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

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

Research output: Contribution to journalArticle

121 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2395-2400
Number of pages6
JournalEMBO Journal
Volume10
Issue number9
StatePublished - Sep 23 1991

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Biosynthesis
Nerve Growth Factor
Nerve Growth Factors
Protein Precursors
Brain-Derived Neurotrophic Factor
Mutagenesis
COS Cells
Processing
Proteins

Keywords

  • Biosynthesis
  • NGF
  • Neurotrophin
  • Processing
  • Propeptide

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF. / Suter, U.; Heymach, J. V.; Shooter, E. M.

In: EMBO Journal, Vol. 10, No. 9, 23.09.1991, p. 2395-2400.

Research output: Contribution to journalArticle

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