In vitro production of an active neurotrophic factor, neuregulin-1: Qualitative comparison of different cell-free translation systems

Neuroscience Letters

Volumn 497, Issue 2, 2011, Pages 90-93

  Wang, Ran ^a   Iwakura, Yuriko ^a   Araki, Kazuaki ^a   Sotoyama, Hidekazu ^a   Takei, Nobuyuki ^a   Nawa, Hiroyuki ^a  

^a NIIGATA UNIVERSITY   (Japan)

Author keywords

ErbB4; Heparin; In vitro translation; Neuregulin 1; Protein refolding

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 4; HEPARIN; MESSENGER RNA; NEU DIFFERENTIATION FACTOR; NEUROTROPHIC FACTOR;

ARTICLE; BIOLOGICAL ACTIVITY; CELL LYSATE; HELA CELL; IN VITRO STUDY; INTERNAL RIBOSOME ENTRY SITE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; QUALITATIVE ANALYSIS; RETICULOCYTE LYSATE; RNA TRANSLATION; TRANSLATION REGULATION; WHEAT GERM;

ALTERNATIVE SPLICING; ANIMALS; CELL LINE; CELL-FREE SYSTEM; HELA CELLS; HUMANS; MICE; NERVE GROWTH FACTORS; NEUREGULIN-1; PROTEIN BIOSYNTHESIS; PROTEIN REFOLDING; RABBITS; RETICULOCYTES; WHEAT GERM AGGLUTININS;

EID: 79956313653     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2011.04.036     Document Type: Article

References (19)

1. Asselbergs F.A., Meulenberg E., van Venrooij W.J., Bloemendal H. Preferential translation of mRNAs in an mRNA-dependent reticulocyte lysate. Eur. J. Biochem. 1980, 109:159-165.
2. Backliwal G., Hildinger M., Chenuet S., Wulhfard S., De Jesus M., Wurm F.M. Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1g/l by transient transfection under serum-free conditions. Nucleic Acids Res. 2008, 36:e96.
3. Balbás P. Understanding the art of producing protein and nonprotein molecules in Escherichia coli. Mol. Biotechnol. 2001, 19:251-267.
4. Clark E.D. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 2001, 12:202-207.
5. Hemdan E.S., Zhao Y.J., Sulkowski E., Porath J. Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography. Proc. Natl. Acad. Sci. U.S.A. 1989, 86:1811-1815.
6. Iwakura Y., Piao Y.S., Mizuno M., Takei N., Kakita A., Takahashi H., Nawa H. Influences of dopaminergic lesion on epidermal growth factor-ErbB signals in Parkinson's disease and its model: neurotrophic implication in nigrostriatal neurons. J. Neurochem. 2005, 93:974-983.
7. Kato T., Abe Y., Sotoyama H., Kakita A., Kominami R., Hirokawa S., Ozaki M., Takahashi H., Nawa H. Transient exposure of neonatal mice to neuregulin-1 results in hyperdopaminergic states in adulthood: implication in neurodevelopmental hypothesis for schizophrenia. Mol. Psychiatry 2011, 16:16307-16320.
8. Liu C., Dalby B., Chen W., Kilzer J.M., Chiou H.C. Transient transfection factors for high-level recombinant protein production in suspension cultured mammalian cells. Mol. Biotechnol. 2008, 39:141-153.
9. Lodish F., Rose J.K. Relative importance of 7-methylguanosine in ribosome binding and translation of vesicular stomatitis virus mRNA in wheat germ and reticulocyte cell-free systems. J. Biol. Chem. 1977, 252:1181-1188.
10. Ma Z., Li Q., An H., Pankonin M.S., Wang J., Loeb J.A. Targeting human epidermal growth factor receptor signaling with the neuregulin's heparin-binding domain. J. Biol. Chem. 2009, 284:32108-32115.
11. Mei L., Xiong W.C. Neuregulin-1 in neural development, synaptic plasticity and schizophrenia. Nat. Rev. Neurosci. 2008, 9:437-452.
12. Mikami S., Kobayashi T., Masutani M., Yokoyama S., Imataka H. A human cell-derived in vitro coupled transcription/translation system optimized for production of recombinant proteins. Protein Expr. Purif. 2008, 62:190-198.
13. Mizuno K., Carnahan J., Nawa H. Brain-derived neurotrophic factor promotes differentiation of striatal GABAergic neurons. Dev. Biol. 1994, 165:243-256.
14. Shibuya M., Komi E., Wang R., Kato T., Watanabe Y., Sakai M., Ozaki M., Someya T., Nawa H. Measurement and comparison of serum neuregulin-1 immunoreactivity in control subjects and patients with schizophrenia: an influence of its genetic polymorphism. J. Neural. Transm. 2010, 117:887-895.
15. Sun X., Goh P.E., Wong K.T., Mori T., Yap M.G. Enhancement of transient gene expression by fed-batch culture of HEK 293 EBNA1 cells in suspension. Biotechnol. Lett. 2006, 28:843-848.
16. Wen D., Suggs S.V., Karunagaran D., Liu N., Cupples R.L., Luo Y., Janssen A.M., Ben-Baruch N., Trollinger D.B., Jacobsen V.L., Meng S.Y., Lu H.S., Hu S., Chang D., Yang W., Yanigahara D., Koski R.A., Yarden Y. Structural and functional aspects of the multiplicity of Neu differentiation factors. Mol. Cell Biol. 1994, 14:1909-1919.
17. Witherell G. In vitro translation using HeLa extract. Curr. Protoc. Cell Biol. 2001, (Chapter 11:Unit 11.8). 10.1002/0471143030.cb1108s06.
18. Yang Y.W., Romanus J.A., Liu T.Y., Nissley S.P., Rechler M.M. Biosynthesis of rat insulin-like growth factor II. I. Immunochemical demonstration of a approximately 20-kilodalton biosynthetic precursor of rat insulin-like growth factor II in metabolically labeled BRL-3A rat liver cells. J. Biol. Chem. 1985, 2570-2577.
19. Zong Q., Osmulski P.A., Hager L.P. High-pressure-assisted reconstitution of recombinant chloroperoxidase. Biochemistry 1995, 34:12420-12425.