Vijayagopal P, Srinivasan S R, Radhakrishnamurthy B, Berenson G S
Biochim Biophys Acta. 1983 Jul 5;758(1):70-83. doi: 10.1016/0304-4165(83)90011-9.
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 chondroitinase 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.
对牛主动脉的两种主要蛋白聚糖，即硫酸乙酰肝素蛋白聚糖和硫酸软骨素-硫酸皮肤素蛋白聚糖的生物学特性进行了比较。硫酸乙酰肝素蛋白聚糖可通过弹性蛋白酶消化或用4.0M盐酸胍提取主动脉组织来分离，经CsCl等密度离心分级，并通过软骨素酶ABC处理纯化。第一种方法的产量（约占组织中总硫酸乙酰肝素蛋白聚糖的70%）比第二种方法（占总量的12%）高得多。硫酸软骨素-硫酸皮肤素蛋白聚糖是通过用4.0M盐酸胍提取主动脉组织，然后进行CsCl等密度离心获得的。两种硫酸乙酰肝素蛋白聚糖制剂的化学组成相似。与在Sepharose CL-6B柱的空体积中洗脱的硫酸软骨素-硫酸皮肤素蛋白聚糖不同，硫酸乙酰肝素蛋白聚糖制剂各自被解析为一个高分子量级分（kav = 0.18和0.13）和一个低分子量级分（kav = 0.47和0.36）。硫酸乙酰肝素蛋白聚糖制剂表现出比硫酸软骨素-硫酸皮肤素蛋白聚糖更强的抗凝和抑制血小板聚集活性。蛋白聚糖分子的蛋白核心似乎对其止血特性并非必不可少。在有和没有Ca2+的情况下，硫酸乙酰肝素蛋白聚糖与血清低密度脂蛋白（LDL）形成复合物的能力比硫酸软骨素-硫酸皮肤素蛋白聚糖小得多。硫酸乙酰肝素蛋白聚糖与LDL之间的相互作用对介质离子强度变化的敏感性也比硫酸软骨素-硫酸皮肤素蛋白聚糖与脂蛋白之间的相互作用高得多。由于两种蛋白聚糖的总硫酸盐含量几乎相似，硫酸乙酰肝素蛋白聚糖较小的分子尺寸以及因此较低的总电荷密度似乎部分导致了其对LDL的低亲和力。两种蛋白聚糖生物学特性的差异可能对心血管疾病的病理生理学有影响。
