2 CONSERVED DOMAINS IN THE NGF PROPEPTIDE ARE NECESSARY AND SUFFICIENT FOR THE BIOSYNTHESIS OF CORRECTLY PROCESSED AND BIOLOGICALLY-ACTIVE NGF
2 CONSERVED DOMAINS IN THE NGF PROPEPTIDE ARE NECESSARY AND SUFFICIENT FOR THE BIOSYNTHESIS OF CORRECTLY PROCESSED AND BIOLOGICALLY-ACTIVE NGF
复制标题
DOI：
10.1002/j.1460-2075.1991.tb07778.x
复制
发表时间：
1991-09-01
期刊：
影响因子：
11.4
通讯作者：
SHOOTER, EM
中科院分区：
文献类型：
--
作者：
SUTER, U;HEYMACH, JV;SHOOTER, EM
神经营养因子家族的三个成员(NGF、BDNF和NT-3)被合成为大的前体蛋白，经过蛋白分解处理后产生具有生物活性的成熟的神经营养因子。我们已经使用体外诱变来检测NGF前体蛋白中的前区域，作为全面了解前肽在神经营养因子生物合成中的作用的第一步。我们的结果表明，在COS-7细胞中，只需要NGF前肽中的两个小区域来表达和分泌经过适当加工和具有生物活性的重组小鼠NGF。结构域I在活性NGF的表达中起重要作用，结构域II参与蛋白降解过程。这两个结构域在不同物种分离的NGF蛋白以及BDNF和NT-3的前肽之间都是部分保守的。
The three members of the neurotrophin family (NGF, BDNF and NT-3) are synthesized as large precursor proteins which undergo proteolytic processing to yield biologically active, mature neurotrophic factors. We have used in vitro mutagenesis to examine the pro-region in the NGF precursor protein as a first step towards a general understanding of the role of propeptides in the biosynthesis of neurotrophins. Our results demonstrate that only two small domains within the NGF propeptide are required for the expression and secretion of properly processed and biologically active, recombinant mouse NGF in COS-7 cells. Domain I plays an important role in the expression of active NGF while domain II is involved in proteolytic processing. Both domains are partially conserved between the propeptides of NGF proteins isolated from different species as well as BDNF and NT-3.