with serum low density lipoproteins (LDL) was much less than that of chondroitin sulfate-dermatan sulfate proteoglycan in the presence and absence of Ca2+. Interaction between heparan sulfate proteoglycan and LDL was also much more sensitive to changes in the ionic strength of the medium than that of chondroitin sulfate-dermatan sulfate proteoglycan and the lipoprotein. Since the total sulfate content of both proteoglycans is almost similar, the smaller molecular size and hence the lower overall charge density of the heparan sulfate proteoglycan appears to be partly responsible for its low affinity for LDL. The differences in biologic properties of the two proteoglycans might have implications in the pathophysiology of cardiovascular diseases.