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

See all formats and pricing
More options …
Volume 383, Issue 11 (Nov 2002)


Substrate Specificity and Inhibitor Studies of a Membrane-Bound Ganglioside Sialidase Isolated from Human Brain Tissue

C. Oehler / J. Kopitz / M. Cantz
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.194


A gangliosidespecific sialidase that controls cellular functions such as growth, differentiation, and adhesion has been observed in a variety of cells, but its characterization proved difficult due to firm membrane attachment and lability of the purified enzyme. Here we report on the specificity toward gangliosides and susceptibility to certain inhibitors of a ganglioside sialidase solubilized and purified 5100-fold from human brain. The sialidase removed terminal sialic acids from gangliosides GM3, GM4, GD3, GD2, GD1a, GD1b, GT1b and GQ1b, but was inactive toward gangliosides with sialic acid in a branching position (as in GM1 and GM2). LysoGM3 and GD1a were good substrates, too, whereas Oacetylation of the sialic acid as in 9-OacetylGD3 caused strongly reduced cleavage. The new influenza virus drug 4-guanidino-2-deoxy-2,3- dehydroNacetylneuraminic acid (Zanamivir) exhibited an IC50 value of about 710 5 M that was in the range of the classical sialidase inhibitor 2-deoxy-2,3-dehydro Nacetylneuraminic acid; the bacterial sialidase inhibitor 4-nitrophenyloxamic acid, however, was ineffective. The glycosaminoglycans heparan sulfate, heparin, chondroitin sulfates A and B, as well as dextran sulfate and suramin, were all strongly inhibitory, suggesting that glycosaminoglycans present on the cell surface or in the extracellular matrix may influence the ability of the sialidase to alter the ganglioside composition of the membrane.

About the article

Published Online: 2005-06-01

Published in Print: 2002-11-13

Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.194.

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.

Evelin Tiralongo, Silke Schrader, Hans Lange, Hilmar Lemke, Joe Tiralongo, and Roland Schauer
Journal of Biological Chemistry, 2003, Volume 278, Number 26, Page 23301
Benjamin Bailly, Larissa Dirr, Ibrahim M. El-Deeb, Ralf Altmeyer, Patrice Guillon, and Mark von Itzstein
Scientific Reports, 2016, Volume 6, Number 1
José Abad-Rodríguez and Natalia Díez-Revuelta
Trends in Biochemical Sciences, 2015, Volume 40, Number 7, Page 385
Sandro Sonnino, Massimo Aureli, Nicoletta Loberto, Vanna Chigorno, and Alessandro Prinetti
FEBS Letters, 2010, Volume 584, Number 9, Page 1914
Sadagopan Magesh, Tohru Suzuki, Taeko Miyagi, Hideharu Ishida, and Makoto Kiso
Journal of Molecular Graphics and Modelling, 2006, Volume 25, Number 2, Page 196
D. Wipfler, G. V. Srinivasan, H. Sadick, B. Kniep, S. Arming, M. Willhauck-Fleckenstein, R. Vlasak, R. Schauer, and R. Schwartz-Albiez
Glycobiology, 2011, Volume 21, Number 9, Page 1161
Yanhong Li, Hongzhi Cao, Hai Yu, Yi Chen, Kam Lau, Jingyao Qu, Vireak Thon, Go Sugiarto, and Xi Chen
Molecular BioSystems, 2011, Volume 7, Number 4, Page 1060
Alessandro Prinetti, Vanna Chigorno, Laura Mauri, Nicoletta Loberto, and Sandro Sonnino
Journal of Neurochemistry, 2007, Volume 103, Number s1, Page 113
Robert McGlynn, Kostantin Dobrenis, and Steven U. Walkley
The Journal of Comparative Neurology, 2004, Volume 480, Number 4, Page 415

Comments (0)

Please log in or register to comment.
Log in