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首页> 外文期刊>Journal of Epithelial Biology & Pharmacology >The N-Terminal 81-aa Fragment is Critical for UT-A1 Urea Transporter Bioactivity
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The N-Terminal 81-aa Fragment is Critical for UT-A1 Urea Transporter Bioactivity

机译：N端81-aa片段对于UT-A1尿素转运蛋白的生物活性至关重要

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The serine protease, furin, is involved in the activation of a number of proteins most notably epithelial sodium channels (ENaC). The urea transporter UT-A1, located in the kidney inner medullary collecting duct (IMCD), is important for urine concentrating ability. UT-A1's amino acid sequence has a consensus furin cleavage site (RSKR) in the Nterminal region. Despite the putative cleavage site, we find that UT-A1, either from the cytosolic or cell surface pool, is not cleaved by furin in CHO cells. This result was further confirmed by an inability of furin to cleave in vitro an 35Slabeled UT-A1 or the 126 N-terminal UT-A1 fragment. Functionally, mutation of the furin site (R78A, R81A) does not affect UT-A1 urea transport activity. However, deletion of the 81-aa N-terminal portion does not affect UT-A1 cell surface trafficking, but seriously impair UT-A1 urea transport activity. Our results indicate that UT-A1 maturation and activation does not require furin-dependent cleavage. The N-terminal 81-aa fragment is required for proper UT-A1 urea transport activity, but its effect is not through changing UT-A1 membrane trafficking.
机译：丝氨酸蛋白酶弗林蛋白酶参与许多蛋白质的激活，最显着的是上皮钠通道（ENaC）。尿素转运蛋白UT-A1位于肾脏内髓收集管（IMCD）中，对尿液浓缩能力很重要。 UT-A1的氨基酸序列在N末端区域具有共有弗林蛋白酶切割位点（RSKR）。尽管有假定的切割位点，我们发现从胞质或细胞表面池中获得的UT-A1在CHO细胞中并未被弗林蛋白酶切割。弗林蛋白酶不能体外切割35S标记的UT-A1或126个N端UT-A1片段，进一步证实了这一结果。在功能上，弗林蛋白酶位点（R78A，R81A）的突变不影响UT-A1尿素转运活性。但是，删除81-aa N端部分不会影响UT-A1细胞表面运输，但会严重损害UT-A1尿素转运活性。我们的结果表明，UT-A1的成熟和激活不需要弗林蛋白酶依赖性的裂解。 N末端81-aa片段是适当的UT-A1尿素转运活性所必需的，但其作用不是通过改变UT-A1膜运输来实现的。

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