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首页> 外文期刊>Journal of receptor and signal transduction research >Brain-specific angiogenesis inhibitor 2 (BAI2) may be activated by proteolytic processing
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Brain-specific angiogenesis inhibitor 2 (BAI2) may be activated by proteolytic processing

机译：脑特异性血管生成抑制剂2（BAI2）可以通过蛋白水解过程激活

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Brain-specific angiogenesis inhibitor 2 (BAI2) is a member of adhesion-G protein-coupled receptors (GPCRs). BAI2 is dominantly expressed in the brain and its physiological ligands and functions are still unclear. Adhesion-GPCRs, including BAI2, commonly have a long N-terminal extracellular region (ECR) containing the GPCR proteolysis site (GPS) and the cleavage of the ECR at the GPS domain is suspected to be important for their function. In this study, we analyzed the proteolytic processing of BAI2 and its activation mechanism. Several cleaved C-terminal fragments of BAI2 were identified in mouse hippocampus. We confirmed that mutation in the GPS domain caused inhibition of the proteolysis of BAI2, which indicated the possibility that BAI2 was cleaved at the GPS domain. The association of the ECR putatively cleaved at the GPS domain and the C-terminal seven-transmembrane (7TM) fragment was detected by co-immunoprecipitation. We also found that furin prohormone convertase cleaved BAI2 at another site in the ECR. Additionally, the C-terminal fragment cleaved at the GPS domain specifically activated the nuclear factor of activated T-cells (NFAT) pathway. These results suggest that BAI2 is a functional GPCR regulated by proteolytic processing and activates the NFAT pathway.
机译：脑特异性血管生成抑制剂2（BAI2）是粘附G蛋白偶联受体（GPCR）的成员。 BAI2主要在大脑中表达，其生理配体和功能仍不清楚。包括BAI2在内的粘附GPCR通常具有一个长的N末端胞外区（ECR），其中包含GPCR蛋白质水解位点（GPS），并且怀疑在GPS域中ECR的裂解对其功能很重要。在这项研究中，我们分析了BAI2的蛋白水解过程及其激活机制。在小鼠海马体中鉴定出几个BAI2的C末端裂解片段。我们证实，GPS域中的突变引起BAI2蛋白水解的抑制，这表明BAI2在GPS域被切割的可能性。通过共免疫沉淀检测推定在GPS结构域切割的ECR和C端七跨膜（7TM）片段的关联。我们还发现弗林蛋白酶原激素转化酶在ECR的另一个位点切割了BAI2。此外，在GPS域切割的C端片段特异性激活了活化T细胞（NFAT）途径的核因子。这些结果表明，BAI2是由蛋白水解过程调节并激活NFAT途径的功能性GPCR。

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