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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >PROTEOLYTIC MATURATION OF PROTEIN C UPON ENGINEERING THE MOUSE MAMMARY GLAND TO EXPRESS FURIN
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PROTEOLYTIC MATURATION OF PROTEIN C UPON ENGINEERING THE MOUSE MAMMARY GLAND TO EXPRESS FURIN

机译：通过工程化小鼠乳腺表达尿蛋白来进行蛋白水解

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摘要

Endoproteolytic processing of the human protein C (HPC) precursor to its mature form involves cleavage of the propeptide after amino acids Lys(-2)-Arg(-1) and removal of a Lys(156)-Arg(157) dipeptide connecting the light and heavy chains. This processing was inefficient in the mammary gland of transgenic mice and pigs, We hypothesized that the protein processing capacity of specific animal organs may be improved by the coexpression of selected processing enzymes. We tested this by targeting expression of the human proprotein processing enzyme, named paired basic amino acid cleaving enzyme (PACE)/furin, or an enzymatically inactive mutant, PACEM, to the mouse mammary gland. In contrast to mice expressing HPC alone, or to HPC/PACEM bigenic mice, coexpression of PACE with HPC resulted in efficient conversion of the precursor to mature protein, with cleavage at the appropriate sites. These results suggest the involvement of PACE in the processing of HPC in vivo and represent an example of the engineering of animal organs into bioreactors with enhanced protein professing capacity. [References: 36]
机译：人类蛋白C（HPC）前体的内切水解加工为成熟形式涉及氨基酸Lys（-2）-Arg（-1）后的前肽裂解和连接该蛋白的Lys（156）-Arg（157）二肽的去除。轻链和重链。这种加工在转基因小鼠和猪的乳腺中效率低下。我们假设，特定动物器官的蛋白质加工能力可能会因所选加工酶的共表达而提高。我们通过将人类前蛋白加工酶（称为成对的碱性氨基酸裂解酶（PACE）/弗林蛋白酶，或无酶活性的突变体PACEM）的表达靶向小鼠乳腺来进行测试。与仅表达HPC的小鼠或HPC / PACEM双基因小鼠相比，PACE与HPC的共表达可导致前体有效转化为成熟蛋白，并在适当的位点进行切割。这些结果表明，PACE参与了体内HPC的加工，并代表了将动物器官工程化为具有增强的蛋白质表达能力的生物反应器的例子。 [参考：36]

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