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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

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Source Normalized Impact per Paper (SNIP) 2017: 0.705

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Volume 398, Issue 3


A role for the metalloprotease invadolysin in insulin signaling and adipogenesis

Ching-Wen Chang
  • University of Edinburgh, Queen’s Medical Research Institute, University/BHF Center for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
  • Other articles by this author:
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/ Kanishk Abhinav
  • University of Edinburgh, Queen’s Medical Research Institute, University/BHF Center for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Francesca Di Cara
  • University of Edinburgh, Queen’s Medical Research Institute, University/BHF Center for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
  • Other articles by this author:
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/ Ioanna Panagakou
  • University of Edinburgh, Queen’s Medical Research Institute, University/BHF Center for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
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/ Sharron Vass
  • University of Edinburgh, Queen’s Medical Research Institute, University/BHF Center for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
  • Other articles by this author:
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/ Margarete M.S. Heck
  • Corresponding author
  • University of Edinburgh, Queen’s Medical Research Institute, University/BHF Center for Cardiovascular Science, 47 Little France Crescent, Edinburgh EH16 4TJ, UK
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Published Online: 2016-09-13 | DOI: https://doi.org/10.1515/hsz-2016-0226


Invadolysin is a novel metalloprotease conserved amongst metazoans that is essential for life in Drosophila. We previously showed that invadolysin was essential for the cell cycle and cell migration, linking to metabolism through a role in lipid storage and interaction with mitochondrial proteins. In this study we demonstrate that invadolysin mutants exhibit increased autophagy and decreased glycogen storage – suggestive of a role for invadolysin in insulin signaling in Drosophila. Consistent with this, effectors of insulin signaling were decreased in invadolysin mutants. In addition, we discovered that invadolysin was deposited on newly synthesized lipid droplets in a PKC-dependent manner. We examined two in vitro models of adipogenesis for the expression and localization of invadolysin. The level of invadolysin increased during both murine 3T3-L1 and human Simpson-Golabi-Behmel syndrome (SGBS), adipogenesis. Invadolysin displayed a dynamic localization to lipid droplets over the course of adipogenesis, which may be due to the differential expression of distinct invadolysin variants. Pharmacological inhibition of adipogenesis abrogated the increase in invadolysin. In summary, our results on in vivo and in vitro systems highlight an important role for invadolysin in insulin signaling and adipogenesis.

This article offers supplementary material which is provided at the end of the article.

Keywords: adipogenesis; insulin signaling; lipid droplets; metalloprotease


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About the article

aChing-Wen Chang and Kanishk Abhinav: These authors contributed equally to this work.

bPresent address: Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan.

cPresent address: Department of Cell Biology, Faculty of Medicine, University of Alberta, Edmonton T6G 2H7, Canada.

dPresent address: Edinburgh Napier University, Sighthill Court, Edinburgh EH11 4BN, UK.

Received: 2016-06-08

Accepted: 2016-09-04

Published Online: 2016-09-13

Published in Print: 2017-03-01

Citation Information: Biological Chemistry, Volume 398, Issue 3, Pages 373–393, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2016-0226.

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