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Genetic engineering of mouse embryonic stem cells by Nurr1 enhances differentiation and maturation into dopaminergic neurons (2002)

Chung, Sangmi ; Sonntag, Kai-C. ; Andersson, Therese ; [et al.]

Oxford, UK : Blackwell Science, Ltd

European journal of neuroscience 16 (2002), S. 0

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ISSN: 1460-9568

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Nurr1 is a transcription factor critical for the development of midbrain dopaminergic (DA) neurons. This study modified mouse embryonic stem (ES) cells to constitutively express Nurr1 under the elongation factor-1α promoter. The Nurr1-expression in ES cells lead to up-regulation of all DA neuronal markers tested, resulting in about a 4- to 5-fold increase in the proportion of DA neurons. In contrast, other neuronal and glial markers were not significantly changed by Nurr1 expression. It was also observed that there was an additional 4-fold increase in the number of DA neurons in Nurr1-expressing clones following treatment with Shh, FGF8 and ascorbic acid. Several lines of evidence suggest that these neurons may represent midbrain DA neuronal phenotypes; firstly, they coexpress midbrain DA markers such as aromatic l-amino acid decarboxylase, calretinin, and dopamine transporter, in addition to tyrosine hydroxylase and secondly, they do not coexpress other neurotransmitters such as GABA or serotonin. Finally, consistent with an increased number of DA neurons, the Nurr1 transduction enhanced the ability of these neurons to produce and release DA in response to membrane depolarization. This study demonstrates an efficient genetic manipulation of ES cells that facilitates differentiation to midbrain DA neurons, and it will serve as a framework of genetic engineering of ES cells by key transcription factor to regulate their cell fate.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1046/j.1460-9568.2002.02255.x

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Production and Amyloid Fibril Formation of Recombinant Yeast Prion(Sup35)-Like Protein Fragment (2005)

Kim, Yongae ; Kim, Yuna ; Park, Jae Joon ; [et al.]

s.l. ; Stafa-Zurich, Switzerland

Key engineering materials Vol. 277-279 (Jan. 2005), p. 67-71

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ISSN: 1013-9826

Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008

Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics

Notes: Amyloid fibrils have long been established as the well-known a-helix to b-sheettransition that characterizes the conversion of the cellular form of prion proteins into a scrapie form. A very short sequence of the Yeast prion-like protein GNNQQNY(SupN) is responsible for the aggregation that induces diseases. As such, in the current study, a GST-fused monomer SupN vector is used to express the SupN peptide in Escherichia coli(E. Coli). In addition, a method for the production, purification, and cleavage of the recombinant SupN in E. coli is also described, which yields as much as 2mg per liter of growth of natural abundance fusion proteins in LB media. To gain a better understanding of the aggregation-structure relationship of the 7 residues of the Yeast prion-like protein, the change in the conformational structure is studied by Transmission Electron Microscopy and will be further studied by 13C solid-state NMR. Accordingly, this is the first investigation of the fibril formation of a heptamer peptide expressed in E.coli