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Efficient production of active TNF-alpha by albumin signal peptide.

Authors
  • Maeda, Y
  • Soda, M
  • Ito, K
  • Sato, K
Type
Published Article
Journal
Biochemistry and molecular biology international
Publication Date
Jul 01, 1997
Volume
42
Issue
4
Pages
825–832
Identifiers
DOI: 10.1080/15216549700203261
PMID: 19856300
Source
Medline
License
Unknown

Abstract

TNF-alpha is initially synthesized as a membrane-anchored precursor protein and processed proteolytically by a matrix metalloproteinase (MMP)-like enzyme. In order to establish an efficient expression system of TNF-alpha in mammalian cells without involvement of the extracellular enzyme, an expression plasmid (pCN-alb-TNF) was constructed with a signal sequence of the rat albumin gene as a module for secretion. The highest level of production of TNF-alpha was observed in the clone CT-3 by SDS-PAGE and Western blot analysis. Biological activity of the secretion was revealed by repression of catalase gene expression in hepatoma cells and cytotoxity to L929 cells. Attachment of the signal peptide to mature form resulted in the enhancement of production of the cytokine.

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