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Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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1437-4315
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Volume 389, Issue 2 (Feb 2008)

Issues

Insulin-releasing properties of the frog skin peptide pseudin-2 and its [Lys18]-substituted analogue

Yasser H.A. Abdel-Wahab
  • 1School of Biomedical Sciences, University of Ulster, Cromore Road, Coleraine BT52 1SA, UK
/ Gavin J. Power
  • 2School of Biomedical Sciences, University of Ulster, Cromore Road, Coleraine BT52 1SA, UK
/ Ming T. Ng
  • 3School of Biomedical Sciences, University of Ulster, Cromore Road, Coleraine BT52 1SA, UK
/ Peter R. Flatt
  • 4School of Biomedical Sciences, University of Ulster, Cromore Road, Coleraine BT52 1SA, UK
/ J. Michael Conlon
  • 5Department of Biochemistry, Faculty of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates
Published Online: 2008-01-28 | DOI: https://doi.org/10.1515/BC.2008.018

Abstract

Pseudin-2 is a cationic α-helical peptide that was first isolated from the skin of the paradoxical frog Pseudis paradoxa on the basis of its antimicrobial activity. We have investigated the insulin-releasing properties and cytotoxicity of the peptide, together with selected analogues with increased cationicity and hydrophobicity. At concentrations in the range 10-9–10-6 m, pseudin-2, and its [Lys18], [Phe8], and [d-Lys3,d-Lys10,d-Lys14] derivatives, stimulated insulin release from the BRIN-BD11 clonal β-cell line without increasing release of lactate dehydrogenase. The [Lys18] analogue was the most potent (46% increase in insulin release at 10-9 m) and the most effective (215% increase in insulin release at 10-6 m). The more cationic [Lys3,Lys10,Lys14] and [Lys3,Lys10,Lys14,Lys21] analogues lacked insulinotropic action and the more hydrophobic [Phe16] analogue was cytotoxic at concentrations ≥10-7 m. Pseudin-2 and [Lys18]-pseudin-2 had no effect on intracellular calcium concentrations and stimulated insulin release in the absence of external calcium. [Lys18]-pseudin-2 (10-8 m) stimulated insulin release in the presence of diazoxide and verapamil. Our results demonstrate that pseudin-2 stimulates insulin secretion from BRIN-BD11 cells by a mechanism involving Ca2+-independent pathways and identify [Lys18]-pseudin-2 as a peptide that may have potential for development as a therapeutically valuable insulinotropic agent for the treatment of type 2 diabetes.

Keywords: frog skin; insulin secretion; pseudin-2; type 2 diabetes

About the article

Corresponding author


Received: 2007-09-13

Accepted: 2007-10-30

Published Online: 2008-01-28

Published in Print: 2008-02-01



Citation Information: Biological Chemistry, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2008.018. Export Citation

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[1]
Dinesh Srinivasan, Opeolu O. Ojo, Bosede O. Owolabi, J. Michael Conlon, Peter R. Flatt, and Yasser H.A. Abdel-Wahab
European Journal of Pharmacology, 2015
[3]
Dinesh Srinivasan, Opeolu O. Ojo, Yasser H.A. Abdel-Wahab, Peter R. Flatt, Laure Guilhaudis, and J. Michael Conlon
Peptides, 2014, Volume 55, Page 23
[4]
Iain S. Haslam, Eric W. Roubos, Maria Luisa Mangoni, Katsutoshi Yoshizato, Hubert Vaudry, Jennifer E. Kloepper, David M. Pattwell, Paul F. A. Maderson, and Ralf Paus
Biological Reviews, 2014, Volume 89, Number 3, Page 618
[5]
Opeolu O. Ojo, Yasser H. A. Abdel-Wahab, Peter R. Flatt, and J. Michael Conlon
Chemical Biology & Drug Design, 2013, Volume 82, Number 2, Page 196
[6]
Dinesh Srinivasan, Milena Mechkarska, Yasser H.A. Abdel-Wahab, Peter R. Flatt, and J. Michael Conlon
Biochimie, 2013, Volume 95, Number 2, Page 429
[7]
O. O. Ojo, Y. H. A. Abdel-Wahab, P. R. Flatt, M. Mechkarska, and J. M. Conlon
Diabetes, Obesity and Metabolism, 2011, Volume 13, Number 12, Page 1114
[8]
J. Michael Conlon, Gavin J. Power, Yasser H.A. Abdel-Wahab, Peter R. Flatt, Hu Jiansheng, Laurent Coquet, Jérôme Leprince, Thierry Jouenne, and Hubert Vaudry
Regulatory Peptides, 2008, Volume 151, Number 1-3, Page 153
[9]
Seong-Cheol Park, Jin-Young Kim, Chanyoung Jeong, Suyeon Yoo, Kyung-Soo Hahm, and Yoonkyung Park
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2011, Volume 1808, Number 1, Page 171
[10]
J. Michael Conlon, Yasser H.A. Abdel-Wahab, Peter R. Flatt, Jérôme Leprince, Hubert Vaudry, Thierry Jouenne, and Eric Condamine
Peptides, 2009, Volume 30, Number 5, Page 888
[11]
Hyung-Sik Won, Su-Jin Kang, Wahn-Soo Choi, and Bong-Jin Lee
Molecules and Cells, 2011, Volume 31, Number 1, Page 49
[12]
Yao Xiao, Cunbao Liu, and Ren Lai
BioMolecular Concepts, 2011, Volume 2, Number 1-2

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