Perlecan: a major IL-2-binding proteoglycan in murine spleen
Perlecan: a major IL-2-binding proteoglycan in murine spleen
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DOI：
10.1038/sj.icb.7100128
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发表时间：
2008-02-01
影响因子：
4
通讯作者：
Wrenshall, Lucile E.
中科院分区：
文献类型：
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作者：
Miller, John D.;Stevens, Elliott T.;Wrenshall, Lucile E.
虽然白介素2(IL-2)通常被认为是一种可溶的细胞因子，但我们的实验室已经证明，IL-2在淋巴组织中的可用性在一定程度上是由与硫酸乙酰肝素糖胺聚糖的结合来调节的。硫酸乙酰肝素通常以蛋白多糖的形式存在，其中硫酸乙酰肝素链与特定的核心蛋白共价连接。我们现在发现Perlecan是小鼠脾中主要的IL-2结合的硫酸乙酰肝素蛋白多糖之一。IL-2通过硫酸乙酰肝素链与Perlecan结合，因为酶从脾Perlecan中去除硫酸乙酰肝素会取消其与IL-2结合的能力。此外，我们还证明了Perlecan结合的IL-2支持依赖于IL-2的细胞系的增殖。确定Perlecan是一种主要的与IL-2结合的硫酸乙酰肝素蛋白多糖，这对IL-2在体内的定位和调节具有重要意义。
Although interleukin-2 (IL-2) is typically considered a soluble cytokine, our laboratory has shown that the availability of IL-2 in lymphoid tissues is regulated, in part, by an association with heparan sulfate glycosaminoglycan. Heparan sulfate is usually found in proteoglycan form, in which the heparan sulfate chains are covalently linked to a specific core protein. We now show that perlecan is one of the major IL-2-binding heparan sulfate proteoglycans in murine spleen. IL-2 binds perlecan via heparan sulfate chains, as enzymatic removal of heparan sulfate from splenic perlecan abolishes its ability to bind IL-2. Furthermore, we demonstrate that perlecan-bound IL-2 supports the proliferation of an IL-2-dependent cell line. Identification of perlecan as a major heparan sulfate proteoglycan that binds IL-2 has implications for both the localization and regulation of IL-2 in vivo.