Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF.

作者: U. Suter , J.V. Heymach , E.M. Shooter

DOI: 10.1002/J.1460-2075.1991.TB07778.X

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摘要: 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 examine pro-region NGF protein a first step towards general understanding role propeptides biosynthesis neurotrophins. Our results demonstrate that only two small domains within propeptide required for expression secretion properly processed recombinant mouse COS-7 cells. Domain I plays an important active while domain II is involved processing. Both partially conserved between isolated from different species well NT-3.

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