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Use of the luciferase reporter constructs for investigation of the capacity of Noggin2 protein to inhibit cell signaling pathways in Xenopus laevis embryos

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Abstract

Noggin (Noggin1) protein inhibits Smad1-dependent TGF-β (BMP) signaling cascades by extracellular binding of BMP proteins. Recently, we identified two previously unknown members of the Noggin family, Noggin2 and Noggin4 proteins. In this work, using luciferase reporter constructs, it was shown that Noggin2 is able to inhibit in addition to the BMP-signaling cascade, the Activin/Nodal and Wnt signaling pathways in Xenopus laevis early embryos. The inhibition efficiency of Noggin2 is comparable to well-known extracellular inhibitors Cerberus and Follistatin. In addition to revealing novel properties of Noggin2, this work demonstrates that luciferase reporter constructs are a convenient tool for studying the regulation of molecular signaling cascades in the model of Xenopus laevis embryos.

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Abbreviations

BMP:

bone morphogenetic protein

CMV:

cytomegalovirus

RFP:

red fluorescent protein

TGF:

transforming growth factor

Xnr2:

xenopus nodal-related

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Authors and Affiliations

  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russia

    F. M. Eroshkin, A. V. Bayramov, N. Y. Martynova & A. G. Zaraisky

Authors
  1. F. M. Eroshkin
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  2. A. V. Bayramov
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  3. N. Y. Martynova
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  4. A. G. Zaraisky
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Corresponding author

Correspondence to A. G. Zaraisky.

Additional information

Original Russian Text © F.M. Eroshkin, A.V. Bayramov, N.Y. Martynova, A.G. Zaraisky, 2012, published in Bioorganicheskaya Khimiya, 2012, Vol. 38, No. 3, pp. 385–388.

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Eroshkin, F.M., Bayramov, A.V., Martynova, N.Y. et al. Use of the luciferase reporter constructs for investigation of the capacity of Noggin2 protein to inhibit cell signaling pathways in Xenopus laevis embryos. Russ J Bioorg Chem 38, 338–340 (2012). https://doi.org/10.1134/S106816201203003X

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  • DOI: https://doi.org/10.1134/S106816201203003X

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