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首页> 外文期刊>The Journal of Immunology: Official Journal of the American Association of Immunologists >A high endothelial venule secretory protein, mac25/angiomodulin, interacts with multiple high endothelial venule-associated molecules including chemokines.
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A high endothelial venule secretory protein, mac25/angiomodulin, interacts with multiple high endothelial venule-associated molecules including chemokines.

机译：高内皮小静脉分泌蛋白，mac25 /血管调节蛋白，与多种与高内皮小静脉相关的分子（包括趋化因子）相互作用。

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摘要

We previously reported that mac25/angiomodulin (AGM), a 30-kDa secretory protein, is abundantly expressed in high endothelial venules (HEVs), which play a crucial role in lymphocyte trafficking to the lymph nodes and Peyer's patches. We report that mac25/AGM interacts preferentially with certain molecules that are expressed in or around HEVs. In particular, mac25/AGM interacted with not only the extracellular matrix proteins and glycosaminoglycans that are expressed in most blood vessels including HEVs, but also with some chemokines that are implicated in the regulation of lymphocyte trafficking, such as the secondary lymphoid-tissue chemokine (SLC; CCL21), IFN-gamma-inducible protein 10 (IP-10; CXCL10), and RANTES (CCL5). The binding of mac25/AGM to SLC and IP-10 was dose-dependent and saturable. The binding to IP-10 could be inhibited by SLC but not by a non-mac25/AGM-binding chemokine, EBI1-ligand chemokine (ELC; CCL19). Interestingly, mac25/AGM failed to interact with 18 other chemokines, suggesting that it binds to certain chemokines preferentially. Immunohistochemical analysis indicated that mac25/AGM colocalizes at least partially with SLC and IP-10 at the basal lamina of HEVs. Upon binding with mac25/AGM, SLC and IP-10 retained all their Ca(2+)-signaling activity in vitro, suggesting that mac25/AGM can hold and present chemokines in the basal lamina of HEVs. These results imply that mac25/AGM plays a multifunctional role, serving not only as an adhesion protein to interact with glycosaminoglycans and extracellular matrix proteins but also as a molecule to present chemokines so that lymphocytes extravasating through HEVs receive further directional cues subsequent to the luminal encounter with lymphoid chemokines.
机译：我们以前曾报道过，mac25 /血管调节蛋白（AGM），一种30 kDa的分泌蛋白，在高内皮小静脉（HEVs）中大量表达，而高内皮小静脉（HEVs）在淋巴细胞向淋巴结和淋巴集结的转运中起着至关重要的作用。我们报告mac25 / AGM优先与HEVs或周围表达的某些分子相互作用。特别是，mac25 / AGM不仅与大多数血管（包括HEV）中表达的细胞外基质蛋白和糖胺聚糖相互作用，而且还与某些参与淋巴细胞运输调控的趋化因子相互作用，例如次级淋巴组织趋化因子（ SLC; CCL21），IFN-γ诱导蛋白10（IP-10; CXCL10）和RANTES（CCL5）。 mac25 / AGM与SLC和IP-10的结合具有剂量依赖性和饱和性。与IP-10的结合可以被SLC抑制，但不能被非mac25 / AGM结合趋化因子EBI1-配体趋化因子（ELC; CCL19）抑制。有趣的是，mac25 / AGM无法与其他18种趋化因子相互作用，表明它优先结合某些趋化因子。免疫组织化学分析表明，mac25 / AGM在HEV的基底层至少与SLC和IP-10共定位。与mac25 / AGM结合后，SLC和IP-10在体外保留了其所有的Ca（2+）信号转导活性，表明mac25 / AGM可以在HEV的基底层中保持和呈现趋化因子。这些结果表明，mac25 / AGM发挥多功能作用，不仅充当与糖胺聚糖和细胞外基质蛋白相互作用的粘附蛋白，而且作为呈递趋化因子的分子发挥作用，从而使通过HEV渗透的淋巴细胞在遇到腔后继而受到进一步的定向提示。与淋巴趋化因子。

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