Heparin releasable and nonreleasable forms of heparan sulfate proteoglycan are found on the surfaces of cultured porcine aortic endothelial cells.
Heparin releasable and nonreleasable forms of heparan sulfate proteoglycan are found on the surfaces of cultured porcine aortic endothelial cells.
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在培养的猪主动脉内皮细胞的表面上发现了肝素可释放和不可释放形式的硫酸乙酰肝素蛋白多糖。
DOI：
10.1007/bf00230873
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发表时间：
1992
影响因子：
4.3
通讯作者：
Patton2nd,WA
中科院分区：
文献类型：
--
作者：
Lowe-Krentz,LJ;Thompson,K;Patton2nd,WA
有证据表明，内皮细胞层硫酸乙酰肝素蛋白聚糖包括多种不同大小的分子，这些分子很可能含有不同的蛋白核心。在本报告中，大约一半的内皮细胞表面相关的硫酸乙酰肝素蛋白多糖被证明可通过可溶性肝素释放。剩余的细胞表面硫酸乙酰肝素蛋白多糖以及细胞外基质硫酸乙酰肝素蛋白多糖不能用肝素从细胞中去除。肝素不可释放的细胞表面蛋白多糖可以通过膜破坏剂释放，并且能够嵌入脂质体中。当比较肝素可释放和不可释放的细胞表面硫酸乙酰肝素蛋白多糖时，蛋白多糖大小的差异也很明显。此外，完整的肝素可释放的硫酸乙酰肝素蛋白多糖在尺寸上更接近于从细胞外基质和生长培养基中分离的蛋白多糖，而不是肝素不可释放的蛋白多糖。这些数据表明，培养的猪主动脉内皮细胞含有至少两种不同类型的细胞表面硫酸乙酰肝素蛋白聚糖，其中一种似乎通过其糖胺聚糖链与细胞相关。另一个（关联更紧密）可能通过膜嵌入的蛋白质核心连接。
Evidence suggests that endothelial cell layer heparan sulfate proteoglycans include a variety of different sized molecules which most likely contain different protein cores. In the present report, approximately half of endothelial cell surface associated heparan sulfate proteoglycan is shown to be releasable with soluble heparin. The remaining cell surface heparan sulfate proteoglycan, as well as extracellular matrix heparan sulfate proteoglycan, cannot be removed from the cells with heparin. The heparin nonreleasable cell surface proteoglycan can be released by membrane disrupting agents and is able to intercalate into liposomes. When the heparin releasable and nonreleasable cell surface heparan sulfate proteoglycans are compared, differences in proteoglycan size are also evident. Furthermore, the intact heparin releasable heparan sulfate proteoglycan is closer in size to proteoglycans isolated from the extracellular matrix and from growth medium than to that which is heparin nonreleasable. These data indicate that cultured porcine aortic endothelial cells contain at least two distinct types of cell surface heparan sulfate proteoglycans, one of which appears to be associated with the cells through its glycosaminoglycan chains. The other (which is more tightly associated) is probably linked via a membrane intercalated protein core.