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

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 383, Issue 7-8 (Aug 2002)

Issues

Probing the Active Sites and Mechanisms of Rat Metalloproteases Meprin A and B

G. P. Bertenshaw / J. P. Villa / J. A. Hengst / J. S. Bond
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.129

Abstract

Meprin A and B are highly regulated, secreted and cellsurface homo and heterooligomeric enzymes. Meprins are abundantly expressed in kidney and intestine. The multidomain α and β subunits have high sequence identity, however they have very different substrate specificities, oligomerization potentials and are differentially regulated. Here we describe that meprin subunit activities are modulated differently by physicochemical factors. Homooligomeric meprin B had an acidic pH optimum. The low pH protonation indicated the existence of at least two ionizable groups. An additional ionizable group generated a shoulder in the basic pH range. Homooligomeric meprin A had a neutral pH optimum and the activity curve revealed that two ionizable groups might be protonated at acidic pH similar to meprin B. Increasing the concentration of salt generally inhibited meprin B activity. Meprin A was inhibited at low salt concentrations but activated as salt was increased. This work has important implications in the elucidation of the catalytic mechanisms of meprins and other metalloproteases. In addition, the activity of meprin oligomers that arise in tissues will be affected by variations in pH and NaCl. This could have profound implications because meprins are exposed to a range of conditions in the extracellular milieu of renal and intestinal tissues and in inflammation and cancer.

About the article

Published Online: 2005-06-01

Published in Print: 2002-08-27


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.129.

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.

[1]
Timothy R. Keiffer and Judith S. Bond
Journal of Biological Chemistry, 2014, Volume 289, Number 11, Page 7580
[2]
Sanjita Banerjee and Judith S. Bond
Journal of Biological Chemistry, 2008, Volume 283, Number 46, Page 31371
[3]
Faoud T. Ishmael, Vincent K. Shier, Susan S. Ishmael, and Judith S. Bond
Journal of Biological Chemistry, 2005, Volume 280, Number 14, Page 13895
[4]
Susan S. Ishmael, Faoud T. Ishmael, A. Daniel Jones, and Judith S. Bond
Journal of Biological Chemistry, 2006, Volume 281, Number 49, Page 37404
[5]
Greg P. Bertenshaw, Mona T. Norcum, and Judith S. Bond
Journal of Biological Chemistry, 2003, Volume 278, Number 4, Page 2522
[6]
James P. Villa, Greg P. Bertenshaw, and Judith S. Bond
Journal of Biological Chemistry, 2003, Volume 278, Number 43, Page 42545
[7]
Christian Herzog, Randy S. Haun, Sudhir V. Shah, and Gur P. Kaushal
Biochemistry and Biophysics Reports, 2016, Volume 8, Page 146
[8]
D. Schlenzig, M. Wermann, D. Ramsbeck, T. Moenke-Wedler, and S. Schilling
Protein Expression and Purification, 2015, Volume 116, Page 75
[9]
Jochen Hinkelbein, Lennert Böhm, Oliver Spelten, David Sander, Stefan Soltész, and Stefan Braunecker
Disease Markers, 2015, Volume 2015, Page 1
[10]
A. Schutte, A. Ermund, C. Becker-Pauly, M. E. V. Johansson, A. M. Rodriguez-Pineiro, F. Backhed, S. Muller, D. Lottaz, J. S. Bond, and G. C. Hansson
Proceedings of the National Academy of Sciences, 2014, Volume 111, Number 34, Page 12396
[12]
Christian Herzog, Randy S. Haun, Varsha Kaushal, Philip R. Mayeux, Sudhir V. Shah, and Gur P. Kaushal
Biochemical and Biophysical Research Communications, 2009, Volume 379, Number 4, Page 904
[13]
Pan Gao, Rui-wei Guo, Jian-fei Chen, Yang Chen, Hong Wang, Yang Yu, and Lan Huang
Atherosclerosis, 2009, Volume 207, Number 1, Page 84
[14]
John E. Bylander, Greg P. Bertenshaw, Gail L. Matters, Simon J. Hubbard, and Judith S. Bond
Biological Chemistry, 2007, Volume 388, Number 11
[15]
S Banerjee, B Oneda, L M Yap, D P Jewell, G L Matters, L R Fitzpatrick, F Seibold, E E Sterchi, T Ahmad, D Lottaz, and J S Bond
Mucosal Immunology, 2009, Volume 2, Number 3, Page 220
[16]
S. A. Semenova and G. N. Rudenskaya
Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry, 2009, Volume 3, Number 1, Page 17

Comments (0)

Please log in or register to comment.
Log in