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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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ISSN
1437-4315
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Volume 387, Issue 4

Issues

Monomeric and dimeric GDF-5 show equal type I receptor binding and oligomerization capability and have the same biological activity

Christina Sieber
  • Institut für Chemie/Biochemie, Freie Universität Berlin, Thielallee 63, D-14195 Berlin, Germany
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/ Frank Plöger / Raphaela Schwappacher
  • Institut für Chemie/Biochemie, Freie Universität Berlin, Thielallee 63, D-14195 Berlin, Germany
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/ Rolf Bechtold / Michael Hanke / Shinji Kawai
  • Department of Oral Frontier Biology Osaka University, Graduate School of Dentistry, 1-8 Yamadaoka, Suita-Osaka 565-0871, Japan
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/ Yoshifumi Muraki
  • Therapeutic Area-Oncology, Clinical Development, Scientific Affairs, Aventis Pharma Ltd., Sanofi-Aventis Group, Tokyo Opera City Tower 3-20-2, Nishi shinjyuku, Shinjyuku-ku, Tokyo 163-1488, Japan
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/ Mieko Katsuura
  • DDS Institute, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato, Tokyo 105-8461, Japan
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/ Michio Kimura
  • DDS Institute, The Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato, Tokyo 105-8461, Japan
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/ Maya Mouler Rechtman
  • Department of Neurobiochemistry, Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
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/ Yoav I. Henis
  • Department of Neurobiochemistry, Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
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/ Jens Pohl / Petra Knaus
  • Institut für Chemie/Biochemie, Freie Universität Berlin, Thielallee 63, D-14195 Berlin, Germany
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Published Online: 2006-04-11 | DOI: https://doi.org/10.1515/BC.2006.060

Abstract

Growth and differentiation factor 5 (GDF-5) is a homodimeric protein stabilized by a single disulfide bridge between cysteine 465 in the respective monomers, as well as by three intramolecular cysteine bridges within each subunit. A mature recombinant human GDF-5 variant with cysteine 465 replaced by alanine (rhGDF-5 C465A) was expressed in E. coli, purified to homogeneity, and chemically renatured. Biochemical analysis showed that this procedure eliminated the sole interchain disulfide bond. Surprisingly, the monomeric variant of rhGDF-5 is as potent in vitro as the dimeric form. This could be confirmed by alkaline phosphatase assays and Smad reporter gene activation. Furthermore, dimeric and monomeric rhGDF-5 show comparable binding to their specific type I receptor, BRIb. Studies on living cells showed that both the dimeric and monomeric rhGDF-5 induce homomeric BRIb and heteromeric BRIb/BRII oligomers. Our results suggest that rhGDF-5 C465A has the same biological activity as rhGDF-5 with respect to binding to, oligomerization of and signaling through the BMP receptor type Ib.

Keywords: BMP; BMP receptor; GDF-5; Smad signaling; TGF-β superfamily

About the article

Corresponding authors ;


Received: October 27, 2005

Accepted: January 25, 2006

Published Online: 2006-04-11

Published in Print: 2006-04-01


Citation Information: Biological Chemistry, Volume 387, Issue 4, Pages 451–460, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.060.

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