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Molecular characterization of a germ-cell-specific antigen, TEX101, from mouse testis

Published online by Cambridge University Press:  01 August 2006

Hong Jin
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan. Department of Obstetrics & Gynecology, Juntendo University Faculty of Medicine, Tokyo 113-8595, Japan.
Hiroshi Yoshitake
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan.
Hiroki Tsukamoto
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan.
Mai Takahashi
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan.
Miki Mori
Affiliation:
Department of Molecular Anatomy, Nippon Medical School, Tokyo 113-8602, Japan.
Toshihiro Takizawa
Affiliation:
Department of Molecular Anatomy, Nippon Medical School, Tokyo 113-8602, Japan.
Kenji Takamori
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan.
Hideoki Ogawa
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan.
Katsuyuki Kinoshita
Affiliation:
Department of Obstetrics & Gynecology, Juntendo University Faculty of Medicine, Tokyo 113-8595, Japan.
Yoshihiko Araki*
Affiliation:
Institute for Environmental & Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba 279-0021, Japan.
*
All correspondence to: Yoshihiko Araki, MD, DMedSci, Institute for Environmental and Gender-Specific Medicine, Juntendo University Graduate School of Medicine, 2-1-1 Tomioka, Urayasu-City, Chiba 279-0021, Japan. Fax: +81 47 3533178. e-mail: yaraki@med.juntendo.ac.jp

Summary

TEX101, a glycoprotein we recently identified, is primarily characterized as a unique germ-cell-specific marker protein that shows sexually dimorphic expression during mouse gonad development. Based on data obtained from molecular biological as well as immuno-morphological studies, we believe this molecule may play a role in the process underlying germ cell formation. However, many points remain unclear as the molecular characteristics and its physiological functions are far from being completely understood. To clarify the molecular basis of TEX101, we herein report a further biochemical characterization of the molecule using testicular Triton X-100 extracts from mice. Deglycosylation studies using endoglycohydrolases that delete N-linked oligosaccharides (OS) from the molecule show that TEX101 is highly (approximately 47%) N-glycosylated. All potential N-glycosylation sites within TEX101 are glycosylated and most of these sites are occupied by endoglycosidase F2-sensitive biantennary complex type OS units. In addition, an extremely low population among TEX101 possesses only endoglycosidase H-sensitive hybrid type OS units. In studies using phosphatidylinositol-specific phospholipase C against native testicular cells or TEX101 transfectant, the enzyme treatment caused major reduction of the TEX101 expression on the cell, suggesting that TEX101, at least in part, is expressed as a glycosylphosphatidylinositol-anchored protein. Taken together, these findings will help elucidate the molecular nature of TEX101, a marker molecule that appeared on germ cells during gametogenesis.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2006

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