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Glycobiology Advance Access published online on February 6, 2006
Glycobiology, doi:10.1093/glycob/cwj084
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© The Author 2006. Published by Oxford University Press. All rights reserved. The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org
Received July 5, 2005
Revised January 23, 2006
Accepted January 27, 2006

Article

Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues; its possible role in prolonged stability in vivo by aberrant glycosylation

Yasuhiro Ito 1, Ayumi Akinaga 2, Kanako Yamanaka 2, Takatoshi Nakagawa 3, Akihiro Kondo 3, Robert B. Dickson 4, Chen-Yong Lin 4, Akira Miyauchi 1, Naoyuki Taniguchi 2, and Eiji Miyoshi 5 *

1 Department of Surgery, Kuma Hospital
2 Department of Biochemistry, Osaka University Graduate School of Medicine
3 CREST; Department of Glyco-therapeutics, Osaka University Graduate School of Medicine
4 Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center
5 Department of Biochemistry, Osaka University Graduate School of Medicine, Japan; CREST

* To whom correspondence should be addressed.
Eiji Miyoshi, E-mail: miyoshi34{at}biochem.med.osaka-u.ac.jp


  Abstract

UDP-N-acetylglucosamine: alpha-mannoside beta 1,6 N-acetylglucosaminyl-transferase (GnT-V) catalyzes the formation of beta 1-6 GlcNAc branches on asparagine-linked oligosaccharides, which is directly linked to tumorigenesis. Our recent studies indicate that the secretion of matriptase from cancer cells is increased via the action of GnT-V, as evidenced by the fact that matriptase bearing beta 1-6 GlcNAc branching is dramatically inhibited. In this study, we report on an investigation of the expression of GnT-V and matriptase in thyroid neoplasm tissues to determine the clinical significance on the co-expression of these two proteins in thyroid cancer. While neither GnT-V nor matriptase was expressed in normal thyroid tissue, positive staining for matriptase and GnT-V was observed in 52/68 and 66/68 cases of papillary carcinoma, 3/23 and 10/23 cases of follicular carcinoma, 5/13 and 9/13 cases of follicular adenoma, and 11/28 and 6/28 cases of anaplastic carcinoma, respectively. Immunohistochemistry, as well as western blotting, showed that the expression of matriptase paralleled the expression to GnT-V. However, the expression of matriptase mRNA was not correlated with its protein levels, suggesting that the enhancement in matriptase expression could be regulated by a post-translational modification such as glycosylation through GnT-V-mediated glycosylation. In the case of papillary carcinoma, the levels of expression of both GnT-V and matriptase were significantly higher in tumors1 cm or less in size (microcarcinoma) and in those without poorly differentiated lesions, and the two proteins were significantly correlated. In contrast, the prognosis of thyroid carcinoma after surgery was neither correlated with the expression GnT-V nor matriptase, because the levels of their expression were quite low in anaplastic (undifferentiated) carcinomas. These results suggest that prolonged stabilization of matriptase is stabilized by GnT-V-mediated glycosylation in vivo thus extending its halftime and permitting it to play a role in the early phases of papillary carcinoma, but not in its later phase progression.

Keywords: GnT-V/matriptase/thyroid cancer/growth factor.
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