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Glycobiology Advance Access originally published online on February 6, 2006
Glycobiology 2006 16(5):368-374; doi:10.1093/glycob/cwj084
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org.
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Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues—its possible role in prolonged stability in vivo by aberrant glycosylation

Yasuhiro Ito2, Ayumi Akinaga3, Kanako Yamanaka3, Takatoshi Nakagawa4,5, Akihiro Kondo4,5, Robert B. Dickson6, Chen-Yong Lin6, Akira Miyauchi2, Naoyuki Taniguchi3, and Eiji Miyoshi1,3,4

2 Department of Surgery, Kuma Hospital, 8-2-35 Shimoyamate-dori, Chuo-ku, Kobe 650-0011, Japan; 3 Department of Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka Suita, Osaka 565-0871, Japan; 4 CREST, JST, 4-1-8 Honcho Kawaguchi, Saitama, 332-0012, Japan; 5 Department of Glyco-therapeutics, Osaka University Graduate School of Medicine, 2-2 Yamadaoka Suita, Osaka 565-0871, Japan; 6 Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, 3970 Reservoir Road NW, Washington, DC 20057-1421

1 To whom correspondence should be addressed; e-mail: miyoshi34{at}biochem.med.osaka-u.ac.jp

Received on July 5, 2005; revised on January 23, 2006; accepted on January 27, 2006

UDP-N-acetylglucosamine:{alpha}-mannoside ß-1,6-N-acetylglucosaminyltransferase (GnT-V) catalyzes the formation of ß-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 ß-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. Although 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 posttranslational modification such as glycosylation through GnT-V-mediated glycosylation. In papillary carcinoma, the levels of expression of both GnT-V and matriptase were significantly higher in tumors 1 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 role in the early phases of papillary carcinoma, but not in its later phase progression.

Key words: GnT-V / growth factor / matriptase / thyroid cancer


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