Skip Navigation


Journal of Biochemistry Advance Access originally published online on July 16, 2008
Journal of Biochemistry 2008 144(3):279-285; doi:10.1093/jb/mvn089
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
144/3/279    most recent
mvn089v4
mvn089v3
mvn089v2
mvn089v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Miyagi, T.
Right arrow Articles by Shiozaki, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miyagi, T.
Right arrow Articles by Shiozaki, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Japanese Biochemical Society

JB Minireviews-New Paradigm in Glycobiology

Plasma Membrane-associated Sialidase as a Crucial Regulator of Transmembrane Signalling

Taeko Miyagi*, Tadashi Wada, Kazunori Yamaguchi, Keiko Hata and Kazuhiro Shiozaki

Division of Biochemistry, Miyagi Cancer Center Research Institute, Natori, 981-1293, and CREST, JST, Japan

*To whom correspondence should be addressed. Tel: +81-22-384-3151, Fax: +81-22-381-1195, E-mail: miyagi-ta173{at}pref.miyagi.jp

Received May 6, 2008; Accepted June 30, 2008


  Abstract

Mammalian sialidases, glycosidases responsible for the removal of sialic acids from glycoproteins and glycolipids, has been implicated to participate in many biological processes as well as in lysosomal catabolism. Among those forms identified to date, plasma membrane-associated sialidase, Neu3, is a key enzyme in degradation of gangliosides, for which it exhibits a special substrate preference. This sialidase has been shown to control transmembrane signalling for many cellular processes, including cell differentiation, cell growth and apoptosis, and human orthologue NEU3 is markedly up-regulated in various cancers. It is known to suppress apoptosis in cancer cells. Furthermore, its overexpression causes impaired glucose tolerance and hyper-insulinaemia together with overproduction of insulin in enlarged islets in the transgenic mice. The present review primarily summarizes our recent results, focusing on Neu3 as a regulator of transmembrane signalling.

Key Words: cancer, diabetes, gangliosides, sialidase, transmembrane signalling

Abbreviations: EGFR, epidermal growth factor receptor; ERK, extracellular signal-related kinase; FAK, focal adhesion kinase; IR, insulin receptor; IRS-1, insulin receptor substrate I; LacCer, lactosylceramide


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Lipid Res.Home page
R. K. Yu, Y. Nakatani, and M. Yanagisawa
The role of glycosphingolipid metabolism in the developing brain
J. Lipid Res., April 1, 2009; 50(Supplement): S440 - S445.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Anastasia, N. Papini, F. Colazzo, G. Palazzolo, C. Tringali, L. Dileo, M. Piccoli, E. Conforti, C. Sitzia, E. Monti, et al.
NEU3 Sialidase Strictly Modulates GM3 Levels in Skeletal Myoblasts C2C12 Thus Favoring Their Differentiation and Protecting Them from Apoptosis
J. Biol. Chem., December 26, 2008; 283(52): 36265 - 36271.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.