Jump to ContentJump to Main Navigation
Show Summary Details
More options …

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

See all formats and pricing
More options …
Volume 392, Issue 3


Outside or inside: role of the subcellular localization of DP4-like enzymes for substrate conversion and inhibitor effects

Ute Bank / Anke Heimburg / Astrid Wohlfarth / Gudrun Koch / Karsten Nordhoff / Heiko Julius / Martin Helmuth / Doreen Breyer / Dirk Reinhold
  • Institute of Molecular and Clinical Immunology, Otto von Guericke University Magdeburg, D-39120 Magdeburg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Michael Täger / Siegfried Ansorge
Published Online: 2011-06-18 | DOI: https://doi.org/10.1515/bc.2011.025


The discovery of the DP4-related enzymes DP8 and DP9 raised controversial discussion regarding the physiological and pathophysiological function of distinct members of the DP4 family. Particularly with regard to their potential relevance in regulating immune functions, it is of interest to know which role the subcellular distribution of the enzymes play. Synthetic substrates as well as low molecular weight inhibitors are widely used as tools, but little is yet known regarding their features in cell experiments, such as their plasma membrane penetration capacity. The fluorogenic substrates Gly-Pro-AMC or (Ala-Pro)2-R110 predominantly detect plasma membrane-bound activities of viable cells (less than 0.1% of fluorochromes R110 or AMC inside viable cells after 1 h incubation). Additionally, the selective and non-selective DP8/9 inhibitors allo-Ile-isoindoline and Lys[Z(NO2)]-pyrrolidide were found to be incapable of passing the plasma membrane easily. This suggests that previously reported cellular effects are not due to inhibition of the cytosolic enzymes DP8 or DP9. Moreover, our enzymatic studies with viable cells provided evidence that DP8 and/or DP9 are also present on the surface of immune cells under certain circumstances and could gain relevance particularly in the absence of DP4 expression. In summary, in cells which do express DP4 on the surface, this archetypical member of the DP4 family is the most relevant peptidase in the regulation of cellular functions.

Keywords: CD26; dipeptidyl peptidase; inhibitors; lymphocytes; neuropeptide Y (NPY); substrates

About the article

Corresponding author

Received: 2010-07-05

Accepted: 2010-12-01

Published Online: 2011-06-18

Published in Print: 2011-03-01

Citation Information: Biological Chemistry, Volume 392, Issue 3, Pages 169–187, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2011.025.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Erin E. Mulvihill and Daniel J. Drucker
Endocrine Reviews, 2014, Volume 35, Number 6, Page 992
Munkyung Kim, Lilly von Muenchow, Thomas Le Meur, Benjamin Kueng, Berangere Gapp, Delphine Weber, William Dietrich, Jiri Kovarik, Antonius G. Rolink, and Iwona Ksiazek
Immunology Letters, 2018
Suncica Buljevic, Dijana Detel, Ester P. Pugel, and Jadranka Varljen
Journal of Cellular Biochemistry, 2018
Sumaiya Chowdhury, Yiqian Chen, Tsun-Wen Yao, Katerina Ajami, Xin M Wang, Yury Popov, Detlef Schuppan, Patrick Bertolino, Geoffrey W McCaughan, Denise MT Yu, and Mark D Gorrell
World Journal of Gastroenterology, 2013, Volume 19, Number 19, Page 2883
International Journal of Oncology, 2012, Volume 41, Number 3, Page 919
S. R. Quist, A. Heimburg, U. Bank, D. Mahnkopf, G. Koch, H. Gollnick, M. Täger, and S. Ansorge
Clinical and Experimental Dermatology, 2017, Volume 42, Number 6, Page 607
Emilija Zapletal, Barbara Cupic, and Jelka Gabrilovac
Cell Biochemistry and Function, 2017, Volume 35, Number 2, Page 124
Jelka Gabrilovac, Barbara Čupić, Emilija Zapletal, Ognjen Kraus, and Jasminka Jakić-Razumović
Immunobiology, 2017, Volume 222, Number 2, Page 327
L. Wagner, C. Klemann, M. Stephan, and S. von Hörsten
Clinical & Experimental Immunology, 2016, Volume 184, Number 3, Page 265
Hui Zhang, Yiqian Chen, Carol Wadham, Geoffrey W. McCaughan, Fiona M. Keane, and Mark D. Gorrell
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2015, Volume 1853, Number 2, Page 470
Adam Rainczuk, Jyothsna R. Rao, Jessica L. Gathercole, Nicole J. Fairweather, Simon Chu, Rina Masadah, Thomas W. Jobling, Santanu Deb-Choudhury, Jolon Dyer, and Andrew N. Stephens
International Journal of Cancer, 2014, Volume 134, Number 3, Page 530
Petr Busek, Jarmila Stremenova, Lucie Sromova, Marek Hilser, Eva Balaziova, Dalibor Kosek, Jana Trylcova, Hynek Strnad, Evzen Krepela, and Aleksi Sedo
The International Journal of Biochemistry & Cell Biology, 2012, Volume 44, Number 5, Page 738
Torsten Hoffmann and Hans-Ulrich Demuth
Biological Chemistry, 2011, Volume 392, Number 3

Comments (0)

Please log in or register to comment.
Log in