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Journal of Biochemistry Advance Access first published online on July 16, 2008
This version published online on August 5, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn089
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© 2008 The Japanese Biochemical Society

JB Minireview

Plasma membane-associated sialidase as a crucial regulator of transmenbrane signaling

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

Corresponding author: Dr. Taeko Miyagi. Division of Biochemistry, Miyagi Cancer Center Research Institute, 47-1, Nodayama, Medeshima-shiode, Natori, Miyagi, 981-1293, Japan. 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 an especial substrate preference. This sialidase has been shown to control transmembrane signaling for many cellular processes, including cell differentiation, cell growth and apoptosis, and human ortholog 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-insulinemia 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 signaling.

Key Words: Cancer, Diabetes, Gangliosides, Sialidase, Transmembrane signaling


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